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Conserved domains on  [gi|1063734875|ref|NP_001331291|]
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pfkB-like carbohydrate kinase family protein [Arabidopsis thaliana]

Protein Classification

pyridoxal kinase( domain architecture ID 10010958)

pyridoxal kinase catalyzes the transfer of a phosphate group from ATP to the 5-hydroxylmethyl group of pyridoxal to form the biologically active pyridoxal phosphate, an active form of vitamin B6

CATH:  3.40.1190.20
EC:  2.7.1.35
Gene Ontology:  GO:0005524|GO:0046872|GO:0008478|GO:0009443|GO:0008615
PubMed:  8382990|7748903|15581583|8690703|15189147|17109392
SCOP:  4000759

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02978 PLN02978
pyridoxal kinase
 2-309 0e+00

pyridoxal kinase


:

Pssm-ID: 215529 [Multi-domain]  Cd Length: 308  Bit Score: 634.47  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734875   2 TTPPVLSLALPSDTGRVLSIQSHTVQGYVGNKSAVFPLQLLGYDVDPINSVQFSNHTGYPTFKGQVLNGQQLCDLIEGLE 81
Cdd:PLN02978    1 MAPPVLSLALPSSTGRVLSIQSHTVHGYVGNKSAVFPLQLLGFDVDPINSVQFSNHTGYPTFKGQVLDGEQLWALIEGLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734875  82 ANDLLFYTHVLTGYIGSVSFLDTILEVINKLRSVNPNLTYVCDPVMGDEGKLYVPEELVHVYREKVVPLASMLTPNQFEA 161
Cdd:PLN02978   81 ANGLLFYTHLLTGYIGSVSFLRTVLRVVKKLRSVNPNLTYVCDPVLGDEGKLYVPPELVPVYREKVVPLATMLTPNQFEA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734875 162 EKLTGLRINSEEDGREACAILHAAGPSKVVITSITIGGILLLIGSHQKEKGLKPEQFKILIHKIPAYFTGTGDLMTALLL 241
Cdd:PLN02978  161 EQLTGIRIVTEEDAREACAILHAAGPSKVVITSIDIDGKLLLVGSHRKEKGARPEQFKIVIPKIPAYFTGTGDLMAALLL 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063734875 242 GWSNKYPDNLDKAAELAVSTLQALLRRTLDDYKRAGYDPTSSSLEIRLIQSQEDIRNPKVELKAERYS 309
Cdd:PLN02978  241 GWSHKYPDNLDKAAELAVSSLQAVLRRTLADYKRAGADPKSSSLELRLVQSQDDIRHPQVRFKAERYS 308
 
Name Accession Description Interval E-value
PLN02978 PLN02978
pyridoxal kinase
 2-309 0e+00

pyridoxal kinase


Pssm-ID: 215529 [Multi-domain]  Cd Length: 308  Bit Score: 634.47  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734875   2 TTPPVLSLALPSDTGRVLSIQSHTVQGYVGNKSAVFPLQLLGYDVDPINSVQFSNHTGYPTFKGQVLNGQQLCDLIEGLE 81
Cdd:PLN02978    1 MAPPVLSLALPSSTGRVLSIQSHTVHGYVGNKSAVFPLQLLGFDVDPINSVQFSNHTGYPTFKGQVLDGEQLWALIEGLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734875  82 ANDLLFYTHVLTGYIGSVSFLDTILEVINKLRSVNPNLTYVCDPVMGDEGKLYVPEELVHVYREKVVPLASMLTPNQFEA 161
Cdd:PLN02978   81 ANGLLFYTHLLTGYIGSVSFLRTVLRVVKKLRSVNPNLTYVCDPVLGDEGKLYVPPELVPVYREKVVPLATMLTPNQFEA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734875 162 EKLTGLRINSEEDGREACAILHAAGPSKVVITSITIGGILLLIGSHQKEKGLKPEQFKILIHKIPAYFTGTGDLMTALLL 241
Cdd:PLN02978  161 EQLTGIRIVTEEDAREACAILHAAGPSKVVITSIDIDGKLLLVGSHRKEKGARPEQFKIVIPKIPAYFTGTGDLMAALLL 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063734875 242 GWSNKYPDNLDKAAELAVSTLQALLRRTLDDYKRAGYDPTSSSLEIRLIQSQEDIRNPKVELKAERYS 309
Cdd:PLN02978  241 GWSHKYPDNLDKAAELAVSSLQAVLRRTLADYKRAGADPKSSSLELRLVQSQDDIRHPQVRFKAERYS 308
pyridoxal_pyridoxamine_kinase cd01173
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ...
 17-271 2.75e-115

