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Conserved domains on  [gi|26006861|ref|NP_742146|]
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pyridoxal kinase [Mus musculus]

Protein Classification

carbohydrate kinase family protein( domain architecture ID 399)

carbohydrate kinase family protein that accepts a wide variety of substrates, including carbohydrates and aromatic small molecules, all being phosphorylated at a hydroxyl group; belongs to the ribokinase/pfkB sugar kinase superfamily

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ribokinase_pfkB_like super family cl00192
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ...
 6-304 6.67e-151

ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including carbohydrates and aromatic small molecules, all are phosphorylated at a hydroxyl group. The superfamily includes ribokinase, fructokinase, ketohexokinase, 2-dehydro-3-deoxygluconokinase, 1-phosphofructokinase, the minor 6-phosphofructokinase (PfkB), inosine-guanosine kinase, and adenosine kinase. Even though there is a high degree of structural conservation within this superfamily, their multimerization level varies widely, monomeric (e.g. adenosine kinase), dimeric (e.g. ribokinase), and trimeric (e.g THZ kinase).


The actual alignment was detected with superfamily member TIGR00687:

Pssm-ID: 469648 [Multi-domain]  Cd Length: 287  Bit Score: 424.63  E-value: 6.67e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26006861     6 RVLSIQSHVVRGYVGNRAAMFPLQVLGFEVDAVNSVQFSNHTGYAHWKGQVLKSQELHELYEGL-KVNDVNKYDYVLTGY 84
Cdd:TIGR00687   3 NVLSIQSHVVYGHVGNRAATFPLQRLGFEVWAVNTVQFSNHTGYGKWTGQVLPPDELHELVEGLeAINKLNQCDAVLSGY 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26006861    85 TRDKSFLAMVVDIVRELKQQNSRLVYVCDPVMGDKWNGegsMYVPQDLLPVYRDKVVPVADIITPNQFEAELLSGRKIHS 164
Cdd:TIGR00687  83 LGSAEQVAMVVGIVRQVKQANPQALYVCDPVMGDPWKG---CYVAPDLLEVYREKAIPVADIITPNQFELELLTGRRINT 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26006861   165 QEEAFEVMDMLHCMGPDTVVITssdlpssqgsdYLIALGSQRMRKPDGSTVTQRIRMEMRKVEAVF----VGTGDLFAAM 240
Cdd:TIGR00687 160 EEEALAAADALIAMGPDIVLVT-----------HLIRAGSQRDRSFEGLVATQEGRWHISRPLAVFdpppVGTGDLIAAL 228

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 26006861   241 LLAwTHKHPDNLKVACEKTVSAMQHVLQRTIRCAKAEAgegqKPSPAQLELRMVQSKRDIEDPE 304
Cdd:TIGR00687 229 LLA-TLLHGNSLKEALEKTVSAVYHVLRTTIQLGKYEL----QPVAAQLEIRMPQSKFDAEKVE 287
 
Name Accession Description Interval E-value
pyridox_kin TIGR00687
pyridoxal kinase; E. coli has an enzyme PdxK that acts in vitro as a pyridoxine/pyridoxal ...
 6-304 6.67e-151

pyridoxal kinase; E. coli has an enzyme PdxK that acts in vitro as a pyridoxine/pyridoxal/pyridoxamine kinase, but mutants lacking PdxK activity retain a specific pyridoxal kinase, PdxY. PdxY acts in the salvage pathway of pyridoxal 5'-phosphate biosynthesis. Mammalian forms of pyridoxal kinase are more similar to PdxY than to PdxK. The PdxK isozyme is omitted from the seed alignment but scores above the trusted cutoff.ThiD and related proteins form an outgroup. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridoxine]


Pssm-ID: 273221 [Multi-domain]  Cd Length: 287  Bit Score: 424.63  E-value: 6.67e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26006861     6 RVLSIQSHVVRGYVGNRAAMFPLQVLGFEVDAVNSVQFSNHTGYAHWKGQVLKSQELHELYEGL-KVNDVNKYDYVLTGY 84
Cdd:TIGR00687   3 NVLSIQSHVVYGHVGNRAATFPLQRLGFEVWAVNTVQFSNHTGYGKWTGQVLPPDELHELVEGLeAINKLNQCDAVLSGY 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26006861    85 TRDKSFLAMVVDIVRELKQQNSRLVYVCDPVMGDKWNGegsMYVPQDLLPVYRDKVVPVADIITPNQFEAELLSGRKIHS 164
Cdd:TIGR00687  83 LGSAEQVAMVVGIVRQVKQANPQALYVCDPVMGDPWKG---CYVAPDLLEVYREKAIPVADIITPNQFELELLTGRRINT 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26006861   165 QEEAFEVMDMLHCMGPDTVVITssdlpssqgsdYLIALGSQRMRKPDGSTVTQRIRMEMRKVEAVF----VGTGDLFAAM 240
Cdd:TIGR00687 160 EEEALAAADALIAMGPDIVLVT-----------HLIRAGSQRDRSFEGLVATQEGRWHISRPLAVFdpppVGTGDLIAAL 228

