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Conserved domains on  [gi|1034627647|ref|XP_016883973|]
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pyridoxal kinase isoform X4 [Homo sapiens]

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 ...
 1-231 3.39e-100

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: 292.89  E-value: 3.39e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034627647   1 MNKYDYVLTGYTRDKSFLAMVVDIVQELKQQNPRLVYVCDPVLGDKWDGegsMYVPEDLLPVYKEKVVPLADIITPNQFE 80
Cdd:TIGR00687  72 LNQCDAVLSGYLGSAEQVAMVVGIVRQVKQANPQALYVCDPVMGDPWKG---CYVAPDLLEVYREKAIPVADIITPNQFE 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034627647  81 AELLSGRKIHSQEEALRVMDMLHSMGPDTVVITssdlpspqgsnYLIVLGSQRRRNPAGSVVMERIRMDIRKVDAVF--- 157
Cdd:TIGR00687 149 LELLTGRRINTEEEALAAADALIAMGPDIVLVT-----------HLIRAGSQRDRSFEGLVATQEGRWHISRPLAVFdpp 217

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034627647 158 -VGTGDLFAAMLLAwTHKHPNNLKVACEKTVSTLHHVLQRTIQCAKAQagegVRPSPMQLELRMVQSKRDIEDPE 231
Cdd:TIGR00687 218 pVGTGDLIAALLLA-TLLHGNSLKEALEKTVSAVYHVLRTTIQLGKYE----LQPVAAQLEIRMPQSKFDAEKVE 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 ...
 1-231 3.39e-100

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: 292.89  E-value: 3.39e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034627647   1 MNKYDYVLTGYTRDKSFLAMVVDIVQELKQQNPRLVYVCDPVLGDKWDGegsMYVPEDLLPVYKEKVVPLADIITPNQFE 80
Cdd:TIGR00687  72 LNQCDAVLSGYLGSAEQVAMVVGIVRQVKQANPQALYVCDPVMGDPWKG---CYVAPDLLEVYREKAIPVADIITPNQFE 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034627647  81 AELLSGRKIHSQEEALRVMDMLHSMGPDTVVITssdlpspqgsnYLIVLGSQRRRNPAGSVVMERIRMDIRKVDAVF--- 157
Cdd:TIGR00687 149 LELLTGRRINTEEEALAAADALIAMGPDIVLVT-----------HLIRAGSQRDRSFEGLVATQEGRWHISRPLAVFdpp 217

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034627647 158 -VGTGDLFAAMLLAwTHKHPNNLKVACEKTVSTLHHVLQRTIQCAKAQagegVRPSPMQLELRMVQSKRDIEDPE 231
Cdd:TIGR00687 218 pVGTGDLIAALLLA-TLLHGNSLKEALEKTVSAVYHVLRTTIQLGKYE----LQPVAAQLEIRMPQSKFDAEKVE 287
PLN02978 PLN02978
pyridoxal kinase
 3-237 1.11e-88

pyridoxal kinase


Pssm-ID: 215529 [Multi-domain]  Cd Length: 308  Bit Score: 264.29  E-value: 1.11e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034627647   3 KYDYVLTGYTRDKSFLAMVVDIVQELKQQNPRLVYVCDPVLGDkwdgEGSMYVPEDLLPVYKEKVVPLADIITPNQFEAE 82
Cdd:PLN02978   86 FYTHLLTGYIGSVSFLRTVLRVVKKLRSVNPNLTYVCDPVLGD----EGKLYVPPELVPVYREKVVPLATMLTPNQFEAE 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034627647  83 LLSGRKIHSQEEALRVMDMLHSMGPDTVVITSSDLPspqgsNYLIVLGSQRRRNPAGSvvmERIRMDIRKVDAVFVGTGD 162
Cdd:PLN02978  162 QLTGIRIVTEEDAREACAILHAAGPSKVVITSIDID-----GKLLLVGSHRKEKGARP---EQFKIVIPKIPAYFTGTGD 233

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034627647 163 LFAAMLLAWTHKHPNNLKVACEKTVSTLHHVLQRTIQCAKAqagEGVRPSPMQLELRMVQSKRDIEDPEIVVQAT 237
Cdd:PLN02978  234 LMAALLLGWSHKYPDNLDKAAELAVSSLQAVLRRTLADYKR---AGADPKSSSLELRLVQSQDDIRHPQVRFKAE 305
pyridoxal_pyridoxamine_kinase cd01173
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ...
 2-199 9.12e-71