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: 333.01  E-value: 2.75e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734875  17 RVLSIQSHTVQGYVGNKSAVFPLQLLGYDVDPINSVQFSNHTGYPTFKGQVLNGQQLCDLIEGLEANDLL-FYTHVLTGY 95
Cdd:cd01173     1 RVLSIQSHVVHGYVGNSAAVFPLQRLGWDVDALPTVQFSNHTGYGTWTGFVLSAEELEDLLEGLEALGLLlEYDAVLTGY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734875  96 IGSVSFLDTILEVINKLRSVNPNLTYVCDPVMGDEGKLYV-PEELVHVYREKVVPLASMLTPNQFEAEKLTGLRINSEED 174
Cdd:cd01173    81 LGSAEQVEAVAEIVKRLKEKNPNLLYVCDPVMGDNGKLYVvAEEIVPVYRDLLVPLADIITPNQFELELLTGKKINDLED 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734875 175 GREACAILHAAGPSKVVITSITIG--GILLLIGSHQKEKGLkpeqFKILIHKIPAYFTGTGDLMTALLLGWSNKYPDnLD 252
Cdd:cd01173   161 AKAAARALHAKGPKTVVVTSVELAddDRIEMLGSTATEAWL----VQRPKIPFPAYFNGTGDLFAALLLARLLKGKS-LA 235

                         250
                  ....*....|....*....
gi 1063734875 253 KAAELAVSTLQALLRRTLD 271
Cdd:cd01173   236 EALEKALNFVHEVLEATYE 254
PdxK COG2240
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal ...
 17-296 1.83e-88

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: 265.47  E-value: 1.83e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734875  17 RVLSIQSHTVQGYVGNKSAVFPLQLLGYDVDPINSVQFSNHTGYPTFKGQVLNGQQLCDLIEGLEANDLLFYTH-VLTGY 95
Cdd:COG2240     3 RVLSIQSHVVYGHVGNSAAVPPLSALGVEVWPLPTVLLSNHTGYGTFTGRDLPTDDIADILDGWKELGVLLEFDaVLSGY 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734875  96 IGSVSFLDTILEVINKLRSVNPNLTYVCDPVMGDEGKLY-VPEELVHVYREKVVPLASMLTPNQFEAEKLTGLRINSEED 174
Cdd:COG2240    83 LGSAEQGDIIADFVARVKAANPDALYLCDPVMGDNGKGYyVFPGIAEFIMRRLVPLADIITPNLTELALLTGRPYETLEE 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734875 175 GREACAILHAAGPSKVVITSITIGGI------LLLIGshqkekglkPEQFKILIH-KIPAYFTGTGDLMTALLLGWSNKY 247
Cdd:COG2240   163 ALAAARALLALGPKIVVVTSVPLDDTpadkigNLAVT---------ADGAWLVETpLLPFSPNGTGDLFAALLLAHLLRG 233

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1063734875 248 pDNLDKAAELAVSTLQALLRRTLDdykrAGYDptssslEIRLIQSQEDI 296
Cdd:COG2240   234 -KSLEEALERAAAFVYEVLERTAA----AGSD------ELLLEAALDEL 271
pyridox_kin TIGR00687
pyridoxal kinase; E. coli has an enzyme PdxK that acts in vitro as a pyridoxine/pyridoxal ...
 17-307 4.11e-87

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: 262.46  E-value: 4.11e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734875  17 RVLSIQSHTVQGYVGNKSAVFPLQLLGYDVDPINSVQFSNHTGYPTFKGQVLNGQQLCDLIEGLEA-NDLLFYTHVLTGY 95
Cdd:TIGR00687   3 NVLSIQSHVVYGHVGNRAATFPLQRLGFEVWAVNTVQFSNHTGYGKWTGQVLPPDELHELVEGLEAiNKLNQCDAVLSGY 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734875  96 IGSVSFLDTILEVINKLRSVNPNLTYVCDPVMGDEGK-LYVPEELVHVYREKVVPLASMLTPNQFEAEKLTGLRINSEED 174
Cdd:TIGR00687  83 LGSAEQVAMVVGIVRQVKQANPQALYVCDPVMGDPWKgCYVAPDLLEVYREKAIPVADIITPNQFELELLTGRRINTEEE 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734875 175 GREACAILHAAGPSKVVITSITIGGillLIGSHQKEKGLKPEQFKILIHKIPAYF----TGTGDLMTALLLGwSNKYPDN 250
Cdd:TIGR00687 163 ALAAADALIAMGPDIVLVTHLIRAG---SQRDRSFEGLVATQEGRWHISRPLAVFdpppVGTGDLIAALLLA-TLLHGNS 238

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1063734875 251 LDKAAELAVSTLQALLRRTlddyKRAGydptssSLEIRLIQSQEDIRNPKVELKAER 307
Cdd:TIGR00687 239 LKEALEKTVSAVYHVLRTT----IQLG------KYELQPVAAQLEIRMPQSKFDAEK 285
Phos_pyr_kin pfam08543
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ...
 93-193 5.20e-18

