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Conserved domains on  [gi|2217338257|ref|XP_047296957|]
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pyridoxal kinase isoform X2 [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 ...
 91-365 4.29e-130

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: 374.17  E-value: 4.29e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217338257  91 VLGFEIDAVNSVQFSNHTGYAHWKGQVLNSDELQELYEGL-RLNNMNKYDYVLTGYTRDKSFLAMVVDIVQELKQQNPRL 169
Cdd:TIGR00687  27 RLGFEVWAVNTVQFSNHTGYGKWTGQVLPPDELHELVEGLeAINKLNQCDAVLSGYLGSAEQVAMVVGIVRQVKQANPQA 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217338257 170 VYVCDPVLGDKWDGegsMYVPEDLLPVYKEKVVPLADIITPNQFEAELLSGRKIHSQEEALRVMDMLHSMGPDTVVITss 249
Cdd:TIGR00687 107 LYVCDPVMGDPWKG---CYVAPDLLEVYREKAIPVADIITPNQFELELLTGRRINTEEEALAAADALIAMGPDIVLVT-- 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217338257 250 dlpspqgsnYLIVLGSQRRRNPAGSVVMERIRMDIRKVDAVF----VGTGDLFAAMLLAwTHKHPNNLKVACEKTVSTLH 325
Cdd:TIGR00687 182 ---------HLIRAGSQRDRSFEGLVATQEGRWHISRPLAVFdpppVGTGDLIAALLLA-TLLHGNSLKEALEKTVSAVY 251

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 2217338257 326 HVLQRTIQCAKAQagegVRPSPMQLELRMVQSKRDIEDPE 365
Cdd:TIGR00687 252 HVLRTTIQLGKYE----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 ...
 91-365 4.29e-130

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: 374.17  E-value: 4.29e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217338257  91 VLGFEIDAVNSVQFSNHTGYAHWKGQVLNSDELQELYEGL-RLNNMNKYDYVLTGYTRDKSFLAMVVDIVQELKQQNPRL 169
Cdd:TIGR00687  27 RLGFEVWAVNTVQFSNHTGYGKWTGQVLPPDELHELVEGLeAINKLNQCDAVLSGYLGSAEQVAMVVGIVRQVKQANPQA 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217338257 170 VYVCDPVLGDKWDGegsMYVPEDLLPVYKEKVVPLADIITPNQFEAELLSGRKIHSQEEALRVMDMLHSMGPDTVVITss 249
Cdd:TIGR00687 107 LYVCDPVMGDPWKG---CYVAPDLLEVYREKAIPVADIITPNQFELELLTGRRINTEEEALAAADALIAMGPDIVLVT-- 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217338257 250 dlpspqgsnYLIVLGSQRRRNPAGSVVMERIRMDIRKVDAVF----VGTGDLFAAMLLAwTHKHPNNLKVACEKTVSTLH 325
Cdd:TIGR00687 182 ---------HLIRAGSQRDRSFEGLVATQEGRWHISRPLAVFdpppVGTGDLIAALLLA-TLLHGNSLKEALEKTVSAVY 251

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 2217338257 326 HVLQRTIQCAKAQagegVRPSPMQLELRMVQSKRDIEDPE 365
Cdd:TIGR00687 252 HVLRTTIQLGKYE----LQPVAAQLEIRMPQSKFDAEKVE 287
PLN02978 PLN02978
pyridoxal kinase
 91-371 7.63e-117

pyridoxal kinase


Pssm-ID: 215529 [Multi-domain]  Cd Length: 308  Bit Score: 341.33  E-value: 7.63e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217338257  91 VLGFEIDAVNSVQFSNHTGYAHWKGQVLNSDELQELYEGLRLNNMNKYDYVLTGYTRDKSFLAMVVDIVQELKQQNPRLV 170
Cdd:PLN02978   40 LLGFDVDPINSVQFSNHTGYPTFKGQVLDGEQLWALIEGLEANGLLFYTHLLTGYIGSVSFLRTVLRVVKKLRSVNPNLT 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217338257 171 YVCDPVLGDkwdgEGSMYVPEDLLPVYKEKVVPLADIITPNQFEAELLSGRKIHSQEEALRVMDMLHSMGPDTVVITSSD 250
Cdd:PLN02978  120 YVCDPVLGD----EGKLYVPPELVPVYREKVVPLATMLTPNQFEAEQLTGIRIVTEEDAREACAILHAAGPSKVVITSID 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217338257 251 LPspqgsNYLIVLGSQRRRNPAGSvvmERIRMDIRKVDAVFVGTGDLFAAMLLAWTHKHPNNLKVACEKTVSTLHHVLQR 330
Cdd:PLN02978  196 ID-----GKLLLVGSHRKEKGARP---EQFKIVIPKIPAYFTGTGDLMAALLLGWSHKYPDNLDKAAELAVSSLQAVLRR 267

