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Conserved domains on  [gi|145358598|ref|NP_198601|]
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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
 36-343 0e+00

pyridoxal kinase


:

Pssm-ID: 215529 [Multi-domain]  Cd Length: 308  Bit Score: 635.24  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145358598  36 TTPPVLSLALPSDTGRVLSIQSHTVQGYVGNKSAVFPLQLLGYDVDPINSVQFSNHTGYPTFKGQVLNGQQLCDLIEGLE 115
Cdd:PLN02978   1 MAPPVLSLALPSSTGRVLSIQSHTVHGYVGNKSAVFPLQLLGFDVDPINSVQFSNHTGYPTFKGQVLDGEQLWALIEGLE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145358598 116 ANDLLFYTHVLTGYIGSVSFLDTILEVINKLRSVNPNLTYVCDPVMGDEGKLYVPEELVHVYREKVVPLASMLTPNQFEA 195
Cdd:PLN02978  81 ANGLLFYTHLLTGYIGSVSFLRTVLRVVKKLRSVNPNLTYVCDPVLGDEGKLYVPPELVPVYREKVVPLATMLTPNQFEA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145358598 196 EKLTGLRINSEEDGREACAILHAAGPSKVVITSITIGGILLLIGSHQKEKGLKPEQFKILIHKIPAYFTGTGDLMTALLL 275
Cdd:PLN02978 161 EQLTGIRIVTEEDAREACAILHAAGPSKVVITSIDIDGKLLLVGSHRKEKGARPEQFKIVIPKIPAYFTGTGDLMAALLL 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145358598 276 GWSNKYPDNLDKAAELAVSTLQALLRRTLDDYKRAGYDPTSSSLEIRLIQSQEDIRNPKVELKAERYS 343
Cdd:PLN02978 241 GWSHKYPDNLDKAAELAVSSLQAVLRRTLADYKRAGADPKSSSLELRLVQSQDDIRHPQVRFKAERYS 308
 
Name Accession Description Interval E-value
PLN02978 PLN02978
pyridoxal kinase
 36-343 0e+00

pyridoxal kinase


Pssm-ID: 215529 [Multi-domain]  Cd Length: 308  Bit Score: 635.24  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145358598  36 TTPPVLSLALPSDTGRVLSIQSHTVQGYVGNKSAVFPLQLLGYDVDPINSVQFSNHTGYPTFKGQVLNGQQLCDLIEGLE 115
Cdd:PLN02978   1 MAPPVLSLALPSSTGRVLSIQSHTVHGYVGNKSAVFPLQLLGFDVDPINSVQFSNHTGYPTFKGQVLDGEQLWALIEGLE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145358598 116 ANDLLFYTHVLTGYIGSVSFLDTILEVINKLRSVNPNLTYVCDPVMGDEGKLYVPEELVHVYREKVVPLASMLTPNQFEA 195
Cdd:PLN02978  81 ANGLLFYTHLLTGYIGSVSFLRTVLRVVKKLRSVNPNLTYVCDPVLGDEGKLYVPPELVPVYREKVVPLATMLTPNQFEA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145358598 196 EKLTGLRINSEEDGREACAILHAAGPSKVVITSITIGGILLLIGSHQKEKGLKPEQFKILIHKIPAYFTGTGDLMTALLL 275
Cdd:PLN02978 161 EQLTGIRIVTEEDAREACAILHAAGPSKVVITSIDIDGKLLLVGSHRKEKGARPEQFKIVIPKIPAYFTGTGDLMAALLL 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145358598 276 GWSNKYPDNLDKAAELAVSTLQALLRRTLDDYKRAGYDPTSSSLEIRLIQSQEDIRNPKVELKAERYS 343
Cdd:PLN02978 241 GWSHKYPDNLDKAAELAVSSLQAVLRRTLADYKRAGADPKSSSLELRLVQSQDDIRHPQVRFKAERYS 308
pyridoxal_pyridoxamine_kinase cd01173
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ...
 51-305 6.86e-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: 6.86e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145358598  51 RVLSIQSHTVQGYVGNKSAVFPLQLLGYDVDPINSVQFSNHTGYPTFKGQVLNGQQLCDLIEGLEANDLL-FYTHVLTGY 129
Cdd:cd01173    1 RVLSIQSHVVHGYVGNSAAVFPLQRLGWDVDALPTVQFSNHTGYGTWTGFVLSAEELEDLLEGLEALGLLlEYDAVLTGY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145358598 130 IGSVSFLDTILEVINKLRSVNPNLTYVCDPVMGDEGKLYV-PEELVHVYREKVVPLASMLTPNQFEAEKLTGLRINSEED 208
Cdd:cd01173   81 LGSAEQVEAVAEIVKRLKEKNPNLLYVCDPVMGDNGKLYVvAEEIVPVYRDLLVPLADIITPNQFELELLTGKKINDLED 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145358598 209 GREACAILHAAGPSKVVITSITIG--GILLLIGSHQKEKGLkpeqFKILIHKIPAYFTGTGDLMTALLLGWSNKYPDnLD 286
Cdd:cd01173  161 AKAAARALHAKGPKTVVVTSVELAddDRIEMLGSTATEAWL----VQRPKIPFPAYFNGTGDLFAALLLARLLKGKS-LA 235