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: 81.37  E-value: 5.20e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734875  93 TGYIGSVSFLDTILEVINKlrsvnPNLTYVCDPVM--GDEGKLyVPEELVHVYREKVVPLASMLTPNQFEAEKLTGLRIN 170
Cdd:pfam08543  66 TGMLGSAEIIEAVAEKLDK-----YGVPVVLDPVMvaKSGDSL-LDDEAIEALKEELLPLATLITPNLPEAEALTGRKIK 139

                          90       100
                  ....*....|....*....|...
gi 1063734875 171 SEEDGREACAILHAAGPSKVVIT 193
Cdd:pfam08543 140 TLEDMKEAAKKLLALGAKAVLIK 162
 
Name Accession Description Interval E-value
PLN02978 PLN02978
pyridoxal kinase
 2-309 0e+00

pyridoxal kinase


Pssm-ID: 215529 [Multi-domain]  Cd Length: 308  Bit Score: 634.47  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734875   2 TTPPVLSLALPSDTGRVLSIQSHTVQGYVGNKSAVFPLQLLGYDVDPINSVQFSNHTGYPTFKGQVLNGQQLCDLIEGLE 81
Cdd:PLN02978    1 MAPPVLSLALPSSTGRVLSIQSHTVHGYVGNKSAVFPLQLLGFDVDPINSVQFSNHTGYPTFKGQVLDGEQLWALIEGLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734875  82 ANDLLFYTHVLTGYIGSVSFLDTILEVINKLRSVNPNLTYVCDPVMGDEGKLYVPEELVHVYREKVVPLASMLTPNQFEA 161
Cdd:PLN02978   81 ANGLLFYTHLLTGYIGSVSFLRTVLRVVKKLRSVNPNLTYVCDPVLGDEGKLYVPPELVPVYREKVVPLATMLTPNQFEA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734875 162 EKLTGLRINSEEDGREACAILHAAGPSKVVITSITIGGILLLIGSHQKEKGLKPEQFKILIHKIPAYFTGTGDLMTALLL 241
Cdd:PLN02978  161 EQLTGIRIVTEEDAREACAILHAAGPSKVVITSIDIDGKLLLVGSHRKEKGARPEQFKIVIPKIPAYFTGTGDLMAALLL 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063734875 242 GWSNKYPDNLDKAAELAVSTLQALLRRTLDDYKRAGYDPTSSSLEIRLIQSQEDIRNPKVELKAERYS 309
Cdd:PLN02978  241 GWSHKYPDNLDKAAELAVSSLQAVLRRTLADYKRAGADPKSSSLELRLVQSQDDIRHPQVRFKAERYS 308
PTZ00344 PTZ00344
pyridoxal kinase; Provisional
 13-299 2.29e-123

pyridoxal kinase; Provisional


Pssm-ID: 240372 [Multi-domain]  Cd Length: 296  Bit Score: 355.16  E-value: 2.29e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734875  13 SDTGRVLSIQSHTVQGYVGNKSAVFPLQLLGYDVDPINSVQFSNHTGYPTFKGQVLNGQQLCDLIEGLEANDLLF-YTHV 91
Cdd:PTZ00344    2 SMEKKVLSIQSHVTHGYVGNRAATFPLQLLGFDVDFVNTVQLSNHTGYPVIKGHRLDLNELITLMDGLRANNLLSdYTYV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734875  92 LTGYIGSVSFLDTILEVINKLRSVNPNLTYVCDPVMGDEGKLYVPEELVHVYREkVVPLASMLTPNQFEAEKLTGLRINS 171
Cdd:PTZ00344   82 LTGYINSADILREVLATVKEIKELRPKLIFLCDPVMGDDGKLYVKEEVVDAYRE-LIPYADVITPNQFEASLLSGVEVKD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734875 172 EEDGREACAILHAAGPSKVVITSITIG----GILLLIGSHQKEKGlKPEQFKILIHKIPAYFTGTGDLMTALLLGWSNKY 247
Cdd:PTZ00344  161 LSDALEAIDWFHEQGIPVVVITSFREDedptHLRFLLSCRDKDTK-NNKRFTGKVPYIEGRYTGTGDLFAALLLAFSHQH 239

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1063734875 248 PdnLDKAAELAVSTLQALLRRTlDDYKRAGyDPTSSSLEIRLIQSQEDIRNP 299
Cdd:PTZ00344  240 P--MDLAVGKAMGVLQDIIKAT-RESGGSG-SSSLMSRELRLIQSPRDLLNP 287
pyridoxal_pyridoxamine_kinase cd01173
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ...
 17-271 2.75e-115