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 2217338257 331 TIQCAKAqagEGVRPSPMQLELRMVQSKRDIEDPEIVVQAT 371
Cdd:PLN02978  268 TLADYKR---AGADPKSSSLELRLVQSQDDIRHPQVRFKAE 305
pyridoxal_pyridoxamine_kinase cd01173
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ...
 83-333 1.16e-97

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: 290.64  E-value: 1.16e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217338257  83 LISVSSQSV---------------LGFEIDAVNSVQFSNHTGYAHWKGQVLNSDELQELYEGLRLNNM-NKYDYVLTGYT 146
Cdd:cd01173     2 VLSIQSHVVhgyvgnsaavfplqrLGWDVDALPTVQFSNHTGYGTWTGFVLSAEELEDLLEGLEALGLlLEYDAVLTGYL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217338257 147 RDKSFLAMVVDIVQELKQQNPRLVYVCDPVLGDkwdgEGSMYV-PEDLLPVYKEKVVPLADIITPNQFEAELLSGRKIHS 225
Cdd:cd01173    82 GSAEQVEAVAEIVKRLKEKNPNLLYVCDPVMGD----NGKLYVvAEEIVPVYRDLLVPLADIITPNQFELELLTGKKIND 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217338257 226 QEEALRVMDMLHSMGPDTVVITSSDLPSPqgsnylivlgsqRRRNPAGSVVMERIRMDIRKVD--AVFVGTGDLFAAMLL 303
Cdd:cd01173   158 LEDAKAAARALHAKGPKTVVVTSVELADD------------DRIEMLGSTATEAWLVQRPKIPfpAYFNGTGDLFAALLL 225

                         250       260       270
                  ....*....|....*....|....*....|
gi 2217338257 304 AWTHKHPnNLKVACEKTVSTLHHVLQRTIQ 333
Cdd:cd01173   226 ARLLKGK-SLAEALEKALNFVHEVLEATYE 254
PdxK COG2240
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal ...
 84-333 6.47e-68

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: 215.01  E-value: 6.47e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217338257  84 ISVSSQSV---------------LGFEIDAVNSVQFSNHTGYAHWKGQVLNSDELQELYEGL-RLNNMNKYDYVLTGYTR 147
Cdd:COG2240     5 LSIQSHVVyghvgnsaavpplsaLGVEVWPLPTVLLSNHTGYGTFTGRDLPTDDIADILDGWkELGVLLEFDAVLSGYLG 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217338257 148 DKSFLAMVVDIVQELKQQNPRLVYVCDPVLGDkwDGEGsMYVPEDLLPVYKEKVVPLADIITPNQFEAELLSGRKIHSQE 227
Cdd:COG2240    85 SAEQGDIIADFVARVKAANPDALYLCDPVMGD--NGKG-YYVFPGIAEFIMRRLVPLADIITPNLTELALLTGRPYETLE 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217338257 228 EALRVMDMLHSMGPDTVVITS---SDLPSPQGSNYLIvlgsqrrrNPAGSVVMERirmdiRKVDAVFVGTGDLFAAMLLA 304
Cdd:COG2240   162 EALAAARALLALGPKIVVVTSvplDDTPADKIGNLAV--------TADGAWLVET-----PLLPFSPNGTGDLFAALLLA 228

                         250       260       270
                  ....*....|....*....|....*....|
gi 2217338257 305 -WTHKHPnnLKVACEKTVSTLHHVLQRTIQ 333
Cdd:COG2240   229 hLLRGKS--LEEALERAAAFVYEVLERTAA 256
Phos_pyr_kin pfam08543
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ...
 158-256 1.62e-16

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: 78.29  E-value: 1.62e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217338257 158 IVQELKQQNPRLVyvCDPVLGDKwdgEGSMYVPEDLLPVYKEKVVPLADIITPNQFEAELLSGRKIHSQEEALRVMDMLH 237
Cdd:pfam08543  78 VAEKLDKYGVPVV--LDPVMVAK---SGDSLLDDEAIEALKEELLPLATLITPNLPEAEALTGRKIKTLEDMKEAAKKLL 152

                          90
                  ....*....|....*....
gi 2217338257 238 SMGPDTVVITSSDLPSPQG 256
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 ...
 91-365 4.29e-130