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: 217.07  E-value: 9.12e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034627647   2 NKYDYVLTGYTRDKSFLAMVVDIVQELKQQNPRLVYVCDPVLGDkwdgEGSMYV-PEDLLPVYKEKVVPLADIITPNQFE 80
Cdd:cd01173    71 LEYDAVLTGYLGSAEQVEAVAEIVKRLKEKNPNLLYVCDPVMGD----NGKLYVvAEEIVPVYRDLLVPLADIITPNQFE 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034627647  81 AELLSGRKIHSQEEALRVMDMLHSMGPDTVVITSSDLPSPqgsnylivlgsqRRRNPAGSVVMERIRMDIRKVD--AVFV 158
Cdd:cd01173   147 LELLTGKKINDLEDAKAAARALHAKGPKTVVVTSVELADD------------DRIEMLGSTATEAWLVQRPKIPfpAYFN 214

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1034627647 159 GTGDLFAAMLLAWTHKHPnNLKVACEKTVSTLHHVLQRTIQ 199
Cdd:cd01173   215 GTGDLFAALLLARLLKGK-SLAEALEKALNFVHEVLEATYE 254
PdxK COG2240
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal ...
 5-199 7.97e-50

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: 163.78  E-value: 7.97e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034627647   5 DYVLTGYTRDKSFLAMVVDIVQELKQQNPRLVYVCDPVLGDkwDGEGsMYVPEDLLPVYKEKVVPLADIITPNQFEAELL 84
Cdd:COG2240    76 DAVLSGYLGSAEQGDIIADFVARVKAANPDALYLCDPVMGD--NGKG-YYVFPGIAEFIMRRLVPLADIITPNLTELALL 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034627647  85 SGRKIHSQEEALRVMDMLHSMGPDTVVITS---SDLPSPQGSNYLIvlgsqrrrNPAGSVVMERirmdiRKVDAVFVGTG 161
Cdd:COG2240   153 TGRPYETLEEALAAARALLALGPKIVVVTSvplDDTPADKIGNLAV--------TADGAWLVET-----PLLPFSPNGTG 219

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1034627647 162 DLFAAMLLA-WTHKHPnnLKVACEKTVSTLHHVLQRTIQ 199
Cdd:COG2240   220 DLFAALLLAhLLRGKS--LEEALERAAAFVYEVLERTAA 256
Phos_pyr_kin pfam08543
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ...
 24-122 5.25e-17

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: 77.14  E-value: 5.25e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034627647  24 IVQELKQQNPRLVyvCDPVLGDKwdgEGSMYVPEDLLPVYKEKVVPLADIITPNQFEAELLSGRKIHSQEEALRVMDMLH 103
Cdd:pfam08543  78 VAEKLDKYGVPVV--LDPVMVAK---SGDSLLDDEAIEALKEELLPLATLITPNLPEAEALTGRKIKTLEDMKEAAKKLL 152

                          90
                  ....*....|....*....
gi 1034627647 104 SMGPDTVVITSSDLPSPQG 122
Cdd:pfam08543 153 ALGAKAVLIKGGHLEGEEA 171
 
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 ...
 1-231 3.39e-100

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: 292.89  E-value: 3.39e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034627647   1 MNKYDYVLTGYTRDKSFLAMVVDIVQELKQQNPRLVYVCDPVLGDKWDGegsMYVPEDLLPVYKEKVVPLADIITPNQFE 80
Cdd:TIGR00687  72 LNQCDAVLSGYLGSAEQVAMVVGIVRQVKQANPQALYVCDPVMGDPWKG---CYVAPDLLEVYREKAIPVADIITPNQFE 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034627647  81 AELLSGRKIHSQEEALRVMDMLHSMGPDTVVITssdlpspqgsnYLIVLGSQRRRNPAGSVVMERIRMDIRKVDAVF--- 157
Cdd:TIGR00687 149 LELLTGRRINTEEEALAAADALIAMGPDIVLVT-----------HLIRAGSQRDRSFEGLVATQEGRWHISRPLAVFdpp 217