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: 333.01  E-value: 2.75e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734875  17 RVLSIQSHTVQGYVGNKSAVFPLQLLGYDVDPINSVQFSNHTGYPTFKGQVLNGQQLCDLIEGLEANDLL-FYTHVLTGY 95
Cdd:cd01173     1 RVLSIQSHVVHGYVGNSAAVFPLQRLGWDVDALPTVQFSNHTGYGTWTGFVLSAEELEDLLEGLEALGLLlEYDAVLTGY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734875  96 IGSVSFLDTILEVINKLRSVNPNLTYVCDPVMGDEGKLYV-PEELVHVYREKVVPLASMLTPNQFEAEKLTGLRINSEED 174
Cdd:cd01173    81 LGSAEQVEAVAEIVKRLKEKNPNLLYVCDPVMGDNGKLYVvAEEIVPVYRDLLVPLADIITPNQFELELLTGKKINDLED 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734875 175 GREACAILHAAGPSKVVITSITIG--GILLLIGSHQKEKGLkpeqFKILIHKIPAYFTGTGDLMTALLLGWSNKYPDnLD 252
Cdd:cd01173   161 AKAAARALHAKGPKTVVVTSVELAddDRIEMLGSTATEAWL----VQRPKIPFPAYFNGTGDLFAALLLARLLKGKS-LA 235

                         250
                  ....*....|....*....
gi 1063734875 253 KAAELAVSTLQALLRRTLD 271
Cdd:cd01173   236 EALEKALNFVHEVLEATYE 254
PdxK COG2240
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal ...
 17-296 1.83e-88

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: 265.47  E-value: 1.83e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734875  17 RVLSIQSHTVQGYVGNKSAVFPLQLLGYDVDPINSVQFSNHTGYPTFKGQVLNGQQLCDLIEGLEANDLLFYTH-VLTGY 95
Cdd:COG2240     3 RVLSIQSHVVYGHVGNSAAVPPLSALGVEVWPLPTVLLSNHTGYGTFTGRDLPTDDIADILDGWKELGVLLEFDaVLSGY 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734875  96 IGSVSFLDTILEVINKLRSVNPNLTYVCDPVMGDEGKLY-VPEELVHVYREKVVPLASMLTPNQFEAEKLTGLRINSEED 174
Cdd:COG2240    83 LGSAEQGDIIADFVARVKAANPDALYLCDPVMGDNGKGYyVFPGIAEFIMRRLVPLADIITPNLTELALLTGRPYETLEE 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734875 175 GREACAILHAAGPSKVVITSITIGGI------LLLIGshqkekglkPEQFKILIH-KIPAYFTGTGDLMTALLLGWSNKY 247
Cdd:COG2240   163 ALAAARALLALGPKIVVVTSVPLDDTpadkigNLAVT---------ADGAWLVETpLLPFSPNGTGDLFAALLLAHLLRG 233

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1063734875 248 pDNLDKAAELAVSTLQALLRRTLDdykrAGYDptssslEIRLIQSQEDI 296
Cdd:COG2240   234 -KSLEEALERAAAFVYEVLERTAA----AGSD------ELLLEAALDEL 271
pyridox_kin TIGR00687
pyridoxal kinase; E. coli has an enzyme PdxK that acts in vitro as a pyridoxine/pyridoxal ...
 17-307 4.11e-87

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: 262.46  E-value: 4.11e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734875  17 RVLSIQSHTVQGYVGNKSAVFPLQLLGYDVDPINSVQFSNHTGYPTFKGQVLNGQQLCDLIEGLEA-NDLLFYTHVLTGY 95
Cdd:TIGR00687   3 NVLSIQSHVVYGHVGNRAATFPLQRLGFEVWAVNTVQFSNHTGYGKWTGQVLPPDELHELVEGLEAiNKLNQCDAVLSGY 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734875  96 IGSVSFLDTILEVINKLRSVNPNLTYVCDPVMGDEGK-LYVPEELVHVYREKVVPLASMLTPNQFEAEKLTGLRINSEED 174
Cdd:TIGR00687  83 LGSAEQVAMVVGIVRQVKQANPQALYVCDPVMGDPWKgCYVAPDLLEVYREKAIPVADIITPNQFELELLTGRRINTEEE 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734875 175 GREACAILHAAGPSKVVITSITIGGillLIGSHQKEKGLKPEQFKILIHKIPAYF----TGTGDLMTALLLGwSNKYPDN 250
Cdd:TIGR00687 163 ALAAADALIAMGPDIVLVTHLIRAG---SQRDRSFEGLVATQEGRWHISRPLAVFdpppVGTGDLIAALLLA-TLLHGNS 238

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1063734875 251 LDKAAELAVSTLQALLRRTlddyKRAGydptssSLEIRLIQSQEDIRNPKVELKAER 307
Cdd:TIGR00687 239 LKEALEKTVSAVYHVLRTT----IQLG------KYELQPVAAQLEIRMPQSKFDAEK 285
PRK05756 PRK05756
pyridoxal kinase PdxY;
15-307 4.40e-80

pyridoxal kinase PdxY;