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: 374.17  E-value: 4.29e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217338257  91 VLGFEIDAVNSVQFSNHTGYAHWKGQVLNSDELQELYEGL-RLNNMNKYDYVLTGYTRDKSFLAMVVDIVQELKQQNPRL 169
Cdd:TIGR00687  27 RLGFEVWAVNTVQFSNHTGYGKWTGQVLPPDELHELVEGLeAINKLNQCDAVLSGYLGSAEQVAMVVGIVRQVKQANPQA 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217338257 170 VYVCDPVLGDKWDGegsMYVPEDLLPVYKEKVVPLADIITPNQFEAELLSGRKIHSQEEALRVMDMLHSMGPDTVVITss 249
Cdd:TIGR00687 107 LYVCDPVMGDPWKG---CYVAPDLLEVYREKAIPVADIITPNQFELELLTGRRINTEEEALAAADALIAMGPDIVLVT-- 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217338257 250 dlpspqgsnYLIVLGSQRRRNPAGSVVMERIRMDIRKVDAVF----VGTGDLFAAMLLAwTHKHPNNLKVACEKTVSTLH 325
Cdd:TIGR00687 182 ---------HLIRAGSQRDRSFEGLVATQEGRWHISRPLAVFdpppVGTGDLIAALLLA-TLLHGNSLKEALEKTVSAVY 251

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 2217338257 326 HVLQRTIQCAKAQagegVRPSPMQLELRMVQSKRDIEDPE 365
Cdd:TIGR00687 252 HVLRTTIQLGKYE----LQPVAAQLEIRMPQSKFDAEKVE 287
PLN02978 PLN02978
pyridoxal kinase
 91-371 7.63e-117

pyridoxal kinase


Pssm-ID: 215529 [Multi-domain]  Cd Length: 308  Bit Score: 341.33  E-value: 7.63e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217338257  91 VLGFEIDAVNSVQFSNHTGYAHWKGQVLNSDELQELYEGLRLNNMNKYDYVLTGYTRDKSFLAMVVDIVQELKQQNPRLV 170
Cdd:PLN02978   40 LLGFDVDPINSVQFSNHTGYPTFKGQVLDGEQLWALIEGLEANGLLFYTHLLTGYIGSVSFLRTVLRVVKKLRSVNPNLT 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217338257 171 YVCDPVLGDkwdgEGSMYVPEDLLPVYKEKVVPLADIITPNQFEAELLSGRKIHSQEEALRVMDMLHSMGPDTVVITSSD 250
Cdd:PLN02978  120 YVCDPVLGD----EGKLYVPPELVPVYREKVVPLATMLTPNQFEAEQLTGIRIVTEEDAREACAILHAAGPSKVVITSID 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217338257 251 LPspqgsNYLIVLGSQRRRNPAGSvvmERIRMDIRKVDAVFVGTGDLFAAMLLAWTHKHPNNLKVACEKTVSTLHHVLQR 330
Cdd:PLN02978  196 ID-----GKLLLVGSHRKEKGARP---EQFKIVIPKIPAYFTGTGDLMAALLLGWSHKYPDNLDKAAELAVSSLQAVLRR 267

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 2217338257 331 TIQCAKAqagEGVRPSPMQLELRMVQSKRDIEDPEIVVQAT 371
Cdd:PLN02978  268 TLADYKR---AGADPKSSSLELRLVQSQDDIRHPQVRFKAE 305
PTZ00344 PTZ00344
pyridoxal kinase; Provisional
 91-373 3.23e-100

pyridoxal kinase; Provisional


Pssm-ID: 240372 [Multi-domain]  Cd Length: 296  Bit Score: 298.53  E-value: 3.23e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217338257  91 VLGFEIDAVNSVQFSNHTGYAHWKGQVLNSDELQELYEGLRLNNM-NKYDYVLTGYTRDKSFLAMVVDIVQELKQQNPRL 169
Cdd:PTZ00344   30 LLGFDVDFVNTVQLSNHTGYPVIKGHRLDLNELITLMDGLRANNLlSDYTYVLTGYINSADILREVLATVKEIKELRPKL 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217338257 170 VYVCDPVLGDkwdgEGSMYVPEDLLPVYKEkVVPLADIITPNQFEAELLSGRKIHSQEEALRVMDMLHSMGPDTVVITSS 249
Cdd:PTZ00344  110 IFLCDPVMGD----DGKLYVKEEVVDAYRE-LIPYADVITPNQFEASLLSGVEVKDLSDALEAIDWFHEQGIPVVVITSF 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217338257 250 DLpsPQGSNYLIVLGSQRRRNPAGSvvmERIRMDIRKVDAVFVGTGDLFAAMLLAWTHKHPnnLKVACEKTVSTLHHVLQ 329
Cdd:PTZ00344  185 RE--DEDPTHLRFLLSCRDKDTKNN---KRFTGKVPYIEGRYTGTGDLFAALLLAFSHQHP--MDLAVGKAMGVLQDIIK 257