                        250
                 ....*....|....*....
gi 145358598 287 KAAELAVSTLQALLRRTLD 305
Cdd:cd01173  236 EALEKALNFVHEVLEATYE 254
PdxK COG2240
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal ...
 51-330 4.26e-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: 265.86  E-value: 4.26e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145358598  51 RVLSIQSHTVQGYVGNKSAVFPLQLLGYDVDPINSVQFSNHTGYPTFKGQVLNGQQLCDLIEGLEANDLLFYTH-VLTGY 129
Cdd:COG2240    3 RVLSIQSHVVYGHVGNSAAVPPLSALGVEVWPLPTVLLSNHTGYGTFTGRDLPTDDIADILDGWKELGVLLEFDaVLSGY 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145358598 130 IGSVSFLDTILEVINKLRSVNPNLTYVCDPVMGDEGKLY-VPEELVHVYREKVVPLASMLTPNQFEAEKLTGLRINSEED 208
Cdd:COG2240   83 LGSAEQGDIIADFVARVKAANPDALYLCDPVMGDNGKGYyVFPGIAEFIMRRLVPLADIITPNLTELALLTGRPYETLEE 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145358598 209 GREACAILHAAGPSKVVITSITIGGI------LLLIGshqkekglkPEQFKILIH-KIPAYFTGTGDLMTALLLGWSNKY 281
Cdd:COG2240  163 ALAAARALLALGPKIVVVTSVPLDDTpadkigNLAVT---------ADGAWLVETpLLPFSPNGTGDLFAALLLAHLLRG 233

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 145358598 282 pDNLDKAAELAVSTLQALLRRTLDdykrAGYDptssslEIRLIQSQEDI 330
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 ...
 51-341 1.32e-86

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: 1.32e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145358598   51 RVLSIQSHTVQGYVGNKSAVFPLQLLGYDVDPINSVQFSNHTGYPTFKGQVLNGQQLCDLIEGLEA-NDLLFYTHVLTGY 129
Cdd:TIGR00687   3 NVLSIQSHVVYGHVGNRAATFPLQRLGFEVWAVNTVQFSNHTGYGKWTGQVLPPDELHELVEGLEAiNKLNQCDAVLSGY 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145358598  130 IGSVSFLDTILEVINKLRSVNPNLTYVCDPVMGDEGK-LYVPEELVHVYREKVVPLASMLTPNQFEAEKLTGLRINSEED 208
Cdd:TIGR00687  83 LGSAEQVAMVVGIVRQVKQANPQALYVCDPVMGDPWKgCYVAPDLLEVYREKAIPVADIITPNQFELELLTGRRINTEEE 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145358598  209 GREACAILHAAGPSKVVITSITIGGillLIGSHQKEKGLKPEQFKILIHKIPAYF----TGTGDLMTALLLGwSNKYPDN 284
Cdd:TIGR00687 163 ALAAADALIAMGPDIVLVTHLIRAG---SQRDRSFEGLVATQEGRWHISRPLAVFdpppVGTGDLIAALLLA-TLLHGNS 238