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 26006861   241 LLAwTHKHPDNLKVACEKTVSAMQHVLQRTIRCAKAEAgegqKPSPAQLELRMVQSKRDIEDPE 304
Cdd:TIGR00687 229 LLA-TLLHGNSLKEALEKTVSAVYHVLRTTIQLGKYEL----QPVAAQLEIRMPQSKFDAEKVE 287
PLN02978 PLN02978
pyridoxal kinase
 6-310 3.50e-140

pyridoxal kinase


Pssm-ID: 215529 [Multi-domain]  Cd Length: 308  Bit Score: 398.34  E-value: 3.50e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26006861    6 RVLSIQSHVVRGYVGNRAAMFPLQVLGFEVDAVNSVQFSNHTGYAHWKGQVLKSQELHELYEGLKVNDVNKYDYVLTGYT 85
Cdd:PLN02978  16 RVLSIQSHTVHGYVGNKSAVFPLQLLGFDVDPINSVQFSNHTGYPTFKGQVLDGEQLWALIEGLEANGLLFYTHLLTGYI 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26006861   86 RDKSFLAMVVDIVRELKQQNSRLVYVCDPVMGDkwngEGSMYVPQDLLPVYRDKVVPVADIITPNQFEAELLSGRKIHSQ 165
Cdd:PLN02978  96 GSVSFLRTVLRVVKKLRSVNPNLTYVCDPVLGD----EGKLYVPPELVPVYREKVVPLATMLTPNQFEAEQLTGIRIVTE 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26006861  166 EEAFEVMDMLHCMGPDTVVITSSDLPSSqgsdyLIALGSQrmRKPDGSTVTQrIRMEMRKVEAVFVGTGDLFAAMLLAWT 245
Cdd:PLN02978 172 EDAREACAILHAAGPSKVVITSIDIDGK-----LLLVGSH--RKEKGARPEQ-FKIVIPKIPAYFTGTGDLMAALLLGWS 243

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 26006861  246 HKHPDNLKVACEKTVSAMQHVLQRTIRCAKAeagEGQKPSPAQLELRMVQSKRDIEDPEIVVQAT 310
Cdd:PLN02978 244 HKYPDNLDKAAELAVSSLQAVLRRTLADYKR---AGADPKSSSLELRLVQSQDDIRHPQVRFKAE 305
pyridoxal_pyridoxamine_kinase cd01173
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ...
 6-272 4.43e-116

Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5'-phosphate (PLP), by catalyzing the phosphorylation of the precursor vitamin B6 in the presence of Zn2+ and ATP. Mammals are unable to synthesize PLP de novo and require its precursors in the form of vitamin B6 (pyridoxal, pyridoxine, and pyridoxamine) from their diet. Pyridoxal kinase encoding genes are also found in many other species including yeast and bacteria.


Pssm-ID: 238578 [Multi-domain]  Cd Length: 254  Bit Score: 334.94  E-value: 4.43e-116
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26006861   6 RVLSIQSHVVRGYVGNRAAMFPLQVLGFEVDAVNSVQFSNHTGYAHWKGQVLKSQELHELYEGLKVNDV-NKYDYVLTGY 84
Cdd:cd01173   1 RVLSIQSHVVHGYVGNSAAVFPLQRLGWDVDALPTVQFSNHTGYGTWTGFVLSAEELEDLLEGLEALGLlLEYDAVLTGY 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26006861  85 TRDKSFLAMVVDIVRELKQQNSRLVYVCDPVMGDkwNGEGsMYVPQDLLPVYRDKVVPVADIITPNQFEAELLSGRKIHS 164
Cdd:cd01173  81 LGSAEQVEAVAEIVKRLKEKNPNLLYVCDPVMGD--NGKL-YVVAEEIVPVYRDLLVPLADIITPNQFELELLTGKKIND 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26006861 165 QEEAFEVMDMLHCMGPDTVVITSSDLPssqGSDYLIALGSQRMRkpdgstvTQRIRMEMRKVEAVFVGTGDLFAAMLLAW 244
Cdd:cd01173 158 LEDAKAAARALHAKGPKTVVVTSVELA---DDDRIEMLGSTATE-------AWLVQRPKIPFPAYFNGTGDLFAALLLAR 227

                       250       260
                ....*....|....*....|....*...
gi 26006861 245 THKHPDnLKVACEKTVSAMQHVLQRTIR 272
Cdd:cd01173 228 LLKGKS-LAEALEKALNFVHEVLEATYE 254
PdxK COG2240
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal ...
 6-272 4.74e-86

Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal/pyridoxine/pyridoxamine kinase is part of the Pathway/BioSystem: Pyridoxal phosphate biosynthesis


Pssm-ID: 441841 [Multi-domain]  Cd Length: 272  Bit Score: 259.31  E-value: 4.74e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26006861   6 RVLSIQSHVVRGYVGNRAAMFPLQVLGFEVDAVNSVQFSNHTGYAHWKGQVLKSQELHELYEGLKVNDVN-KYDYVLTGY 84
Cdd:COG2240   3 RVLSIQSHVVYGHVGNSAAVPPLSALGVEVWPLPTVLLSNHTGYGTFTGRDLPTDDIADILDGWKELGVLlEFDAVLSGY 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26006861  85 TRDKSFLAMVVDIVRELKQQNSRLVYVCDPVMGDkwNGEGsMYVPQDLLPVYRDKVVPVADIITPNQFEAELLSGRKIHS 164
Cdd:COG2240  83 LGSAEQGDIIADFVARVKAANPDALYLCDPVMGD--NGKG-YYVFPGIAEFIMRRLVPLADIITPNLTELALLTGRPYET 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26006861 165 QEEAFEVMDMLHCMGPDTVVITSsdLPSSQGSDYLIA-LGSQRmrkpDGSTVTQRirmemRKVEAVFVGTGDLFAAMLLA 243
Cdd:COG2240 160 LEEALAAARALLALGPKIVVVTS--VPLDDTPADKIGnLAVTA----DGAWLVET-----PLLPFSPNGTGDLFAALLLA 228