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 2217338257 330 RTIqcakaQAGEGVRPSPMQLELRMVQSKRDIEDPEIVVQATVL 373
Cdd:PTZ00344  258 ATR-----ESGGSGSSSLMSRELRLIQSPRDLLNPETVFKVTPL 296
pyridoxal_pyridoxamine_kinase cd01173
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ...
 83-333 1.16e-97

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: 290.64  E-value: 1.16e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217338257  83 LISVSSQSV---------------LGFEIDAVNSVQFSNHTGYAHWKGQVLNSDELQELYEGLRLNNM-NKYDYVLTGYT 146
Cdd:cd01173     2 VLSIQSHVVhgyvgnsaavfplqrLGWDVDALPTVQFSNHTGYGTWTGFVLSAEELEDLLEGLEALGLlLEYDAVLTGYL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217338257 147 RDKSFLAMVVDIVQELKQQNPRLVYVCDPVLGDkwdgEGSMYV-PEDLLPVYKEKVVPLADIITPNQFEAELLSGRKIHS 225
Cdd:cd01173    82 GSAEQVEAVAEIVKRLKEKNPNLLYVCDPVMGD----NGKLYVvAEEIVPVYRDLLVPLADIITPNQFELELLTGKKIND 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217338257 226 QEEALRVMDMLHSMGPDTVVITSSDLPSPqgsnylivlgsqRRRNPAGSVVMERIRMDIRKVD--AVFVGTGDLFAAMLL 303
Cdd:cd01173   158 LEDAKAAARALHAKGPKTVVVTSVELADD------------DRIEMLGSTATEAWLVQRPKIPfpAYFNGTGDLFAALLL 225

                         250       260       270
                  ....*....|....*....|....*....|
gi 2217338257 304 AWTHKHPnNLKVACEKTVSTLHHVLQRTIQ 333
Cdd:cd01173   226 ARLLKGK-SLAEALEKALNFVHEVLEATYE 254
PdxK COG2240
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal ...
 84-333 6.47e-68

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: 215.01  E-value: 6.47e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217338257  84 ISVSSQSV---------------LGFEIDAVNSVQFSNHTGYAHWKGQVLNSDELQELYEGL-RLNNMNKYDYVLTGYTR 147
Cdd:COG2240     5 LSIQSHVVyghvgnsaavpplsaLGVEVWPLPTVLLSNHTGYGTFTGRDLPTDDIADILDGWkELGVLLEFDAVLSGYLG 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217338257 148 DKSFLAMVVDIVQELKQQNPRLVYVCDPVLGDkwDGEGsMYVPEDLLPVYKEKVVPLADIITPNQFEAELLSGRKIHSQE 227
Cdd:COG2240    85 SAEQGDIIADFVARVKAANPDALYLCDPVMGD--NGKG-YYVFPGIAEFIMRRLVPLADIITPNLTELALLTGRPYETLE 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217338257 228 EALRVMDMLHSMGPDTVVITS---SDLPSPQGSNYLIvlgsqrrrNPAGSVVMERirmdiRKVDAVFVGTGDLFAAMLLA 304
Cdd:COG2240   162 EALAAARALLALGPKIVVVTSvplDDTPADKIGNLAV--------TADGAWLVET-----PLLPFSPNGTGDLFAALLLA 228

                         250       260       270
                  ....*....|....*....|....*....|
gi 2217338257 305 -WTHKHPnnLKVACEKTVSTLHHVLQRTIQ 333
Cdd:COG2240   229 hLLRGKS--LEEALERAAAFVYEVLERTAA 256
PRK05756 PRK05756
pyridoxal kinase PdxY;
92-373 3.66e-58

pyridoxal kinase PdxY;


Pssm-ID: 235592 [Multi-domain]  Cd Length: 286  Bit Score: 190.47  E-value: 3.66e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217338257  92 LGFEIDAVNSVQFSNHTGYAHWKGQVLNSDELQELYEGL-RLNNMNKYDYVLTGYTRDKSFLAMVVDIVQELKQQNPRLV 170
Cdd:PRK05756   28 LGVNVWPLNTVQFSNHTGYGKWTGCVMPPSHLTEIVQGIaDIGWLGECDAVLSGYLGSAEQGEAILDAVRRVKAANPQAL 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217338257 171 YVCDPVLGDKwdgEGSMYVPEDLLPVYKEKVVPLADIITPNQFEAELLSGRKIHSQEEALRVMDMLHSMGPDTVVITSSD 250
Cdd:PRK05756  108 YFCDPVMGDP---EKGCIVAPGVAEFLRDRALPAADIITPNLFELEWLSGRPVETLEDAVAAARALIARGPKIVLVTSLA 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217338257 251 LP-SPQGSNYLIVLgsqrrrNPAGSVVMERIRMDIRKVDavfVGTGDLFAAMLLAWtHKHPNNLKVACEKTVSTLHHVLQ 329
Cdd:PRK05756  185 RAgYPADRFEMLLV------TADGAWHISRPLVDFMRQP---VGVGDLTSALFLAR-LLQGGSLEEALEHTTAAVYEVMA 254