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034627647 158 -VGTGDLFAAMLLAwTHKHPNNLKVACEKTVSTLHHVLQRTIQCAKAQagegVRPSPMQLELRMVQSKRDIEDPE 231
Cdd:TIGR00687 218 pVGTGDLIAALLLA-TLLHGNSLKEALEKTVSAVYHVLRTTIQLGKYE----LQPVAAQLEIRMPQSKFDAEKVE 287
PLN02978 PLN02978
pyridoxal kinase
 3-237 1.11e-88

pyridoxal kinase


Pssm-ID: 215529 [Multi-domain]  Cd Length: 308  Bit Score: 264.29  E-value: 1.11e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034627647   3 KYDYVLTGYTRDKSFLAMVVDIVQELKQQNPRLVYVCDPVLGDkwdgEGSMYVPEDLLPVYKEKVVPLADIITPNQFEAE 82
Cdd:PLN02978   86 FYTHLLTGYIGSVSFLRTVLRVVKKLRSVNPNLTYVCDPVLGD----EGKLYVPPELVPVYREKVVPLATMLTPNQFEAE 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034627647  83 LLSGRKIHSQEEALRVMDMLHSMGPDTVVITSSDLPspqgsNYLIVLGSQRRRNPAGSvvmERIRMDIRKVDAVFVGTGD 162
Cdd:PLN02978  162 QLTGIRIVTEEDAREACAILHAAGPSKVVITSIDID-----GKLLLVGSHRKEKGARP---EQFKIVIPKIPAYFTGTGD 233

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034627647 163 LFAAMLLAWTHKHPNNLKVACEKTVSTLHHVLQRTIQCAKAqagEGVRPSPMQLELRMVQSKRDIEDPEIVVQAT 237
Cdd:PLN02978  234 LMAALLLGWSHKYPDNLDKAAELAVSSLQAVLRRTLADYKR---AGADPKSSSLELRLVQSQDDIRHPQVRFKAE 305
PTZ00344 PTZ00344
pyridoxal kinase; Provisional
 2-239 2.29e-76

pyridoxal kinase; Provisional


Pssm-ID: 240372 [Multi-domain]  Cd Length: 296  Bit Score: 232.66  E-value: 2.29e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034627647   2 NKYDYVLTGYTRDKSFLAMVVDIVQELKQQNPRLVYVCDPVLGDkwdgEGSMYVPEDLLPVYKEkVVPLADIITPNQFEA 81
Cdd:PTZ00344   76 SDYTYVLTGYINSADILREVLATVKEIKELRPKLIFLCDPVMGD----DGKLYVKEEVVDAYRE-LIPYADVITPNQFEA 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034627647  82 ELLSGRKIHSQEEALRVMDMLHSMGPDTVVITSSDLpsPQGSNYLIVLGSQRRRNPAGSvvmERIRMDIRKVDAVFVGTG 161
Cdd:PTZ00344  151 SLLSGVEVKDLSDALEAIDWFHEQGIPVVVITSFRE--DEDPTHLRFLLSCRDKDTKNN---KRFTGKVPYIEGRYTGTG 225

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034627647 162 DLFAAMLLAWTHKHPnnLKVACEKTVSTLHHVLQRTIqcakaQAGEGVRPSPMQLELRMVQSKRDIEDPEIVVQATVL 239
Cdd:PTZ00344  226 DLFAALLLAFSHQHP--MDLAVGKAMGVLQDIIKATR-----ESGGSGSSSLMSRELRLIQSPRDLLNPETVFKVTPL 296
pyridoxal_pyridoxamine_kinase cd01173
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ...
 2-199 9.12e-71

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: 217.07  E-value: 9.12e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034627647   2 NKYDYVLTGYTRDKSFLAMVVDIVQELKQQNPRLVYVCDPVLGDkwdgEGSMYV-PEDLLPVYKEKVVPLADIITPNQFE 80
Cdd:cd01173    71 LEYDAVLTGYLGSAEQVEAVAEIVKRLKEKNPNLLYVCDPVMGD----NGKLYVvAEEIVPVYRDLLVPLADIITPNQFE 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034627647  81 AELLSGRKIHSQEEALRVMDMLHSMGPDTVVITSSDLPSPqgsnylivlgsqRRRNPAGSVVMERIRMDIRKVD--AVFV 158
Cdd:cd01173   147 LELLTGKKINDLEDAKAAARALHAKGPKTVVVTSVELADD------------DRIEMLGSTATEAWLVQRPKIPfpAYFN 214

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1034627647 159 GTGDLFAAMLLAWTHKHPnNLKVACEKTVSTLHHVLQRTIQ 199
Cdd:cd01173   215 GTGDLFAALLLARLLKGK-SLAEALEKALNFVHEVLEATYE 254
PdxK COG2240
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal ...
 5-199 7.97e-50