                       250       260
                ....*....|....*....|....*....
gi 26006861 244 WTHKHpDNLKVACEKTVSAMQHVLQRTIR 272
Cdd:COG2240 229 HLLRG-KSLEEALERAAAFVYEVLERTAA 256
Phos_pyr_kin pfam08543
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ...
 97-201 8.57e-15

Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate (TPP) synthesis pathway, TPP is an essential cofactor for many enzymes.


Pssm-ID: 430062 [Multi-domain]  Cd Length: 246  Bit Score: 72.51  E-value: 8.57e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26006861    97 IVRELKQQNSRLVyvCDPVMGDKwngEGSMYVPQDLLPVYRDKVVPVADIITPNQFEAELLSGRKIHSQEEAFEVMDMLH 176
Cdd:pfam08543  78 VAEKLDKYGVPVV--LDPVMVAK---SGDSLLDDEAIEALKEELLPLATLITPNLPEAEALTGRKIKTLEDMKEAAKKLL 152

                          90       100
                  ....*....|....*....|....*..
gi 26006861   177 CMGPDTVVITSSDLPSSQG--SDYLIA 201
Cdd:pfam08543 153 ALGAKAVLIKGGHLEGEEAvvTDVLYD 179
 
Name Accession Description Interval E-value
pyridox_kin TIGR00687
pyridoxal kinase; E. coli has an enzyme PdxK that acts in vitro as a pyridoxine/pyridoxal ...
 6-304 6.67e-151

pyridoxal kinase; E. coli has an enzyme PdxK that acts in vitro as a pyridoxine/pyridoxal/pyridoxamine kinase, but mutants lacking PdxK activity retain a specific pyridoxal kinase, PdxY. PdxY acts in the salvage pathway of pyridoxal 5'-phosphate biosynthesis. Mammalian forms of pyridoxal kinase are more similar to PdxY than to PdxK. The PdxK isozyme is omitted from the seed alignment but scores above the trusted cutoff.ThiD and related proteins form an outgroup. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridoxine]


Pssm-ID: 273221 [Multi-domain]  Cd Length: 287  Bit Score: 424.63  E-value: 6.67e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26006861     6 RVLSIQSHVVRGYVGNRAAMFPLQVLGFEVDAVNSVQFSNHTGYAHWKGQVLKSQELHELYEGL-KVNDVNKYDYVLTGY 84
Cdd:TIGR00687   3 NVLSIQSHVVYGHVGNRAATFPLQRLGFEVWAVNTVQFSNHTGYGKWTGQVLPPDELHELVEGLeAINKLNQCDAVLSGY 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26006861    85 TRDKSFLAMVVDIVRELKQQNSRLVYVCDPVMGDKWNGegsMYVPQDLLPVYRDKVVPVADIITPNQFEAELLSGRKIHS 164
Cdd:TIGR00687  83 LGSAEQVAMVVGIVRQVKQANPQALYVCDPVMGDPWKG---CYVAPDLLEVYREKAIPVADIITPNQFELELLTGRRINT 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26006861   165 QEEAFEVMDMLHCMGPDTVVITssdlpssqgsdYLIALGSQRMRKPDGSTVTQRIRMEMRKVEAVF----VGTGDLFAAM 240
Cdd:TIGR00687 160 EEEALAAADALIAMGPDIVLVT-----------HLIRAGSQRDRSFEGLVATQEGRWHISRPLAVFdpppVGTGDLIAAL 228

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 26006861   241 LLAwTHKHPDNLKVACEKTVSAMQHVLQRTIRCAKAEAgegqKPSPAQLELRMVQSKRDIEDPE 304
Cdd:TIGR00687 229 LLA-TLLHGNSLKEALEKTVSAVYHVLRTTIQLGKYEL----QPVAAQLEIRMPQSKFDAEKVE 287
PLN02978 PLN02978
pyridoxal kinase
 6-310 3.50e-140

pyridoxal kinase


Pssm-ID: 215529 [Multi-domain]  Cd Length: 308  Bit Score: 398.34  E-value: 3.50e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26006861    6 RVLSIQSHVVRGYVGNRAAMFPLQVLGFEVDAVNSVQFSNHTGYAHWKGQVLKSQELHELYEGLKVNDVNKYDYVLTGYT 85
Cdd:PLN02978  16 RVLSIQSHTVHGYVGNKSAVFPLQLLGFDVDPINSVQFSNHTGYPTFKGQVLDGEQLWALIEGLEANGLLFYTHLLTGYI 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26006861   86 RDKSFLAMVVDIVRELKQQNSRLVYVCDPVMGDkwngEGSMYVPQDLLPVYRDKVVPVADIITPNQFEAELLSGRKIHSQ 165
Cdd:PLN02978  96 GSVSFLRTVLRVVKKLRSVNPNLTYVCDPVLGD----EGKLYVPPELVPVYREKVVPLATMLTPNQFEAEQLTGIRIVTE 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26006861  166 EEAFEVMDMLHCMGPDTVVITSSDLPSSqgsdyLIALGSQrmRKPDGSTVTQrIRMEMRKVEAVFVGTGDLFAAMLLAWT 245
Cdd:PLN02978 172 EDAREACAILHAAGPSKVVITSIDIDGK-----LLLVGSH--RKEKGARPEQ-FKIVIPKIPAYFTGTGDLMAALLLGWS 243