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 145358598  285 LDKAAELAVSTLQALLRRTlddyKRAGydptssSLEIRLIQSQEDIRNPKVELKAER 341
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 ...
 127-227 6.20e-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: 81.76  E-value: 6.20e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145358598  127 TGYIGSVSFLDTILEVINKlrsvnPNLTYVCDPVM--GDEGKLyVPEELVHVYREKVVPLASMLTPNQFEAEKLTGLRIN 204
Cdd:pfam08543  66 TGMLGSAEIIEAVAEKLDK-----YGVPVVLDPVMvaKSGDSL-LDDEAIEALKEELLPLATLITPNLPEAEALTGRKIK 139

                          90       100
                  ....*....|....*....|...
gi 145358598  205 SEEDGREACAILHAAGPSKVVIT 227
Cdd:pfam08543 140 TLEDMKEAAKKLLALGAKAVLIK 162
 
Name Accession Description Interval E-value
PLN02978 PLN02978
pyridoxal kinase
 36-343 0e+00

pyridoxal kinase


Pssm-ID: 215529 [Multi-domain]  Cd Length: 308  Bit Score: 635.24  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145358598  36 TTPPVLSLALPSDTGRVLSIQSHTVQGYVGNKSAVFPLQLLGYDVDPINSVQFSNHTGYPTFKGQVLNGQQLCDLIEGLE 115
Cdd:PLN02978   1 MAPPVLSLALPSSTGRVLSIQSHTVHGYVGNKSAVFPLQLLGFDVDPINSVQFSNHTGYPTFKGQVLDGEQLWALIEGLE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145358598 116 ANDLLFYTHVLTGYIGSVSFLDTILEVINKLRSVNPNLTYVCDPVMGDEGKLYVPEELVHVYREKVVPLASMLTPNQFEA 195
Cdd:PLN02978  81 ANGLLFYTHLLTGYIGSVSFLRTVLRVVKKLRSVNPNLTYVCDPVLGDEGKLYVPPELVPVYREKVVPLATMLTPNQFEA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145358598 196 EKLTGLRINSEEDGREACAILHAAGPSKVVITSITIGGILLLIGSHQKEKGLKPEQFKILIHKIPAYFTGTGDLMTALLL 275
Cdd:PLN02978 161 EQLTGIRIVTEEDAREACAILHAAGPSKVVITSIDIDGKLLLVGSHRKEKGARPEQFKIVIPKIPAYFTGTGDLMAALLL 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145358598 276 GWSNKYPDNLDKAAELAVSTLQALLRRTLDDYKRAGYDPTSSSLEIRLIQSQEDIRNPKVELKAERYS 343
Cdd:PLN02978 241 GWSHKYPDNLDKAAELAVSSLQAVLRRTLADYKRAGADPKSSSLELRLVQSQDDIRHPQVRFKAERYS 308
PTZ00344 PTZ00344
pyridoxal kinase; Provisional
 47-333 1.04e-122