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 2217338257 330 RTIQCakaqageGVRpspmqlELRMVQSKRDIEDPEIVVQATVL 373
Cdd:PRK05756  255 RTKER-------GSY------ELQLVAAQDSIATPRAMFQARRL 285
pdxK PRK08176
pyridoxine/pyridoxal/pyridoxamine kinase;
84-334 6.03e-26

pyridoxine/pyridoxal/pyridoxamine kinase;


Pssm-ID: 181269 [Multi-domain]  Cd Length: 281  Bit Score: 105.12  E-value: 6.03e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217338257  84 ISVSSQSV---------------LGFEIDAVNSVQFSNHTGYAHWKGQVLNSD----ELQELYE--GLRlnnmnKYDYVL 142
Cdd:PRK08176   19 VAVQSQVVygsvgnsiavpaikaNGLRVFAVPTVLLSNTPHYPTFYGGAIPDEwfsgYLRALQErdALR-----QLRAVT 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217338257 143 TGYTRDKSFLAMVVDIVQELKQQNPRLVYVCDPVLGDkwDGEGsMYVPEDLLPVYKEKVVPLADIITPNQFEAELLSGRK 222
Cdd:PRK08176   94 TGYMGSASQIKILAEWLTALRADHPDLLIMVDPVIGD--IDSG-IYVKPDLPEAYRQHLLPLAQGLTPNIFELEILTGKP 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217338257 223 IHSQEEALRVMDMLHSMGPDTVVITSSDLPSPQGS-NYLIVLGSQRrrnpagsVVMERIRmdirkVDAVFVGTGDLFAAM 301
Cdd:PRK08176  171 CRTLDSAIAAAKSLLSDTLKWVVITSAAGNEENQEmQVVVVTADSV-------NVISHPR-----VDTDLKGTGDLFCAE 238

                         250       260       270
                  ....*....|....*....|....*....|....
gi 2217338257 302 LLA-WTHKHPnnLKVACEKTVSTLHHVLQRTIQC 334
Cdd:PRK08176  239 LVSgLLKGKA--LTDAAHRAGLRVLEVMRYTQQA 270
ribokinase_pfkB_like cd00287
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ...
 138-305 9.32e-20

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: 85.99  E-value: 9.32e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217338257 138 YDYVLTGYTRDKsfLAMVVDIVQELKQQNPRlvYVCDPVLGDK-WDGEGsmyvpedllpvyKEKVVPLADIITPNQFEAE 216
Cdd:cd00287    58 ADAVVISGLSPA--PEAVLDALEEARRRGVP--VVLDPGPRAVrLDGEE------------LEKLLPGVDILTPNEEEAE 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217338257 217 LLSGRKIHSQEEALRVMDMLHSMGPDTVVITssdlpspQGSNYLIVLGSQRRRNPAGSVvmerirmdirKVDAV-FVGTG 295
Cdd:cd00287   122 ALTGRRDLEVKEAAEAAALLLSKGPKVVIVT-------LGEKGAIVATRGGTEVHVPAF----------PVKVVdTTGAG 184

                         170
                  ....*....|
gi 2217338257 296 DLFAAMLLAW 305
Cdd:cd00287   185 DAFLAALAAG 194
ThiD COG0351
Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; ...
 153-300 9.40e-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: 84.70  E-value: 9.40e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217338257 153 AMVVDIVQELKQQNprlvYVCDPVLGDKWDGEGSmyvPEDLLPVYKEKVVPLADIITPNQFEAELLSGRKIHSQEEALRV 232
Cdd:COG0351    82 EAVAEILADYPLVP----VVLDPVMVAKSGDRLL---DEDAVEALRELLLPLATVVTPNLPEAEALLGIEITTLDDMREA 154

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217338257 233 MDMLHSMGPDTVVITSSDLPSPQGSNYLiVLGSQRRRnpagsVVMERIRmdirkvDAVFVGTGDLFAA 300
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 ...
 158-256 1.62e-16

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: 78.29  E-value: 1.62e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217338257 158 IVQELKQQNPRLVyvCDPVLGDKwdgEGSMYVPEDLLPVYKEKVVPLADIITPNQFEAELLSGRKIHSQEEALRVMDMLH 237
Cdd:pfam08543  78 VAEKLDKYGVPVV--LDPVMVAK---SGDSLLDDEAIEALKEELLPLATLITPNLPEAEALTGRKIKTLEDMKEAAKKLL 152