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: 163.78  E-value: 7.97e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034627647   5 DYVLTGYTRDKSFLAMVVDIVQELKQQNPRLVYVCDPVLGDkwDGEGsMYVPEDLLPVYKEKVVPLADIITPNQFEAELL 84
Cdd:COG2240    76 DAVLSGYLGSAEQGDIIADFVARVKAANPDALYLCDPVMGD--NGKG-YYVFPGIAEFIMRRLVPLADIITPNLTELALL 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034627647  85 SGRKIHSQEEALRVMDMLHSMGPDTVVITS---SDLPSPQGSNYLIvlgsqrrrNPAGSVVMERirmdiRKVDAVFVGTG 161
Cdd:COG2240   153 TGRPYETLEEALAAARALLALGPKIVVVTSvplDDTPADKIGNLAV--------TADGAWLVET-----PLLPFSPNGTG 219

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1034627647 162 DLFAAMLLA-WTHKHPnnLKVACEKTVSTLHHVLQRTIQ 199
Cdd:COG2240   220 DLFAALLLAhLLRGKS--LEEALERAAAFVYEVLERTAA 256
PRK05756 PRK05756
pyridoxal kinase PdxY;
5-239 1.50e-40

pyridoxal kinase PdxY;


Pssm-ID: 235592 [Multi-domain]  Cd Length: 286  Bit Score: 140.39  E-value: 1.50e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034627647   5 DYVLTGYTRDKSFLAMVVDIVQELKQQNPRLVYVCDPVLGDKwdgEGSMYVPEDLLPVYKEKVVPLADIITPNQFEAELL 84
Cdd:PRK05756   76 DAVLSGYLGSAEQGEAILDAVRRVKAANPQALYFCDPVMGDP---EKGCIVAPGVAEFLRDRALPAADIITPNLFELEWL 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034627647  85 SGRKIHSQEEALRVMDMLHSMGPDTVVITSSDLP-SPQGSNYLIVLgsqrrrNPAGSVVMERIRMDIRKVDavfVGTGDL 163
Cdd:PRK05756  153 SGRPVETLEDAVAAARALIARGPKIVLVTSLARAgYPADRFEMLLV------TADGAWHISRPLVDFMRQP---VGVGDL 223

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034627647 164 FAAMLLAWtHKHPNNLKVACEKTVSTLHHVLQRTIQCakaqageGVRpspmqlELRMVQSKRDIEDPEIVVQATVL 239
Cdd:PRK05756  224 TSALFLAR-LLQGGSLEEALEHTTAAVYEVMARTKER-------GSY------ELQLVAAQDSIATPRAMFQARRL 285
pdxK PRK08176
pyridoxine/pyridoxal/pyridoxamine kinase;
7-200 7.25e-24

pyridoxine/pyridoxal/pyridoxamine kinase;


Pssm-ID: 181269 [Multi-domain]  Cd Length: 281  Bit Score: 96.65  E-value: 7.25e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034627647   7 VLTGYTRDKSFLAMVVDIVQELKQQNPRLVYVCDPVLGDKWDGegsMYVPEDLLPVYKEKVVPLADIITPNQFEAELLSG 86
Cdd:PRK08176   92 VTTGYMGSASQIKILAEWLTALRADHPDLLIMVDPVIGDIDSG---IYVKPDLPEAYRQHLLPLAQGLTPNIFELEILTG 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034627647  87 RKIHSQEEALRVMDMLHSMGPDTVVITSSDLPSPQGS-NYLIVLGSQRrrnpagsVVMERIRmdirkVDAVFVGTGDLFA 165
Cdd:PRK08176  169 KPCRTLDSAIAAAKSLLSDTLKWVVITSAAGNEENQEmQVVVVTADSV-------NVISHPR-----VDTDLKGTGDLFC 236

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1034627647 166 AMLLA-WTHKHPnnLKVACEKTVSTLHHVLQRTIQC 200
Cdd:PRK08176  237 AELVSgLLKGKA--LTDAAHRAGLRVLEVMRYTQQA 270
ribokinase_pfkB_like cd00287
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ...
 4-171 1.63e-19