pyridoxal kinase; Provisional


Pssm-ID: 240372 [Multi-domain]  Cd Length: 296  Bit Score: 354.77  E-value: 1.04e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145358598  47 SDTGRVLSIQSHTVQGYVGNKSAVFPLQLLGYDVDPINSVQFSNHTGYPTFKGQVLNGQQLCDLIEGLEANDLLF-YTHV 125
Cdd:PTZ00344   2 SMEKKVLSIQSHVTHGYVGNRAATFPLQLLGFDVDFVNTVQLSNHTGYPVIKGHRLDLNELITLMDGLRANNLLSdYTYV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145358598 126 LTGYIGSVSFLDTILEVINKLRSVNPNLTYVCDPVMGDEGKLYVPEELVHVYREkVVPLASMLTPNQFEAEKLTGLRINS 205
Cdd:PTZ00344  82 LTGYINSADILREVLATVKEIKELRPKLIFLCDPVMGDDGKLYVKEEVVDAYRE-LIPYADVITPNQFEASLLSGVEVKD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145358598 206 EEDGREACAILHAAGPSKVVITSITIG---GILLLIGSHQKEKGLKPEQFKILIHKIPAYFTGTGDLMTALLLGWSNKYP 282
Cdd:PTZ00344 161 LSDALEAIDWFHEQGIPVVVITSFREDedpTHLRFLLSCRDKDTKNNKRFTGKVPYIEGRYTGTGDLFAALLLAFSHQHP 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 145358598 283 dnLDKAAELAVSTLQALLRRTlDDYKRAGyDPTSSSLEIRLIQSQEDIRNP 333
Cdd:PTZ00344 241 --MDLAVGKAMGVLQDIIKAT-RESGGSG-SSSLMSRELRLIQSPRDLLNP 287
pyridoxal_pyridoxamine_kinase cd01173
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ...
 51-305 6.86e-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: 6.86e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145358598  51 RVLSIQSHTVQGYVGNKSAVFPLQLLGYDVDPINSVQFSNHTGYPTFKGQVLNGQQLCDLIEGLEANDLL-FYTHVLTGY 129
Cdd:cd01173    1 RVLSIQSHVVHGYVGNSAAVFPLQRLGWDVDALPTVQFSNHTGYGTWTGFVLSAEELEDLLEGLEALGLLlEYDAVLTGY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145358598 130 IGSVSFLDTILEVINKLRSVNPNLTYVCDPVMGDEGKLYV-PEELVHVYREKVVPLASMLTPNQFEAEKLTGLRINSEED 208
Cdd:cd01173   81 LGSAEQVEAVAEIVKRLKEKNPNLLYVCDPVMGDNGKLYVvAEEIVPVYRDLLVPLADIITPNQFELELLTGKKINDLED 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145358598 209 GREACAILHAAGPSKVVITSITIG--GILLLIGSHQKEKGLkpeqFKILIHKIPAYFTGTGDLMTALLLGWSNKYPDnLD 286
Cdd:cd01173  161 AKAAARALHAKGPKTVVVTSVELAddDRIEMLGSTATEAWL----VQRPKIPFPAYFNGTGDLFAALLLARLLKGKS-LA 235

                        250
                 ....*....|....*....
gi 145358598 287 KAAELAVSTLQALLRRTLD 305
Cdd:cd01173  236 EALEKALNFVHEVLEATYE 254
PdxK COG2240
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal ...
 51-330 4.26e-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: 265.86  E-value: 4.26e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145358598  51 RVLSIQSHTVQGYVGNKSAVFPLQLLGYDVDPINSVQFSNHTGYPTFKGQVLNGQQLCDLIEGLEANDLLFYTH-VLTGY 129
Cdd:COG2240    3 RVLSIQSHVVYGHVGNSAAVPPLSALGVEVWPLPTVLLSNHTGYGTFTGRDLPTDDIADILDGWKELGVLLEFDaVLSGY 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145358598 130 IGSVSFLDTILEVINKLRSVNPNLTYVCDPVMGDEGKLY-VPEELVHVYREKVVPLASMLTPNQFEAEKLTGLRINSEED 208
Cdd:COG2240   83 LGSAEQGDIIADFVARVKAANPDALYLCDPVMGDNGKGYyVFPGIAEFIMRRLVPLADIITPNLTELALLTGRPYETLEE 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145358598 209 GREACAILHAAGPSKVVITSITIGGI------LLLIGshqkekglkPEQFKILIH-KIPAYFTGTGDLMTALLLGWSNKY 281
Cdd:COG2240  163 ALAAARALLALGPKIVVVTSVPLDDTpadkigNLAVT---------ADGAWLVETpLLPFSPNGTGDLFAALLLAHLLRG 233

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 145358598 282 pDNLDKAAELAVSTLQALLRRTLDdykrAGYDptssslEIRLIQSQEDI 330
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 ...
 51-341 1.32e-86