Pssm-ID: 235592 [Multi-domain]  Cd Length: 286  Bit Score: 244.39  E-value: 4.40e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734875  15 TGRVLSIQSHTVQGYVGNKSAVFPLQLLGYDVDPINSVQFSNHTGYPTFKGQVLNGQQLCDLIEGLEANDLLFYTH-VLT 93
Cdd:PRK05756    1 MKNILSIQSHVVYGHVGNSAAVFPMQRLGVNVWPLNTVQFSNHTGYGKWTGCVMPPSHLTEIVQGIADIGWLGECDaVLS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734875  94 GYIGSVSFLDTILEVINKLRSVNPNLTYVCDPVMGDEGK-LYVPEELVHVYREKVVPLASMLTPNQFEAEKLTGLRINSE 172
Cdd:PRK05756   81 GYLGSAEQGEAILDAVRRVKAANPQALYFCDPVMGDPEKgCIVAPGVAEFLRDRALPAADIITPNLFELEWLSGRPVETL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734875 173 EDGREACAILHAAGPSKVVITSIT-----IGGILLLIGShqkekglkPEQFKILIH-KIPAYF--TGTGDLMTALLLGWS 244
Cdd:PRK05756  161 EDAVAAARALIARGPKIVLVTSLAragypADRFEMLLVT--------ADGAWHISRpLVDFMRqpVGVGDLTSALFLARL 232

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063734875 245 NKyPDNLDKAAELAVSTLQALLRRTlddyKRAGydptssSLEIRLIQSQEDIRNPKVELKAER 307
Cdd:PRK05756  233 LQ-GGSLEEALEHTTAAVYEVMART----KERG------SYELQLVAAQDSIATPRAMFQARR 284
pdxK PRK08176
pyridoxine/pyridoxal/pyridoxamine kinase;
1-279 1.61e-39

pyridoxine/pyridoxal/pyridoxamine kinase;


Pssm-ID: 181269 [Multi-domain]  Cd Length: 281  Bit Score: 139.79  E-value: 1.61e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734875   1 MTTPPVLSLALPSDtgrVLSIQSHTVQGYVGNKSAVFPLQLLGYDVDPINSVQFSNHTGYPTFKGQVLNGQQLCDLIEGL 80
Cdd:PRK08176    4 LLLFNDKSRALQAD---IVAVQSQVVYGSVGNSIAVPAIKANGLRVFAVPTVLLSNTPHYPTFYGGAIPDEWFSGYLRAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734875  81 EANDLLFYTH-VLTGYIGSVSFLDTILEVINKLRSVNPNLTYVCDPVMGDEGK-LYVPEELVHVYREKVVPLASMLTPNQ 158
Cdd:PRK08176   81 QERDALRQLRaVTTGYMGSASQIKILAEWLTALRADHPDLLIMVDPVIGDIDSgIYVKPDLPEAYRQHLLPLAQGLTPNI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734875 159 FEAEKLTGLRINSEEDGREACAILHAAGPSKVVITS----ITIGGILLLIGSHqkekglkpEQFKILIH-KIPAYFTGTG 233
Cdd:PRK08176  161 FELEILTGKPCRTLDSAIAAAKSLLSDTLKWVVITSaagnEENQEMQVVVVTA--------DSVNVISHpRVDTDLKGTG 232

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1063734875 234 DLMTA-----LLLGWSnkypdnLDKAAELAVSTLQALLRRTlddyKRAGYD 279
Cdd:PRK08176  233 DLFCAelvsgLLKGKA------LTDAAHRAGLRVLEVMRYT----QQAGSD 273
PRK07105 PRK07105
pyridoxamine kinase; Validated
 34-275 7.90e-24

pyridoxamine kinase; Validated


Pssm-ID: 180840 [Multi-domain]  Cd Length: 284  Bit Score: 98.06  E-value: 7.90e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734875  34 SAVFP-LQLLGYDVDPINSVQFSNHT-GYPTFKGQvlngqqlcDLIEGLEAndllFYTH----------VLTGYIGSVSF 101
Cdd:PRK07105   22 TASIPiMSSMGLQVCPLPTALLSSHTgGFQNPSII--------DLTDGMQA----FLTHwkslnlkfdaIYSGYLGSPRQ 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734875 102 LDTILEVINKLRsvNPNLTYVCDPVMGDEGKLYVP--EELVHVYReKVVPLASMLTPNQFEAEKLTG----LRINSEEDG 175
Cdd:PRK07105   90 IQIVSDFIKYFK--KKDLLVVVDPVMGDNGKLYQGfdQEMVEEMR-KLIQKADVITPNLTEACLLLDkpylEKSYSEEEI 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734875 176 REACAILHAAGPSKVVITSITIGGILLLIGSHQKEKGlkpeQFKILIHK-IPAYFTGTGDLMTALLLGwSNKYPDNLDKA 254
Cdd:PRK07105  167 KQLLRKLADLGPKIVIITSVPFEDGKIGVAYYDRATD----RFWKVFCKyIPAHYPGTGDIFTSVITG-SLLQGDSLPIA 241