                          90
                  ....*....|....*....
gi 2217338257 238 SMGPDTVVITSSDLPSPQG 256
Cdd:pfam08543 153 ALGAKAVLIKGGHLEGEEA 171
PRK06427 PRK06427
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed
 155-304 2.04e-13

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


Pssm-ID: 180561 [Multi-domain]  Cd Length: 266  Bit Score: 69.38  E-value: 2.04e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217338257 155 VVDIVQELKQQNPRLVYVCDPVL----GDkwdgegsmyvP---EDLLPVYKEKVVPLADIITPNQFEAELLSGRKIHSQE 227
Cdd:PRK06427   87 IIETVAEALKRYPIPPVVLDPVMiaksGD----------PllaDDAVAALRERLLPLATLITPNLPEAEALTGLPIADTE 156

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217338257 228 EALRVM-DMLHSMGPDTVVITSS-DLPSPQGSNYLIvlgsqrrrNPAGSVVMERIRMDIRKVDavfvGTGDLFAAMLLA 304
Cdd:PRK06427  157 DEMKAAaRALHALGCKAVLIKGGhLLDGEESVDWLF--------DGEGEERFSAPRIPTKNTH----GTGCTLSAAIAA 223
PRK07105 PRK07105
pyridoxamine kinase; Validated
 90-331 6.29e-11

pyridoxamine kinase; Validated


Pssm-ID: 180840 [Multi-domain]  Cd Length: 284  Bit Score: 62.63  E-value: 6.29e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217338257  90 SVLGFEIDAVNSVQFSNHTGYAHWKGQVLNSDELQE-LYEGLRLNNmnKYDYVLTGY---TRDksflamvVDIVQELKQ- 164
Cdd:PRK07105   29 SSMGLQVCPLPTALLSSHTGGFQNPSIIDLTDGMQAfLTHWKSLNL--KFDAIYSGYlgsPRQ-------IQIVSDFIKy 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217338257 165 -QNPRLVYVCDPVLGDKwdgeGSMYVP--EDLLPVYKeKVVPLADIITPNQFEAELLSG---RKIHSQEEalRVMDMLH- 237
Cdd:PRK07105  100 fKKKDLLVVVDPVMGDN----GKLYQGfdQEMVEEMR-KLIQKADVITPNLTEACLLLDkpyLEKSYSEE--EIKQLLRk 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217338257 238 --SMGPDTVVITSSdlpsPQGSNYLIVLGSQRRRNpagsvvmERIRMDIRKVDAVFVGTGDLFAAMLLAWTHkHPNNLKV 315
Cdd:PRK07105  173 laDLGPKIVIITSV----PFEDGKIGVAYYDRATD-------RFWKVFCKYIPAHYPGTGDIFTSVITGSLL-QGDSLPI 240

                         250
                  ....*....|....*.
gi 2217338257 316 ACEKTVSTLHHVLQRT 331
Cdd:PRK07105  241 ALDRAVQFIEKGIRAT 256
PfkB pfam00294
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ...
 156-305 8.53e-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: 8.53e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217338257 156 VDIVQELKQQNPRLVYVCDPVLGDKWDgegsmyvpedLLPVYKEkVVPLADIITPNQFEAELLSGRKIHSQEEALRVMDM 235
Cdd:pfam00294 143 EATLEELIEAAKNGGTFDPNLLDPLGA----------AREALLE-LLPLADLLKPNEEELEALTGAKLDDIEEALAALHK 211

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217338257 236 LHSMGPDTVVITSsdlpSPQGSnyLIVLGSQRRRNPAgsvvmerirmdIRKVDAV-FVGTGDLFAAMLLAW 305
Cdd:pfam00294 212 LLAKGIKTVIVTL----GADGA--LVVEGDGEVHVPA-----------VPKVKVVdTTGAGDSFVGGFLAG 265
PRK11142 PRK11142
ribokinase; Provisional
 204-247 2.72e-10

ribokinase; Provisional


Pssm-ID: 236858 [Multi-domain]  Cd Length: 306  Bit Score: 60.65  E-value: 2.72e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2217338257 204 LADIITPNQFEAELLSGRKIHSQEEALRVMDMLHSMGPDTVVIT 247
Cdd:PRK11142  178 LVDIITPNETEAEKLTGIRVEDDDDAAKAAQVLHQKGIETVLIT 221
ribokinase cd01174
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ...
 199-304 3.39e-10

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: 3.39e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217338257 199 EKVVPLADIITPNQFEAELLSGRKIHSQEEALRVMDMLHSMGPDTVVITssdlpspqgsnylivLGSQrrrnpaGSVVM- 277
Cdd:cd01174   170 AELLALVDILVPNETEAALLTGIEVTDEEDAEKAARLLLAKGVKNVIVT---------------LGAK------GALLAs 228