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: 1.32e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145358598   51 RVLSIQSHTVQGYVGNKSAVFPLQLLGYDVDPINSVQFSNHTGYPTFKGQVLNGQQLCDLIEGLEA-NDLLFYTHVLTGY 129
Cdd:TIGR00687   3 NVLSIQSHVVYGHVGNRAATFPLQRLGFEVWAVNTVQFSNHTGYGKWTGQVLPPDELHELVEGLEAiNKLNQCDAVLSGY 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145358598  130 IGSVSFLDTILEVINKLRSVNPNLTYVCDPVMGDEGK-LYVPEELVHVYREKVVPLASMLTPNQFEAEKLTGLRINSEED 208
Cdd:TIGR00687  83 LGSAEQVAMVVGIVRQVKQANPQALYVCDPVMGDPWKgCYVAPDLLEVYREKAIPVADIITPNQFELELLTGRRINTEEE 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145358598  209 GREACAILHAAGPSKVVITSITIGGillLIGSHQKEKGLKPEQFKILIHKIPAYF----TGTGDLMTALLLGwSNKYPDN 284
Cdd:TIGR00687 163 ALAAADALIAMGPDIVLVTHLIRAG---SQRDRSFEGLVATQEGRWHISRPLAVFdpppVGTGDLIAALLLA-TLLHGNS 238

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 145358598  285 LDKAAELAVSTLQALLRRTlddyKRAGydptssSLEIRLIQSQEDIRNPKVELKAER 341
Cdd:TIGR00687 239 LKEALEKTVSAVYHVLRTT----IQLG------KYELQPVAAQLEIRMPQSKFDAEK 285
PRK05756 PRK05756
pyridoxal kinase PdxY;
49-341 1.38e-79

pyridoxal kinase PdxY;


Pssm-ID: 235592 [Multi-domain]  Cd Length: 286  Bit Score: 244.39  E-value: 1.38e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145358598  49 TGRVLSIQSHTVQGYVGNKSAVFPLQLLGYDVDPINSVQFSNHTGYPTFKGQVLNGQQLCDLIEGLEANDLLFYTH-VLT 127
Cdd:PRK05756   1 MKNILSIQSHVVYGHVGNSAAVFPMQRLGVNVWPLNTVQFSNHTGYGKWTGCVMPPSHLTEIVQGIADIGWLGECDaVLS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145358598 128 GYIGSVSFLDTILEVINKLRSVNPNLTYVCDPVMGDEGK-LYVPEELVHVYREKVVPLASMLTPNQFEAEKLTGLRINSE 206
Cdd:PRK05756  81 GYLGSAEQGEAILDAVRRVKAANPQALYFCDPVMGDPEKgCIVAPGVAEFLRDRALPAADIITPNLFELEWLSGRPVETL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145358598 207 EDGREACAILHAAGPSKVVITSIT-----IGGILLLIGShqkekglkPEQFKILIH-KIPAYF--TGTGDLMTALLLGWS 278
Cdd:PRK05756 161 EDAVAAARALIARGPKIVLVTSLAragypADRFEMLLVT--------ADGAWHISRpLVDFMRqpVGVGDLTSALFLARL 232

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 145358598 279 NKyPDNLDKAAELAVSTLQALLRRTlddyKRAGydptssSLEIRLIQSQEDIRNPKVELKAER 341
Cdd:PRK05756 233 LQ-GGSLEEALEHTTAAVYEVMART----KERG------SYELQLVAAQDSIATPRAMFQARR 284
pdxK PRK08176
pyridoxine/pyridoxal/pyridoxamine kinase;
35-313 2.16e-39

pyridoxine/pyridoxal/pyridoxamine kinase;


Pssm-ID: 181269 [Multi-domain]  Cd Length: 281  Bit Score: 140.56  E-value: 2.16e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145358598  35 MTTPPVLSLALPSDtgrVLSIQSHTVQGYVGNKSAVFPLQLLGYDVDPINSVQFSNHTGYPTFKGQVLNGQQLCDLIEGL 114
Cdd:PRK08176   4 LLLFNDKSRALQAD---IVAVQSQVVYGSVGNSIAVPAIKANGLRVFAVPTVLLSNTPHYPTFYGGAIPDEWFSGYLRAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145358598 115 EANDLLFYTH-VLTGYIGSVSFLDTILEVINKLRSVNPNLTYVCDPVMGDEGK-LYVPEELVHVYREKVVPLASMLTPNQ 192
Cdd:PRK08176  81 QERDALRQLRaVTTGYMGSASQIKILAEWLTALRADHPDLLIMVDPVIGDIDSgIYVKPDLPEAYRQHLLPLAQGLTPNI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145358598 193 FEAEKLTGLRINSEEDGREACAILHAAGPSKVVITS----ITIGGILLLIGSHqkekglkpEQFKILIH-KIPAYFTGTG 267
Cdd:PRK08176 161 FELEILTGKPCRTLDSAIAAAKSLLSDTLKWVVITSaagnEENQEMQVVVVTA--------DSVNVISHpRVDTDLKGTG 232