                         250       260
                  ....*....|....*....|.
gi 1063734875 255 AELAVSTLQALLRRTLdDYKR 275
Cdd:PRK07105  242 LDRAVQFIEKGIRATL-GLKY 261
ThiD COG0351
Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; ...
 93-271 5.22e-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: 84.32  E-value: 5.22e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734875  93 TGYIGSVSFLDTILEVINKLRSVNpnltYVCDPVM----GDEGklyVPEELVHVYREKVVPLASMLTPNQFEAEKLTGLR 168
Cdd:COG0351    72 IGMLGSAEIIEAVAEILADYPLVP----VVLDPVMvaksGDRL---LDEDAVEALRELLLPLATVVTPNLPEAEALLGIE 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734875 169 INSEEDGREACAILHAAGPSKVVITsitiGGIL-------LLIGshqkekglkPEQFKILIHK--IPAYFTGTGDL---- 235
Cdd:COG0351   145 ITTLDDMREAAKALLELGAKAVLVK----GGHLpgdeavdVLYD---------GDGVREFSAPriDTGNTHGTGCTlssa 211

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1063734875 236 MTALL-LGWSnkypdnLDKAAELAVSTLQALLRRTLD 271
Cdd:COG0351   212 IAALLaKGLD------LEEAVREAKEYVTQAIRAALR 242
Phos_pyr_kin pfam08543
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ...
 93-193 5.20e-18

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: 81.37  E-value: 5.20e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734875  93 TGYIGSVSFLDTILEVINKlrsvnPNLTYVCDPVM--GDEGKLyVPEELVHVYREKVVPLASMLTPNQFEAEKLTGLRIN 170
Cdd:pfam08543  66 TGMLGSAEIIEAVAEKLDK-----YGVPVVLDPVMvaKSGDSL-LDDEAIEALKEELLPLATLITPNLPEAEALTGRKIK 139

                          90       100
                  ....*....|....*....|...
gi 1063734875 171 SEEDGREACAILHAAGPSKVVIT 193
Cdd:pfam08543 140 TLEDMKEAAKKLLALGAKAVLIK 162
PRK06427 PRK06427
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed
 93-202 4.26e-15

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


Pssm-ID: 180561 [Multi-domain]  Cd Length: 266  Bit Score: 73.62  E-value: 4.26e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734875  93 TGYIGSVSFLDTILEVINKLRSVNpnltYVCDPVM----GDEGklyVPEELVHVYREKVVPLASMLTPNQFEAEKLTGLR 168
Cdd:PRK06427   79 IGMLASAEIIETVAEALKRYPIPP----VVLDPVMiaksGDPL---LADDAVAALRERLLPLATLITPNLPEAEALTGLP 151

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1063734875 169 INSEEDG-REACAILHAAGPSKVVITsitiGGILL 202
Cdd:PRK06427  152 IADTEDEmKAAARALHALGCKAVLIK----GGHLL 182
PRK08573 PRK08573
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
93-192 1.47e-14

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 236297 [Multi-domain]  Cd Length: 448  Bit Score: 73.61  E-value: 1.47e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734875  93 TGYIGSVSFLDTILEVINKLrsvnpNLTYVCDPVM-GDEGKLYVPEELVHVYREKVVPLASMLTPNQFEAEKLTGLRINS 171
Cdd:PRK08573   77 TGMLSNREIIEAVAKTVSKY-----GFPLVVDPVMiAKSGAPLLREDAVDALIKRLLPLATVVTPNRPEAEKLTGMKIRS 151

                          90       100
                  ....*....|....*....|.
gi 1063734875 172 EEDGREACAILHAAGPSKVVI 192
Cdd:PRK08573  152 VEDARKAAKYIVEELGAEAVV 172
PRK12412 PRK12412
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
71-192 8.86e-14

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 183512 [Multi-domain]  Cd Length: 268  Bit Score: 70.00  E-value: 8.86e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734875  71 QQLCDLIEGLEANDLLfythvlTGYIGSVSFLDTILEVINKLRSVNpnltYVCDPVM---GDEGKLYvPEELVhVYREKV 147
Cdd:PRK12412   62 PQLETTIEGVGVDALK------TGMLGSVEIIEMVAETIEKHNFKN----VVVDPVMvckGADEALH-PETND-CLRDVL 129

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1063734875 148 VPLASMLTPNQFEAEKLTGLRINSEEDGREACAILHAAGPSKVVI 192
Cdd:PRK12412  130 VPKALVVTPNLFEAYQLSGVKINSLEDMKEAAKKIHALGAKYVLI 174
ribokinase_pfkB_like cd00287
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ...
 106-243 1.73e-12