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 26006861  246 HKHPDNLKVACEKTVSAMQHVLQRTIRCAKAeagEGQKPSPAQLELRMVQSKRDIEDPEIVVQAT 310
Cdd:PLN02978 244 HKYPDNLDKAAELAVSSLQAVLRRTLADYKR---AGADPKSSSLELRLVQSQDDIRHPQVRFKAE 305
PTZ00344 PTZ00344
pyridoxal kinase; Provisional
 1-312 1.13e-122

pyridoxal kinase; Provisional


Pssm-ID: 240372 [Multi-domain]  Cd Length: 296  Bit Score: 353.23  E-value: 1.13e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26006861    1 MEGECRVLSIQSHVVRGYVGNRAAMFPLQVLGFEVDAVNSVQFSNHTGYAHWKGQVLKSQELHELYEGLKVNDV-NKYDY 79
Cdd:PTZ00344   1 MSMEKKVLSIQSHVTHGYVGNRAATFPLQLLGFDVDFVNTVQLSNHTGYPVIKGHRLDLNELITLMDGLRANNLlSDYTY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26006861   80 VLTGYTRDKSFLAMVVDIVRELKQQNSRLVYVCDPVMGDkwngEGSMYVPQDLLPVYRdKVVPVADIITPNQFEAELLSG 159
Cdd:PTZ00344  81 VLTGYINSADILREVLATVKEIKELRPKLIFLCDPVMGD----DGKLYVKEEVVDAYR-ELIPYADVITPNQFEASLLSG 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26006861  160 RKIHSQEEAFEVMDMLHCMGPDTVVITSSDLPssQGSDYLIALGSQRmRKPDGStvTQRIRMEMRKVEAVFVGTGDLFAA 239
Cdd:PTZ00344 156 VEVKDLSDALEAIDWFHEQGIPVVVITSFRED--EDPTHLRFLLSCR-DKDTKN--NKRFTGKVPYIEGRYTGTGDLFAA 230

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 26006861  240 MLLAWTHKHPdnLKVACEKTVSAMQHVLQRTIrcakaEAGEGQKPSPAQLELRMVQSKRDIEDPEIVVQATVL 312
Cdd:PTZ00344 231 LLLAFSHQHP--MDLAVGKAMGVLQDIIKATR-----ESGGSGSSSLMSRELRLIQSPRDLLNPETVFKVTPL 296
pyridoxal_pyridoxamine_kinase cd01173
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ...
 6-272 4.43e-116

Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5'-phosphate (PLP), by catalyzing the phosphorylation of the precursor vitamin B6 in the presence of Zn2+ and ATP. Mammals are unable to synthesize PLP de novo and require its precursors in the form of vitamin B6 (pyridoxal, pyridoxine, and pyridoxamine) from their diet. Pyridoxal kinase encoding genes are also found in many other species including yeast and bacteria.


Pssm-ID: 238578 [Multi-domain]  Cd Length: 254  Bit Score: 334.94  E-value: 4.43e-116
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26006861   6 RVLSIQSHVVRGYVGNRAAMFPLQVLGFEVDAVNSVQFSNHTGYAHWKGQVLKSQELHELYEGLKVNDV-NKYDYVLTGY 84
Cdd:cd01173   1 RVLSIQSHVVHGYVGNSAAVFPLQRLGWDVDALPTVQFSNHTGYGTWTGFVLSAEELEDLLEGLEALGLlLEYDAVLTGY 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26006861  85 TRDKSFLAMVVDIVRELKQQNSRLVYVCDPVMGDkwNGEGsMYVPQDLLPVYRDKVVPVADIITPNQFEAELLSGRKIHS 164
Cdd:cd01173  81 LGSAEQVEAVAEIVKRLKEKNPNLLYVCDPVMGD--NGKL-YVVAEEIVPVYRDLLVPLADIITPNQFELELLTGKKIND 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26006861 165 QEEAFEVMDMLHCMGPDTVVITSSDLPssqGSDYLIALGSQRMRkpdgstvTQRIRMEMRKVEAVFVGTGDLFAAMLLAW 244
Cdd:cd01173 158 LEDAKAAARALHAKGPKTVVVTSVELA---DDDRIEMLGSTATE-------AWLVQRPKIPFPAYFNGTGDLFAALLLAR 227

                       250       260
                ....*....|....*....|....*...
gi 26006861 245 THKHPDnLKVACEKTVSAMQHVLQRTIR 272
Cdd:cd01173 228 LLKGKS-LAEALEKALNFVHEVLEATYE 254
PdxK COG2240
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal ...
 6-272 4.74e-86

Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal/pyridoxine/pyridoxamine kinase is part of the Pathway/BioSystem: Pyridoxal phosphate biosynthesis