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: 82.91  E-value: 1.63e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034627647   4 YDYVLTGYTRDKsfLAMVVDIVQELKQQNPRlvYVCDPVLGDK-WDGEGsmyvpedllpvyKEKVVPLADIITPNQFEAE 82
Cdd:cd00287    58 ADAVVISGLSPA--PEAVLDALEEARRRGVP--VVLDPGPRAVrLDGEE------------LEKLLPGVDILTPNEEEAE 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034627647  83 LLSGRKIHSQEEALRVMDMLHSMGPDTVVITssdlpspQGSNYLIVLGSQRRRNPAGSVvmerirmdirKVDAV-FVGTG 161
Cdd:cd00287   122 ALTGRRDLEVKEAAEAAALLLSKGPKVVIVT-------LGEKGAIVATRGGTEVHVPAF----------PVKVVdTTGAG 184

                         170
                  ....*....|
gi 1034627647 162 DLFAAMLLAW 171
Cdd:cd00287   185 DAFLAALAAG 194
ThiD COG0351
Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; ...
 19-166 4.59e-19

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: 83.16  E-value: 4.59e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034627647  19 AMVVDIVQELKQQNprlvYVCDPVLGDKWDGEGSmyvPEDLLPVYKEKVVPLADIITPNQFEAELLSGRKIHSQEEALRV 98
Cdd:COG0351    82 EAVAEILADYPLVP----VVLDPVMVAKSGDRLL---DEDAVEALRELLLPLATVVTPNLPEAEALLGIEITTLDDMREA 154

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034627647  99 MDMLHSMGPDTVVITSSDLPSPQGSNYLiVLGSQRRRnpagsVVMERIRmdirkvDAVFVGTGDLFAA 166
Cdd:COG0351   155 AKALLELGAKAVLVKGGHLPGDEAVDVL-YDGDGVRE-----FSAPRID------TGNTHGTGCTLSS 210
Phos_pyr_kin pfam08543
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ...
 24-122 5.25e-17

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: 77.14  E-value: 5.25e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034627647  24 IVQELKQQNPRLVyvCDPVLGDKwdgEGSMYVPEDLLPVYKEKVVPLADIITPNQFEAELLSGRKIHSQEEALRVMDMLH 103
Cdd:pfam08543  78 VAEKLDKYGVPVV--LDPVMVAK---SGDSLLDDEAIEALKEELLPLATLITPNLPEAEALTGRKIKTLEDMKEAAKKLL 152

                          90
                  ....*....|....*....
gi 1034627647 104 SMGPDTVVITSSDLPSPQG 122
Cdd:pfam08543 153 ALGAKAVLIKGGHLEGEEA 171
PRK06427 PRK06427
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed
 21-170 7.45e-14

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


Pssm-ID: 180561 [Multi-domain]  Cd Length: 266  Bit Score: 69.00  E-value: 7.45e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034627647  21 VVDIVQELKQQNPRLVYVCDPVL----GDkwdgegsmyvP---EDLLPVYKEKVVPLADIITPNQFEAELLSGRKIHSQE 93
Cdd:PRK06427   87 IIETVAEALKRYPIPPVVLDPVMiaksGD----------PllaDDAVAALRERLLPLATLITPNLPEAEALTGLPIADTE 156

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034627647  94 EALRVM-DMLHSMGPDTVVITSS-DLPSPQGSNYLIvlgsqrrrNPAGSVVMERIRMDIRKVDavfvGTGDLFAAMLLA 170
Cdd:PRK06427  157 DEMKAAaRALHALGCKAVLIKGGhLLDGEESVDWLF--------DGEGEERFSAPRIPTKNTH----GTGCTLSAAIAA 223
PfkB pfam00294
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ...
 22-171 2.27e-11

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


Pssm-ID: 425587 [Multi-domain]  Cd Length: 294  Bit Score: 61.98  E-value: 2.27e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034627647  22 VDIVQELKQQNPRLVYVCDPVLGDKWDgegsmyvpedLLPVYKEkVVPLADIITPNQFEAELLSGRKIHSQEEALRVMDM 101
Cdd:pfam00294 143 EATLEELIEAAKNGGTFDPNLLDPLGA----------AREALLE-LLPLADLLKPNEEELEALTGAKLDDIEEALAALHK 211