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: 65.19  E-value: 1.73e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734875 106 LEVINKLRSvnPNLTYVCDPVMGdeGKLYVPEELvhvyrEKVVPLASMLTPNQFEAEKLTGLRINSEEDGREACAILHAA 185
Cdd:cd00287    74 LDALEEARR--RGVPVVLDPGPR--AVRLDGEEL-----EKLLPGVDILTPNEEEAEALTGRRDLEVKEAAEAAALLLSK 144

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1063734875 186 GPSKVVITSITIGGILLLIGSHQKEKGLKPEQfkilihkiPAYFTGTGDLMTALLLGW 243
Cdd:cd00287   145 GPKVVIVTLGEKGAIVATRGGTEVHVPAFPVK--------VVDTTGAGDAFLAALAAG 194
PRK11142 PRK11142
ribokinase; Provisional
 153-242 8.29e-11

ribokinase; Provisional


Pssm-ID: 236858 [Multi-domain]  Cd Length: 306  Bit Score: 61.81  E-value: 8.29e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734875 153 MLTPNQFEAEKLTGLRINSEEDGREACAILHAAGPSKVVitsITIG--GILLligSHQKEKGLKPeQFKI-LIHKIPAYF 229
Cdd:PRK11142  181 IITPNETEAEKLTGIRVEDDDDAAKAAQVLHQKGIETVL---ITLGsrGVWL---SENGEGQRVP-GFRVqAVDTIAAGD 253

                          90
                  ....*....|...
gi 1063734875 230 TGTGDLMTALLLG 242
Cdd:PRK11142  254 TFNGALVTALLEG 266
PRK12616 PRK12616
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
46-209 2.27e-10

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 183624  Cd Length: 270  Bit Score: 60.06  E-value: 2.27e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734875  46 VDPINSvqfSNHTGYPTFKGQVLngQQLCDLIEGLEANDLLfythvlTGYIGSVSFLDTILEVINKLRSVNpnltYVCDP 125
Cdd:PRK12616   44 MDPENS---WDHQVFPIDTDTIR--AQLSTIVDGIGVDAMK------TGMLPTVDIIELAADTIKEKQLKN----VVIDP 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734875 126 VM---GDEGKLYvPEElVHVYREKVVPLASMLTPNQFEAEKLTGL-RINSEEDGREACAILHAAGPSKVVITSitiGGIL 201
Cdd:PRK12616  109 VMvckGANEVLY-PEH-AEALREQLAPLATVITPNLFEAGQLSGMgEIKTVEQMKEAAKKIHELGAQYVVITG---GGKL 183


                  ....*...
gi 1063734875 202 lligSHQK 209
Cdd:PRK12616  184 ----KHEK 187
ribokinase cd01174
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ...
 144-193 3.78e-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: 53.71  E-value: 3.78e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1063734875 144 REKVVPLASMLTPNQFEAEKLTGLRINSEEDGREACAILHAAGPSKVVIT 193
Cdd:cd01174   169 PAELLALVDILVPNETEAALLTGIEVTDEEDAEKAARLLLAKGVKNVIVT 218
PLN02898 PLN02898
HMP-P kinase/thiamin-monophosphate pyrophosphorylase
 91-192 3.88e-08

HMP-P kinase/thiamin-monophosphate pyrophosphorylase


Pssm-ID: 215486 [Multi-domain]  Cd Length: 502  Bit Score: 54.39  E-value: 3.88e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734875  91 VLTGYIGSVSFLDTILEVINKLRSVNpnltYVCDPVM----GDEgkLYVPEELvHVYREKVVPLASMLTPNQFEAEKLTG 166
Cdd:PLN02898   82 VKTGMLPSAEIVKVLCQALKEFPVKA----LVVDPVMvstsGDV--LAGPSIL-SALREELLPLATIVTPNVKEASALLG 154

                          90       100
                  ....*....|....*....|....*..
gi 1063734875 167 L-RINSEEDGREACAILHAAGPSKVVI 192
Cdd:PLN02898  155 GdPLETVADMRSAAKELHKLGPRYVLV 181
PfkB pfam00294
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ...
 80-259 2.42e-07

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


Pssm-ID: 425587 [Multi-domain]  Cd Length: 294  Bit Score: 51.19  E-value: 2.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734875  80 LEANDLLfythVLTGYIGSVSFLDTILEVINKLRSVNPNLTYVCDPVMGDEGKLyvpeelvhvyrEKVVPLASMLTPNQF 159
Cdd:pfam00294 125 LENADLL----YISGSLPLGLPEATLEELIEAAKNGGTFDPNLLDPLGAAREAL-----------LELLPLADLLKPNEE 189