Pssm-ID: 441841 [Multi-domain]  Cd Length: 272  Bit Score: 259.31  E-value: 4.74e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26006861   6 RVLSIQSHVVRGYVGNRAAMFPLQVLGFEVDAVNSVQFSNHTGYAHWKGQVLKSQELHELYEGLKVNDVN-KYDYVLTGY 84
Cdd:COG2240   3 RVLSIQSHVVYGHVGNSAAVPPLSALGVEVWPLPTVLLSNHTGYGTFTGRDLPTDDIADILDGWKELGVLlEFDAVLSGY 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26006861  85 TRDKSFLAMVVDIVRELKQQNSRLVYVCDPVMGDkwNGEGsMYVPQDLLPVYRDKVVPVADIITPNQFEAELLSGRKIHS 164
Cdd:COG2240  83 LGSAEQGDIIADFVARVKAANPDALYLCDPVMGD--NGKG-YYVFPGIAEFIMRRLVPLADIITPNLTELALLTGRPYET 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26006861 165 QEEAFEVMDMLHCMGPDTVVITSsdLPSSQGSDYLIA-LGSQRmrkpDGSTVTQRirmemRKVEAVFVGTGDLFAAMLLA 243
Cdd:COG2240 160 LEEALAAARALLALGPKIVVVTS--VPLDDTPADKIGnLAVTA----DGAWLVET-----PLLPFSPNGTGDLFAALLLA 228

                       250       260
                ....*....|....*....|....*....
gi 26006861 244 WTHKHpDNLKVACEKTVSAMQHVLQRTIR 272
Cdd:COG2240 229 HLLRG-KSLEEALERAAAFVYEVLERTAA 256
PRK05756 PRK05756
pyridoxal kinase PdxY;
7-312 8.28e-79

pyridoxal kinase PdxY;


Pssm-ID: 235592 [Multi-domain]  Cd Length: 286  Bit Score: 241.31  E-value: 8.28e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26006861    7 VLSIQSHVVRGYVGNRAAMFPLQVLGFEVDAVNSVQFSNHTGYAHWKGQVLKSQELHELYEGLKVNDV-NKYDYVLTGYT 85
Cdd:PRK05756   4 ILSIQSHVVYGHVGNSAAVFPMQRLGVNVWPLNTVQFSNHTGYGKWTGCVMPPSHLTEIVQGIADIGWlGECDAVLSGYL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26006861   86 RDKSFLAMVVDIVRELKQQNSRLVYVCDPVMGDKwngEGSMYVPQDLLPVYRDKVVPVADIITPNQFEAELLSGRKIHSQ 165
Cdd:PRK05756  84 GSAEQGEAILDAVRRVKAANPQALYFCDPVMGDP---EKGCIVAPGVAEFLRDRALPAADIITPNLFELEWLSGRPVETL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26006861  166 EEAFEVMDMLHCMGPDTVVITSsdlpssqgsdylialgSQRMRKPDGST----VTQR----IRMEMRKVEAVFVGTGDLF 237
Cdd:PRK05756 161 EDAVAAARALIARGPKIVLVTS----------------LARAGYPADRFemllVTADgawhISRPLVDFMRQPVGVGDLT 224

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 26006861  238 AAMLLAWtHKHPDNLKVACEKTVSAMQHVLQRTircakAEAGEgqkpspaqLELRMVQSKRDIEDPEIVVQATVL 312
Cdd:PRK05756 225 SALFLAR-LLQGGSLEEALEHTTAAVYEVMART-----KERGS--------YELQLVAAQDSIATPRAMFQARRL 285
pdxK PRK08176
pyridoxine/pyridoxal/pyridoxamine kinase;
7-277 3.45e-31

pyridoxine/pyridoxal/pyridoxamine kinase;


Pssm-ID: 181269 [Multi-domain]  Cd Length: 281  Bit Score: 118.22  E-value: 3.45e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26006861    7 VLSIQSHVVRGYVGNRAAMFPLQVLGFEVDAVNSVQFSNHTGY---------AHWKGQVLKSQELHELYEGLKVndvnky 77
Cdd:PRK08176  18 IVAVQSQVVYGSVGNSIAVPAIKANGLRVFAVPTVLLSNTPHYptfyggaipDEWFSGYLRALQERDALRQLRA------ 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26006861   78 dyVLTGYTRDKSFLAMVVDIVRELKQQNSRLVYVCDPVMGDKWNGegsMYVPQDLLPVYRDKVVPVADIITPNQFEAELL 157
Cdd:PRK08176  92 --VTTGYMGSASQIKILAEWLTALRADHPDLLIMVDPVIGDIDSG---IYVKPDLPEAYRQHLLPLAQGLTPNIFELEIL 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26006861  158 SGRKIHSQEEAFEVMDMLHCMGPDTVVITSSDlpssqgsdylIALGSQRMR----KPDGSTVTQRIRmemrkVEAVFVGT 233
Cdd:PRK08176 167 TGKPCRTLDSAIAAAKSLLSDTLKWVVITSAA----------GNEENQEMQvvvvTADSVNVISHPR-----VDTDLKGT 231

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 26006861  234 GDLFAAMLLA-WTHKHPdnLKVACEKTVSAMQHVLQRTIRCAKAE 277
Cdd:PRK08176 232 GDLFCAELVSgLLKGKA--LTDAAHRAGLRVLEVMRYTQQAGSDE 274
ThiD COG0351
Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; ...
 92-284 3.06e-18

Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase is part of the Pathway/BioSystem: Thiamine biosynthesis