                          90       100       110
                  ....*....|....*....|....*....|
gi 2217338257 278 --ERIRMDIRKVDAV-FVGTGDLFAAMLLA 304
Cdd:cd01174   229 ggEVEHVPAFKVKAVdTTGAGDTFIGALAA 258
PRK08573 PRK08573
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
172-267 6.24e-09

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 236297 [Multi-domain]  Cd Length: 448  Bit Score: 57.43  E-value: 6.24e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217338257 172 VCDPVLGDKwdgEGSMYVPEDLLPVYKEKVVPLADIITPNQFEAELLSGRKIHSQEEALRVMDMLH-SMGPDTVVITSSD 250
Cdd:PRK08573  101 VVDPVMIAK---SGAPLLREDAVDALIKRLLPLATVVTPNRPEAEKLTGMKIRSVEDARKAAKYIVeELGAEAVVVKGGH 177

                          90
                  ....*....|....*..
gi 2217338257 251 LPSPQGSNYLIVLGSQR 267
Cdd:PRK08573  178 LEGEEAVDVLYHNGTFR 194
RbsK COG0524
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ...
 141-304 1.63e-08

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: 1.63e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217338257 141 VLTGYT-RDKSFLAMVVDIVQELKQQNPRLVYvcDPVLGDKwdgegsmyVPEDLLPVYKEkVVPLADIITPNQFEAELLS 219
Cdd:COG0524   132 HLGGITlASEPPREALLAALEAARAAGVPVSL--DPNYRPA--------LWEPARELLRE-LLALVDILFPNEEEAELLT 200

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217338257 220 GrkIHSQEEALRVmdmLHSMGPDTVVITssdlpspqgsnylivLGSQrrrnpaGSVVM---ERIRMDIRKVDAVF-VGTG 295
Cdd:COG0524   201 G--ETDPEEAAAA---LLARGVKLVVVT---------------LGAE------GALLYtggEVVHVPAFPVEVVDtTGAG 254


                  ....*....
gi 2217338257 296 DLFAAMLLA 304
Cdd:COG0524   255 DAFAAGFLA 263
PRK12616 PRK12616
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
112-247 1.53e-07

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 183624  Cd Length: 270  Bit Score: 51.97  E-value: 1.53e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217338257 112 HWKGQVLNSD------ELQELYEGLRLNNMNkydyvlTGYTRDKSFLAMVVDIVQELKQQNprlvYVCDPVLGDKwdGEG 185
Cdd:PRK12616   49 SWDHQVFPIDtdtiraQLSTIVDGIGVDAMK------TGMLPTVDIIELAADTIKEKQLKN----VVIDPVMVCK--GAN 116

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217338257 186 SMYVPEDLlPVYKEKVVPLADIITPNQFEAELLSGR-KIHSQEEALRVMDMLHSMGPDTVVIT 247
Cdd:PRK12616  117 EVLYPEHA-EALREQLAPLATVITPNLFEAGQLSGMgEIKTVEQMKEAAKKIHELGAQYVVIT 178
PRK12413 PRK12413
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
200-246 1.59e-07

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 183513 [Multi-domain]  Cd Length: 253  Bit Score: 51.99  E-value: 1.59e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2217338257 200 KVVPLADIITPNQFEAELLSGRKIHSQEEALRVMDMLHSMGPDTVVI 246
Cdd:PRK12413  125 QFFPYVTVITPNLVEAELLSGKEIKTLEDMKEAAKKLYDLGAKAVVI 171
PLN02898 PLN02898
HMP-P kinase/thiamin-monophosphate pyrophosphorylase
 139-253 5.98e-07

HMP-P kinase/thiamin-monophosphate pyrophosphorylase


Pssm-ID: 215486 [Multi-domain]  Cd Length: 502  Bit Score: 51.31  E-value: 5.98e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217338257 139 DYVLTGYTRDKSFLAMVVDIVQELKQQNprlvYVCDPVLGDKwdgEGSMYVPEDLLPVYKEKVVPLADIITPNQFEAE-L 217
Cdd:PLN02898   80 DVVKTGMLPSAEIVKVLCQALKEFPVKA----LVVDPVMVST---SGDVLAGPSILSALREELLPLATIVTPNVKEASaL 152

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2217338257 218 LSGRKIHSqeealrVMDM------LHSMGPDTVVITSSDLPS 253
Cdd:PLN02898  153 LGGDPLET------VADMrsaakeLHKLGPRYVLVKGGHLPD 188
PRK12412 PRK12412
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
102-246 2.85e-06