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734875 160 EAEKLTGLRINSEEDGREACAILHAAGPSKVVITSITIGGILLLIGSHQKEKGLKPEQfkilihkiPAYFTGTGDLMTA- 238
Cdd:pfam00294 190 ELEALTGAKLDDIEEALAALHKLLAKGIKTVIVTLGADGALVVEGDGEVHVPAVPKVK--------VVDTTGAGDSFVGg 261

                         170       180
                  ....*....|....*....|.
gi 1063734875 239 LLLGWSNKYPdnLDKAAELAV 259
Cdd:pfam00294 262 FLAGLLAGKS--LEEALRFAN 280
PRK12413 PRK12413
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
105-192 3.46e-07

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 183513 [Multi-domain]  Cd Length: 253  Bit Score: 50.45  E-value: 3.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734875 105 ILEVINKLRSVNPNLTYVCDPVM-----GDEGKLYVPEELVhvyreKVVPLASMLTPNQFEAEKLTGLRINSEEDGREAC 179
Cdd:PRK12413   84 IAEQALDFIKGHPGIPVVLDPVLvcketHDVEVSELRQELI-----QFFPYVTVITPNLVEAELLSGKEIKTLEDMKEAA 158

                          90
                  ....*....|...
gi 1063734875 180 AILHAAGPSKVVI 192
Cdd:PRK12413  159 KKLYDLGAKAVVI 171
RbsK COG0524
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ...
 102-259 5.20e-07

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: 50.27  E-value: 5.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734875 102 LDTILEVINKLRSvnPNLTYVCDPVMGDEGKLYVPEELvhvyrEKVVPLASMLTPNQFEAEKLTGlrinsEEDGREACAI 181
Cdd:COG0524   144 REALLAALEAARA--AGVPVSLDPNYRPALWEPARELL-----RELLALVDILFPNEEEAELLTG-----ETDPEEAAAA 211

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734875 182 LHAAGPSKVVitsITIG--GILLLIGSHqkekglkpeqfkilIHKIPAYF------TGTGD-----LMTALLLGWSnkyp 248
Cdd:COG0524   212 LLARGVKLVV---VTLGaeGALLYTGGE--------------VVHVPAFPvevvdtTGAGDafaagFLAGLLEGLD---- 270

                         170
                  ....*....|.
gi 1063734875 249 dnLDKAAELAV 259
Cdd:COG0524   271 --LEEALRFAN 279
YeiC_kinase_like cd01941
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ...
 154-263 1.24e-06

YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ribokinase/pfkB sugar kinase superfamily. Its oligomerization state is unknown at this time.


Pssm-ID: 238916 [Multi-domain]  Cd Length: 288  Bit Score: 48.85  E-value: 1.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734875 154 LTPNQFEAEKLTGLRINSEEDGREACAILHAAGPSKVVitsITIG--GILLLIGSHQKEKGLKPEqfkILIHKIpAYFTG 231
Cdd:cd01941   180 LTPNRAELEALAGALIENNEDENKAAKILLLPGIKNVI---VTLGakGVLLSSREGGVETKLFPA---PQPETV-VNVTG 252

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1063734875 232 TGD-LMTALLLGWSNKYP--DNLDKAAELAVSTLQ 263
Cdd:cd01941   253 AGDaFVAGLVAGLLEGMSldDSLRFAQAAAALTLE 287
PTZ00347 PTZ00347
phosphomethylpyrimidine kinase; Provisional
 108-192 2.92e-04

phosphomethylpyrimidine kinase; Provisional


Pssm-ID: 240375 [Multi-domain]  Cd Length: 504  Bit Score: 42.26  E-value: 2.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734875 108 VINKLRsvnpNLTYVCDPVM----GDE-GKLYVPEELVHVYREKVVPLASMLTPNQFEAEKLTGLR-INSEEDGREACAI 181
Cdd:PTZ00347  317 VIEKLK----NLPMVVDPVLvatsGDDlVAQKNADDVLAMYKERIFPMATIITPNIPEAERILGRKeITGVYEARAAAQA 392

                          90
                  ....*....|.
gi 1063734875 182 LHAAGPSKVVI 192
Cdd:PTZ00347  393 LAQYGSRYVLV 403
FruK COG1105
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
156-259 4.86e-03

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


Pssm-ID: 440722 [Multi-domain]  Cd Length: 304  Bit Score: 38.19  E-value: 4.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734875 156 PNQFEAEKLTGLRINSEEDGREACAILHAAGpSKVVITSITIGGILLLIGShqkekglkpEQFKILIHKIPAYFT-GTGD 234
Cdd:COG1105   183 PNLEELEELLGRPLETLEDIIAAARELLERG-AENVVVSLGADGALLVTED---------GVYRAKPPKVEVVSTvGAGD 252

                          90       100
                  ....*....|....*....|....*.
gi 1063734875 235 LMTA-LLLGWSNKYPdnLDKAAELAV 259
Cdd:COG1105   253 SMVAgFLAGLARGLD--LEEALRLAV 276
 
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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