Pssm-ID: 440120 [Multi-domain]  Cd Length: 254  Bit Score: 82.39  E-value: 3.06e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26006861  92 AMVVDIVRELKQQNsrlvYVCDPVMGDKWngeGSMYVPQDLLPVYRDKVVPVADIITPNQFEAELLSGRKIHSQEEAFEV 171
Cdd:COG0351  82 EAVAEILADYPLVP----VVLDPVMVAKS---GDRLLDEDAVEALRELLLPLATVVTPNLPEAEALLGIEITTLDDMREA 154

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26006861 172 MDMLHCMGPDTVVITSSDLPSSQGSDYLIalgsqrmrkpDGSTVTqriRMEMRKVEAV-FVGTGDLFAAML---LAwthk 247
Cdd:COG0351 155 AKALLELGAKAVLVKGGHLPGDEAVDVLY----------DGDGVR---EFSAPRIDTGnTHGTGCTLSSAIaalLA---- 217

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 26006861 248 HPDNLKVACEKTvsamQHVLQRTIRCAKAeAGEGQKP 284
Cdd:COG0351 218 KGLDLEEAVREA----KEYVTQAIRAALR-LGMGHGP 249
ribokinase_pfkB_like cd00287
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ...
 77-244 1.42e-15

ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including carbohydrates and aromatic small molecules, all are phosphorylated at a hydroxyl group. The superfamily includes ribokinase, fructokinase, ketohexokinase, 2-dehydro-3-deoxygluconokinase, 1-phosphofructokinase, the minor 6-phosphofructokinase (PfkB), inosine-guanosine kinase, and adenosine kinase. Even though there is a high degree of structural conservation within this superfamily, their multimerization level varies widely, monomeric (e.g. adenosine kinase), dimeric (e.g. ribokinase), and trimeric (e.g THZ kinase).


Pssm-ID: 238177 [Multi-domain]  Cd Length: 196  Bit Score: 73.67  E-value: 1.42e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26006861  77 YDYVLTGYTRDKsfLAMVVDIVRELKQQNsrLVYVCDPVMGDKWNGEGSMYvpqdllpvyrdKVVPVADIITPNQFEAEL 156
Cdd:cd00287  58 ADAVVISGLSPA--PEAVLDALEEARRRG--VPVVLDPGPRAVRLDGEELE-----------KLLPGVDILTPNEEEAEA 122

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26006861 157 LSGRKIHSQEEAFEVMDMLHCMGPDTVVITssdlpssQGSDYLIALGSQRmrkpdgstvtQRIRMEMRKVEAV-FVGTGD 235
Cdd:cd00287 123 LTGRRDLEVKEAAEAAALLLSKGPKVVIVT-------LGEKGAIVATRGG----------TEVHVPAFPVKVVdTTGAGD 185


                ....*....
gi 26006861 236 LFAAMLLAW 244
Cdd:cd00287 186 AFLAALAAG 194
Phos_pyr_kin pfam08543
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ...
 97-201 8.57e-15

Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate (TPP) synthesis pathway, TPP is an essential cofactor for many enzymes.


Pssm-ID: 430062 [Multi-domain]  Cd Length: 246  Bit Score: 72.51  E-value: 8.57e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26006861    97 IVRELKQQNSRLVyvCDPVMGDKwngEGSMYVPQDLLPVYRDKVVPVADIITPNQFEAELLSGRKIHSQEEAFEVMDMLH 176
Cdd:pfam08543  78 VAEKLDKYGVPVV--LDPVMVAK---SGDSLLDDEAIEALKEELLPLATLITPNLPEAEALTGRKIKTLEDMKEAAKKLL 152

                          90       100
                  ....*....|....*....|....*..
gi 26006861   177 CMGPDTVVITSSDLPSSQG--SDYLIA 201
Cdd:pfam08543 153 ALGAKAVLIKGGHLEGEEAvvTDVLYD 179
PRK06427 PRK06427
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed
 94-284 2.61e-13

bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed


Pssm-ID: 180561 [Multi-domain]  Cd Length: 266  Bit Score: 68.61  E-value: 2.61e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26006861   94 VVDIVRELKQQNSRLVYVCDPVM----GDkwngegsmyvP---QDLLPVYRDKVVPVADIITPNQFEAELLSGRKIHSQE 166
Cdd:PRK06427  87 IIETVAEALKRYPIPPVVLDPVMiaksGD----------PllaDDAVAALRERLLPLATLITPNLPEAEALTGLPIADTE 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26006861  167 EAFEVM-DMLHCMGPDTVVITSS-DLPSSQGSDYLIalgsqrmrkpDGSTVTqriRMEMRKVEAVFV-GTGDLFAAMLLA 243
Cdd:PRK06427 157 DEMKAAaRALHALGCKAVLIKGGhLLDGEESVDWLF----------DGEGEE---RFSAPRIPTKNThGTGCTLSAAIAA 223