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 183512 [Multi-domain]  Cd Length: 268  Bit Score: 48.43  E-value: 2.85e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217338257 102 VQFSNHTGYAHwkgQVLNSD------ELQELYEGLRLNNMNkydyvlTGYTRDKSFLAMVVDIVQELKQQNprlvYVCDP 175
Cdd:PRK12412   40 VTMDPHNGWAH---NVFPIPastlkpQLETTIEGVGVDALK------TGMLGSVEIIEMVAETIEKHNFKN----VVVDP 106

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217338257 176 VLGDKwdGEGSMYVPEDLLpVYKEKVVPLADIITPNQFEAELLSGRKIHSQEEALRVMDMLHSMGPDTVVI 246
Cdd:PRK12412  107 VMVCK--GADEALHPETND-CLRDVLVPKALVVTPNLFEAYQLSGVKINSLEDMKEAAKKIHALGAKYVLI 174
FruK COG1105
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
114-310 2.87e-06

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


Pssm-ID: 440722 [Multi-domain]  Cd Length: 304  Bit Score: 48.59  E-value: 2.87e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217338257 114 KGQVLNSDELQELYEGLRlNNMNKYDY-VLTGytrdkSFLAMV-----VDIVQELKQQNPRLVyvcdpvlgdkWDGEGsm 187
Cdd:COG1105   106 PGPEISEEELEALLERLE-ELLKEGDWvVLSG-----SLPPGVppdfyAELIRLARARGAKVV----------LDTSG-- 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217338257 188 yvpEDLLPVYKEKVvplaDIITPNQFEAELLSGRKIHSQEEALRVMDMLHSMGPDTVVITssdlpspqgsnylivLGSQr 267
Cdd:COG1105   168 ---EALKAALEAGP----DLIKPNLEELEELLGRPLETLEDIIAAARELLERGAENVVVS---------------LGAD- 224

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2217338257 268 rrnpaGSVVM---ERIRMDIRKVDAVF-VGTGD-LFAAMLLAWTHKHP 310
Cdd:COG1105   225 -----GALLVtedGVYRAKPPKVEVVStVGAGDsMVAGFLAGLARGLD 267
PTZ00347 PTZ00347
phosphomethylpyrimidine kinase; Provisional
 158-342 1.33e-05

phosphomethylpyrimidine kinase; Provisional


Pssm-ID: 240375 [Multi-domain]  Cd Length: 504  Bit Score: 46.88  E-value: 1.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217338257 158 IVQELKQqnprLVYVCDPVL----GDKWDGEGSMyvpEDLLPVYKEKVVPLADIITPNQFEAELLSGRK-IHSQEEALRV 232
Cdd:PTZ00347  317 VIEKLKN----LPMVVDPVLvatsGDDLVAQKNA---DDVLAMYKERIFPMATIITPNIPEAERILGRKeITGVYEARAA 389

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217338257 233 MDMLhsmgpdtvvitssdlpSPQGSNYLIVLGSQRRRNP--AGSVVMERIRMDIRKVDAVFV------GTGDLFAAMLLA 304
Cdd:PTZ00347  390 AQAL----------------AQYGSRYVLVKGGHDLIDPeaCRDVLYDREKDRFYEFTANRIatinthGTGCTLASAISS 453

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2217338257 305 WTHKHpNNLKVACEKTVSTLHHVLQRTIQCAKAQAGEG 342
Cdd:PTZ00347  454 FLARG-YTVPDAVERAIGYVHEAIVRSCGVPLGQGTNR 490
adenosine_kinase cd01168
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ...
 197-310 8.08e-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: 8.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217338257 197 YKE---KVVPLADIITPNQFEAELLSGRKI-HSQEEALRVMdmlhSMGPDTVVITssdlpspQGSNYLIVLgSQRRRNPA 272
Cdd:cd01168   190 FKEallELLPYVDILFGNEEEAEALAEAETtDDLEAALKLL----ALRCRIVVIT-------QGAKGAVVV-EGGEVYPV 257

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2217338257 273 GSVVMERIrmdirkVDAvfVGTGDLFAA-MLLAWTHKHP 310
Cdd:cd01168   258 PAIPVEKI------VDT--NGAGDAFAGgFLYGLVQGEP 288
KdgK cd01166
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ...
 190-304 2.45e-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: 2.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217338257 190 PEDLLPVYKEkVVPLADIITPNQFEAELLSGRKIHSQ-EEALRvmdmLHSMGPDTVVItssdlpspqgsnylivlgsqrR 268
Cdd:cd01166   172 AEEAREALEE-LLPYVDIVLPSEEEAEALLGDEDPTDaAERAL----ALALGVKAVVV---------------------K 225

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2217338257 269 RNPAGSVVM---ERIRMDIRKVDAV-FVGTGDLFAAMLLA 304
Cdd:cd01166   226 LGAEGALVYtggGRVFVPAYPVEVVdTTGAGDAFAAGFLA 265
 
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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