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034627647 102 LHSMGPDTVVITSsdlpSPQGSnyLIVLGSQRRRNPAgsvvmerirmdIRKVDAV-FVGTGDLFAAMLLAW 171
Cdd:pfam00294 212 LLAKGIKTVIVTL----GADGA--LVVEGDGEVHVPA-----------VPKVKVVdTTGAGDSFVGGFLAG 265
PRK07105 PRK07105
pyridoxamine kinase; Validated
 3-197 7.12e-11

pyridoxamine kinase; Validated


Pssm-ID: 180840 [Multi-domain]  Cd Length: 284  Bit Score: 60.70  E-value: 7.12e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034627647   3 KYDYVLTGY---TRDksflamvVDIVQELKQ--QNPRLVYVCDPVLGDKwdgeGSMYVP--EDLLPVYKeKVVPLADIIT 75
Cdd:PRK07105   75 KFDAIYSGYlgsPRQ-------IQIVSDFIKyfKKKDLLVVVDPVMGDN----GKLYQGfdQEMVEEMR-KLIQKADVIT 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034627647  76 PNQFEAELLSG---RKIHSQEEalRVMDMLH---SMGPDTVVITSSdlpsPQGSNYLIVLGSQRRRNpagsvvmERIRMD 149
Cdd:PRK07105  143 PNLTEACLLLDkpyLEKSYSEE--EIKQLLRklaDLGPKIVIITSV----PFEDGKIGVAYYDRATD-------RFWKVF 209

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1034627647 150 IRKVDAVFVGTGDLFAAMLLAWTHkHPNNLKVACEKTVSTLHHVLQRT 197
Cdd:PRK07105  210 CKYIPAHYPGTGDIFTSVITGSLL-QGDSLPIALDRAVQFIEKGIRAT 256
PRK11142 PRK11142
ribokinase; Provisional
 70-113 7.41e-11

ribokinase; Provisional


Pssm-ID: 236858 [Multi-domain]  Cd Length: 306  Bit Score: 60.65  E-value: 7.41e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1034627647  70 LADIITPNQFEAELLSGRKIHSQEEALRVMDMLHSMGPDTVVIT 113
Cdd:PRK11142  178 LVDIITPNETEAEKLTGIRVEDDDDAAKAAQVLHQKGIETVLIT 221
ribokinase cd01174
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ...
 65-170 9.55e-11

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: 60.26  E-value: 9.55e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034627647  65 EKVVPLADIITPNQFEAELLSGRKIHSQEEALRVMDMLHSMGPDTVVITssdlpspqgsnylivLGSQrrrnpaGSVVM- 143
Cdd:cd01174   170 AELLALVDILVPNETEAALLTGIEVTDEEDAEKAARLLLAKGVKNVIVT---------------LGAK------GALLAs 228

                          90       100       110
                  ....*....|....*....|....*....|
gi 1034627647 144 --ERIRMDIRKVDAV-FVGTGDLFAAMLLA 170
Cdd:cd01174   229 ggEVEHVPAFKVKAVdTTGAGDTFIGALAA 258
PRK08573 PRK08573
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
38-133 1.62e-09

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 236297 [Multi-domain]  Cd Length: 448  Bit Score: 57.43  E-value: 1.62e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034627647  38 VCDPVLGDKwdgEGSMYVPEDLLPVYKEKVVPLADIITPNQFEAELLSGRKIHSQEEALRVMDMLH-SMGPDTVVITSSD 116
Cdd:PRK08573  101 VVDPVMIAK---SGAPLLREDAVDALIKRLLPLATVVTPNRPEAEKLTGMKIRSVEDARKAAKYIVeELGAEAVVVKGGH 177

                          90
                  ....*....|....*..
gi 1034627647 117 LPSPQGSNYLIVLGSQR 133
Cdd:PRK08573  178 LEGEEAVDVLYHNGTFR 194
RbsK COG0524
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ...
 7-170 5.25e-09

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: 55.28  E-value: 5.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034627647   7 VLTGYT-RDKSFLAMVVDIVQELKQQNPRLVYvcDPVLGDKwdgegsmyVPEDLLPVYKEkVVPLADIITPNQFEAELLS 85
Cdd:COG0524   132 HLGGITlASEPPREALLAALEAARAAGVPVSL--DPNYRPA--------LWEPARELLRE-LLALVDILFPNEEEAELLT 200

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034627647  86 GrkIHSQEEALRVmdmLHSMGPDTVVITssdlpspqgsnylivLGSQrrrnpaGSVVM---ERIRMDIRKVDAVF-VGTG 161
Cdd:COG0524   201 G--ETDPEEAAAA---LLARGVKLVVVT---------------LGAE------GALLYtggEVVHVPAFPVEVVDtTGAG 254


                  ....*....
gi 1034627647 162 DLFAAMLLA 170
Cdd:COG0524   255 DAFAAGFLA 263
PRK12413 PRK12413
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
66-112 6.03e-08