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 26006861  244 WTHKHPDNLkvaceKTVSAMQHVLQRTIRCAkAEAGEGQKP 284
Cdd:PRK06427 224 ELAKGASLL-----DAVQTAKDYVTRAIRHA-LEIGQGHGP 258
PRK07105 PRK07105
pyridoxamine kinase; Validated
 76-270 5.46e-13

pyridoxamine kinase; Validated


Pssm-ID: 180840 [Multi-domain]  Cd Length: 284  Bit Score: 68.02  E-value: 5.46e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26006861   76 KYDYVLTGYTRDKSFLAMVVDIVRELKQQNSRLVyvCDPVMGDKwngeGSMYVP--QDLLPVYRdKVVPVADIITPNQFE 153
Cdd:PRK07105  75 KFDAIYSGYLGSPRQIQIVSDFIKYFKKKDLLVV--VDPVMGDN----GKLYQGfdQEMVEEMR-KLIQKADVITPNLTE 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26006861  154 AELLSG---RKIHSQEEafEVMDMLHC---MGPDTVVITSsdLPSSQGSDYLIALGSQ--RMRKPDGstvtqrirmemRK 225
Cdd:PRK07105 148 ACLLLDkpyLEKSYSEE--EIKQLLRKladLGPKIVIITS--VPFEDGKIGVAYYDRAtdRFWKVFC-----------KY 212

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 26006861  226 VEAVFVGTGDLFAAMLLAWTHkHPDNLKVACEKTVSAMQHVLQRT 270
Cdd:PRK07105 213 IPAHYPGTGDIFTSVITGSLL-QGDSLPIALDRAVQFIEKGIRAT 256
PRK11142 PRK11142
ribokinase; Provisional
 145-186 7.70e-10

ribokinase; Provisional


Pssm-ID: 236858 [Multi-domain]  Cd Length: 306  Bit Score: 58.73  E-value: 7.70e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 26006861  145 DIITPNQFEAELLSGRKIHSQEEAFEVMDMLHCMGPDTVVIT 186
Cdd:PRK11142 180 DIITPNETEAEKLTGIRVEDDDDAAKAAQVLHQKGIETVLIT 221
PRK12412 PRK12412
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
6-265 9.31e-10

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 183512 [Multi-domain]  Cd Length: 268  Bit Score: 58.44  E-value: 9.31e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26006861    6 RVLSIQSHVVRGYVGNRAAMFPLQVLG-FEVDAVNS-VQFSNHTGYAHwkgQVLK------SQELHELYEGLKVndvnky 77
Cdd:PRK12412   3 KALTIAGSDTSGGAGIQADLKTFQELGvYGMTSLTTiVTMDPHNGWAH---NVFPipastlKPQLETTIEGVGV------ 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26006861   78 DYVLTGYTRDKSFLAMVVDIVRELKQQNSrlvyVCDPVMGDKwnGEGSMYVPQDLLpVYRDKVVPVADIITPNQFEAELL 157
Cdd:PRK12412  74 DALKTGMLGSVEIIEMVAETIEKHNFKNV----VVDPVMVCK--GADEALHPETND-CLRDVLVPKALVVTPNLFEAYQL 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26006861  158 SGRKIHSQEEAFEVMDMLHCMGPDTVVIT-SSDLPSSQGSDYLIalgsqrmrkpDGSTVTQrirMEMRKVEAVFV-GTGD 235
Cdd:PRK12412 147 SGVKINSLEDMKEAAKKIHALGAKYVLIKgGSKLGTETAIDVLY----------DGETFDL---LESEKIDTTNThGAGC 213

                        250       260       270
                 ....*....|....*....|....*....|...
gi 26006861  236 LFAAMLLAWTHKH---PDNLKVACEKTVSAMQH 265
Cdd:PRK12412 214 TYSAAITAELAKGkpvKEAVKTAKEFITAAIRY 246
PLN02898 PLN02898
HMP-P kinase/thiamin-monophosphate pyrophosphorylase
 78-199 9.49e-10

HMP-P kinase/thiamin-monophosphate pyrophosphorylase


Pssm-ID: 215486 [Multi-domain]  Cd Length: 502  Bit Score: 59.40  E-value: 9.49e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26006861   78 DYVLTGYTRDKSFLAMVVDIVRELKQQNsrlvYVCDPVMGDKwngEGSMYVPQDLLPVYRDKVVPVADIITPNQFEAE-L 156
Cdd:PLN02898  80 DVVKTGMLPSAEIVKVLCQALKEFPVKA----LVVDPVMVST---SGDVLAGPSILSALREELLPLATIVTPNVKEASaL 152

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 26006861  157 LSGRKIHSQEEAFEVMDMLHCMGPDTVVITSSDLPSSQGS-DYL 199
Cdd:PLN02898 153 LGGDPLETVADMRSAAKELHKLGPRYVLVKGGHLPDSLDAvDVL 196
PfkB pfam00294
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ...
 134-244 1.07e-09

pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.


Pssm-ID: 425587 [Multi-domain]  Cd Length: 294  Bit Score: 58.51  E-value: 1.07e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26006861   134 PVYRD----------KVVPVADIITPNQFEAELLSGRKIHSQEEAFEVMDMLHCMGPDTVVITSsdlpSSQGSDYLIALG 203
Cdd:pfam00294 161 PNLLDplgaareallELLPLADLLKPNEEELEALTGAKLDDIEEALAALHKLLAKGIKTVIVTL----GADGALVVEGDG 236

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 26006861   204 SQRMRKPdgstvtqrirmemRKVEAV-FVGTGDLFAAMLLAW 244
Cdd:pfam00294 237 EVHVPAV-------------PKVKVVdTTGAGDSFVGGFLAG 265
PRK08573 PRK08573
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
97-243 4.88e-08