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 183513 [Multi-domain]  Cd Length: 253  Bit Score: 51.99  E-value: 6.03e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1034627647  66 KVVPLADIITPNQFEAELLSGRKIHSQEEALRVMDMLHSMGPDTVVI 112
Cdd:PRK12413  125 QFFPYVTVITPNLVEAELLSGKEIKTLEDMKEAAKKLYDLGAKAVVI 171
PLN02898 PLN02898
HMP-P kinase/thiamin-monophosphate pyrophosphorylase
 5-119 1.84e-07

HMP-P kinase/thiamin-monophosphate pyrophosphorylase


Pssm-ID: 215486 [Multi-domain]  Cd Length: 502  Bit Score: 51.31  E-value: 1.84e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034627647   5 DYVLTGYTRDKSFLAMVVDIVQELKQQNprlvYVCDPVLGDKwdgEGSMYVPEDLLPVYKEKVVPLADIITPNQFEAE-L 83
Cdd:PLN02898   80 DVVKTGMLPSAEIVKVLCQALKEFPVKA----LVVDPVMVST---SGDVLAGPSILSALREELLPLATIVTPNVKEASaL 152

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1034627647  84 LSGRKIHSqeealrVMDM------LHSMGPDTVVITSSDLPS 119
Cdd:PLN02898  153 LGGDPLET------VADMrsaakeLHKLGPRYVLVKGGHLPD 188
PRK12616 PRK12616
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
5-113 1.03e-06

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 183624  Cd Length: 270  Bit Score: 48.50  E-value: 1.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034627647   5 DYVLTGYTRDKSFLAMVVDIVQELKQQNprlvYVCDPVLGDKwdGEGSMYVPEDLlPVYKEKVVPLADIITPNQFEAELL 84
Cdd:PRK12616   76 DAMKTGMLPTVDIIELAADTIKEKQLKN----VVIDPVMVCK--GANEVLYPEHA-EALREQLAPLATVITPNLFEAGQL 148

                          90       100       110
                  ....*....|....*....|....*....|
gi 1034627647  85 SGR-KIHSQEEALRVMDMLHSMGPDTVVIT 113
Cdd:PRK12616  149 SGMgEIKTVEQMKEAAKKIHELGAQYVVIT 178
PRK12412 PRK12412
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
5-112 2.23e-06

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 183512 [Multi-domain]  Cd Length: 268  Bit Score: 47.27  E-value: 2.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034627647   5 DYVLTGYTRDKSFLAMVVDIVQELKQQNprlvYVCDPVLGDKwdGEGSMYVPEDLLpVYKEKVVPLADIITPNQFEAELL 84
Cdd:PRK12412   74 DALKTGMLGSVEIIEMVAETIEKHNFKN----VVVDPVMVCK--GADEALHPETND-CLRDVLVPKALVVTPNLFEAYQL 146

                          90       100
                  ....*....|....*....|....*...
gi 1034627647  85 SGRKIHSQEEALRVMDMLHSMGPDTVVI 112
Cdd:PRK12412  147 SGVKINSLEDMKEAAKKIHALGAKYVLI 174
FruK COG1105
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
22-176 4.37e-06

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


Pssm-ID: 440722 [Multi-domain]  Cd Length: 304  Bit Score: 46.67  E-value: 4.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034627647  22 VDIVQELKQQNPRLVyvcdpvlgdkWDGEGsmyvpEDLLPVYKEKVvplaDIITPNQFEAELLSGRKIHSQEEALRVMDM 101
Cdd:COG1105   148 AELIRLARARGAKVV----------LDTSG-----EALKAALEAGP----DLIKPNLEELEELLGRPLETLEDIIAAARE 208

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034627647 102 LHSMGPDTVVITssdlpspqgsnylivLGSQrrrnpaGSVVM---ERIRMDIRKVDAVF-VGTGD-LFAAMLLAWTHKHP 176
Cdd:COG1105   209 LLERGAENVVVS---------------LGAD------GALLVtedGVYRAKPPKVEVVStVGAGDsMVAGFLAGLARGLD 267
PTZ00347 PTZ00347
phosphomethylpyrimidine kinase; Provisional
 24-208 4.69e-06

phosphomethylpyrimidine kinase; Provisional


Pssm-ID: 240375 [Multi-domain]  Cd Length: 504  Bit Score: 46.88  E-value: 4.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034627647  24 IVQELKQqnprLVYVCDPVL----GDKWDGEGSMyvpEDLLPVYKEKVVPLADIITPNQFEAELLSGRK-IHSQEEALRV 98
Cdd:PTZ00347  317 VIEKLKN----LPMVVDPVLvatsGDDLVAQKNA---DDVLAMYKERIFPMATIITPNIPEAERILGRKeITGVYEARAA 389

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034627647  99 MDMLhsmgpdtvvitssdlpSPQGSNYLIVLGSQRRRNP--AGSVVMERIRMDIRKVDAVFV------GTGDLFAAMLLA 170
Cdd:PTZ00347  390 AQAL----------------AQYGSRYVLVKGGHDLIDPeaCRDVLYDREKDRFYEFTANRIatinthGTGCTLASAISS 453

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1034627647 171 WTHKHpNNLKVACEKTVSTLHHVLQRTIQCAKAQAGEG 208
Cdd:PTZ00347  454 FLARG-YTVPDAVERAIGYVHEAIVRSCGVPLGQGTNR 490
adenosine_kinase cd01168
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ...
 63-176 3.53e-04

Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside analogues at the 5'-hydroxyl using ATP or GTP as the phosphate donor.The physiological function of AK is associated with the regulation of extracellular adenosine levels and the preservation of intracellular adenylate pools. Adenosine kinase is involved in the purine salvage pathway.


Pssm-ID: 238573 [Multi-domain]  Cd Length: 312  Bit Score: 41.06  E-value: 3.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034627647  63 YKE---KVVPLADIITPNQFEAELLSGRKI-HSQEEALRVMdmlhSMGPDTVVITssdlpspQGSNYLIVLgSQRRRNPA 138
Cdd:cd01168   190 FKEallELLPYVDILFGNEEEAEALAEAETtDDLEAALKLL----ALRCRIVVIT-------QGAKGAVVV-EGGEVYPV 257

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1034627647 139 GSVVMERIrmdirkVDAvfVGTGDLFAA-MLLAWTHKHP 176
Cdd:cd01168   258 PAIPVEKI------VDT--NGAGDAFAGgFLYGLVQGEP 288
KdgK cd01166
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ...
 56-170 1.11e-03

2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form 2-keto-3-deoxy-6-phosphogluconate (KDGP). KDG is the common intermediate product, that allows organisms to channel D-glucuronate and/or D-galacturinate into the glycolysis and therefore use polymers, like pectin and xylan as carbon sources.


Pssm-ID: 238571 [Multi-domain]  Cd Length: 294  Bit Score: 39.48  E-value: 1.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034627647  56 PEDLLPVYKEkVVPLADIITPNQFEAELLSGRKIHSQ-EEALRvmdmLHSMGPDTVVItssdlpspqgsnylivlgsqrR 134
Cdd:cd01166   172 AEEAREALEE-LLPYVDIVLPSEEEAEALLGDEDPTDaAERAL----ALALGVKAVVV---------------------K 225

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1034627647 135 RNPAGSVVM---ERIRMDIRKVDAV-FVGTGDLFAAMLLA 170
Cdd:cd01166   226 LGAEGALVYtggGRVFVPAYPVEVVdTTGAGDAFAAGFLA 265
FruK_PfkB_like cd01164
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ...
 22-182 7.39e-03

1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. FruK plays an important role in the predominant pathway for fructose utilisation.This group also contains tagatose-6-phophate kinase, an enzyme of the tagatose 6-phosphate pathway, which responsible for breakdown of the galactose moiety during lactose metabolism by bacteria such as L. lactis.


Pssm-ID: 238570 [Multi-domain]  Cd Length: 289  Bit Score: 36.74  E-value: 7.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034627647  22 VDIVQELKQQNPRLVyvCDPvlgdkwDGEGsmyvpedLLPVYKEKVvplaDIITPNQFEAELLSGRKIHSQEEALRVMDM 101
Cdd:cd01164   148 AELVRLAREKGARVI--LDT------SGEA-------LLAALAAKP----FLIKPNREELEELFGRPLGDEEDVIAAARK 208

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034627647 102 LHSMGPDTVVITssdlpspqgsnylivLGSQrrrnpaGSVVMER---IRMDIRKVDAV-FVGTGD-LFAAMLLAWTHKHP 176
Cdd:cd01164   209 LIERGAENVLVS---------------LGAD------GALLVTKdgvYRASPPKVKVVsTVGAGDsMVAGFVAGLAQGLS 267


                  ....*...
gi 1034627647 177 --NNLKVA 182
Cdd:cd01164   268 leEALRLA 275
 
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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