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 236297 [Multi-domain]  Cd Length: 448  Bit Score: 53.96  E-value: 4.88e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26006861   97 IVRELKQQNSRLVY--VCDPVMGDKwngEGSMYVPQDLLPVYRDKVVPVADIITPNQFEAELLSGRKIHSQEEAFEVMDM 174
Cdd:PRK08573  85 IIEAVAKTVSKYGFplVVDPVMIAK---SGAPLLREDAVDALIKRLLPLATVVTPNRPEAEKLTGMKIRSVEDARKAAKY 161

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 26006861  175 LHC-MGPDTVVITSSDLPSSQGSDYLIALGSQR-MRKPdgstvtqriRMEMRKVEavfvGTGDLFAAMLLA 243
Cdd:PRK08573 162 IVEeLGAEAVVVKGGHLEGEEAVDVLYHNGTFReFRAP---------RVESGCTH----GTGCSFSAAIAA 219
ribokinase cd01174
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ...
 137-243 5.53e-08

Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This reaction is the first step in the ribose metabolism. It traps ribose within the cell after uptake and also prepares the sugar for use in the synthesis of nucleotides and histidine, and for entry into the pentose phosphate pathway. Ribokinase is dimeric in solution.


Pssm-ID: 238579 [Multi-domain]  Cd Length: 292  Bit Score: 53.32  E-value: 5.53e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26006861 137 RDKVVPVADIITPNQFEAELLSGRKIHSQEEAFEVMDMLHCMGPDTVVITssdlpssqgsdyliaLGSQrmrkpdGS--- 213
Cdd:cd01174 169 PAELLALVDILVPNETEAALLTGIEVTDEEDAEKAARLLLAKGVKNVIVT---------------LGAK------GAlla 227

                        90       100       110
                ....*....|....*....|....*....|.
gi 26006861 214 TVTQRIRMEMRKVEAV-FVGTGDLFAAMLLA 243
Cdd:cd01174 228 SGGEVEHVPAFKVKAVdTTGAGDTFIGALAA 258
PRK12413 PRK12413
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
111-185 1.52e-07

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 183513 [Multi-domain]  Cd Length: 253  Bit Score: 51.60  E-value: 1.52e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 26006861  111 VCDPVMGDKWNGEGSMYVPQDLLPvyrdKVVPVADIITPNQFEAELLSGRKIHSQEEAFEVMDMLHCMGPDTVVI 185
Cdd:PRK12413 101 VLDPVLVCKETHDVEVSELRQELI----QFFPYVTVITPNLVEAELLSGKEIKTLEDMKEAAKKLYDLGAKAVVI 171
PRK12616 PRK12616
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
51-186 3.21e-07

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 183624  Cd Length: 270  Bit Score: 50.81  E-value: 3.21e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26006861   51 HWKGQVLK------SQELHELYEGLKVndvnkyDYVLTGYTRDKSFLAMVVDIVRELKQQNsrlvYVCDPVMGDKwnGEG 124
Cdd:PRK12616  49 SWDHQVFPidtdtiRAQLSTIVDGIGV------DAMKTGMLPTVDIIELAADTIKEKQLKN----VVIDPVMVCK--GAN 116

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 26006861  125 SMYVPQDLlPVYRDKVVPVADIITPNQFEAELLSGR-KIHSQEEAFEVMDMLHCMGPDTVVIT 186
Cdd:PRK12616 117 EVLYPEHA-EALREQLAPLATVITPNLFEAGQLSGMgEIKTVEQMKEAAKKIHELGAQYVVIT 178
RbsK COG0524
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ...
 80-243 3.89e-06

Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar or nucleoside kinase, ribokinase family is part of the Pathway/BioSystem: Glycolysis


Pssm-ID: 440290 [Multi-domain]  Cd Length: 301  Bit Score: 47.57  E-value: 3.89e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26006861  80 VLTGYT-RDKSFLAMVVDIVRELKQQNSRLVYvcDPvmgdkwNGEGSMYVP-QDLLpvyrDKVVPVADIITPNQFEAELL 157
Cdd:COG0524 132 HLGGITlASEPPREALLAALEAARAAGVPVSL--DP------NYRPALWEPaRELL----RELLALVDILFPNEEEAELL 199

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26006861 158 SGRkihsqEEAFEVMDMLHCMGPDTVVITssdlpssqgsdyliaLGSqrmrkpDGSTV---TQRIRMEMRKVEAVF-VGT 233
Cdd:COG0524 200 TGE-----TDPEEAAAALLARGVKLVVVT---------------LGA------EGALLytgGEVVHVPAFPVEVVDtTGA 253

                       170
                ....*....|
gi 26006861 234 GDLFAAMLLA 243
Cdd:COG0524 254 GDAFAAGFLA 263
FruK COG1105
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
145-256 3.93e-04

1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];


Pssm-ID: 440722 [Multi-domain]  Cd Length: 304  Bit Score: 41.27  E-value: 3.93e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26006861 145 DIITPNQFEAELLSGRKIHSQEEAFEVMDMLHCMGPDTVVITssdlpssqgsdyliaLGSqrmrkpDGS---TVTQRIRM 221
Cdd:COG1105 179 DLIKPNLEELEELLGRPLETLEDIIAAARELLERGAENVVVS---------------LGA------DGAllvTEDGVYRA 237

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 26006861 222 EMRKVEAVF-VGTGD-LFAAMLLAWTHKHP--DNLK--VAC 256
Cdd:COG1105 238 KPPKVEVVStVGAGDsMVAGFLAGLARGLDleEALRlaVAA 278
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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