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 145358598 268 DLMTA-----LLLGWSnkypdnLDKAAELAVSTLQALLRRTlddyKRAGYD 313
Cdd:PRK08176 233 DLFCAelvsgLLKGKA------LTDAAHRAGLRVLEVMRYT----QQAGSD 273
PRK07105 PRK07105
pyridoxamine kinase; Validated
 68-309 1.38e-23

pyridoxamine kinase; Validated


Pssm-ID: 180840 [Multi-domain]  Cd Length: 284  Bit Score: 98.45  E-value: 1.38e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145358598  68 SAVFP-LQLLGYDVDPINSVQFSNHT-GYPTFKGQvlngqqlcDLIEGLEAndllFYTH----------VLTGYIGSVSF 135
Cdd:PRK07105  22 TASIPiMSSMGLQVCPLPTALLSSHTgGFQNPSII--------DLTDGMQA----FLTHwkslnlkfdaIYSGYLGSPRQ 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145358598 136 LDTILEVINKLRsvNPNLTYVCDPVMGDEGKLYVP--EELVHVYReKVVPLASMLTPNQFEAEKLTG----LRINSEEDG 209
Cdd:PRK07105  90 IQIVSDFIKYFK--KKDLLVVVDPVMGDNGKLYQGfdQEMVEEMR-KLIQKADVITPNLTEACLLLDkpylEKSYSEEEI 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145358598 210 REACAILHAAGPSKVVITSITIGGILLLIGSHQKEKGlkpeQFKILIHK-IPAYFTGTGDLMTALLLGwSNKYPDNLDKA 288
Cdd:PRK07105 167 KQLLRKLADLGPKIVIITSVPFEDGKIGVAYYDRATD----RFWKVFCKyIPAHYPGTGDIFTSVITG-SLLQGDSLPIA 241

                        250       260
                 ....*....|....*....|.
gi 145358598 289 AELAVSTLQALLRRTLdDYKR 309
Cdd:PRK07105 242 LDRAVQFIEKGIRATL-GLKY 261
ThiD COG0351
Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; ...
 127-305 6.48e-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: 6.48e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145358598 127 TGYIGSVSFLDTILEVINKLRSVNpnltYVCDPVM----GDEGklyVPEELVHVYREKVVPLASMLTPNQFEAEKLTGLR 202
Cdd:COG0351   72 IGMLGSAEIIEAVAEILADYPLVP----VVLDPVMvaksGDRL---LDEDAVEALRELLLPLATVVTPNLPEAEALLGIE 144

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145358598 203 INSEEDGREACAILHAAGPSKVVITsitiGGIL-------LLIGshqkekglkPEQFKILIHK--IPAYFTGTGDL---- 269
Cdd:COG0351  145 ITTLDDMREAAKALLELGAKAVLVK----GGHLpgdeavdVLYD---------GDGVREFSAPriDTGNTHGTGCTlssa 211

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 145358598 270 MTALL-LGWSnkypdnLDKAAELAVSTLQALLRRTLD 305
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 ...
 127-227 6.20e-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: 81.76  E-value: 6.20e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145358598  127 TGYIGSVSFLDTILEVINKlrsvnPNLTYVCDPVM--GDEGKLyVPEELVHVYREKVVPLASMLTPNQFEAEKLTGLRIN 204
Cdd:pfam08543  66 TGMLGSAEIIEAVAEKLDK-----YGVPVVLDPVMvaKSGDSL-LDDEAIEALKEELLPLATLITPNLPEAEALTGRKIK 139

                          90       100
                  ....*....|....*....|...
gi 145358598  205 SEEDGREACAILHAAGPSKVVIT 227
Cdd:pfam08543 140 TLEDMKEAAKKLLALGAKAVLIK 162
PRK06427 PRK06427
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed
 127-236 5.38e-15

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


Pssm-ID: 180561 [Multi-domain]  Cd Length: 266  Bit Score: 74.01  E-value: 5.38e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145358598 127 TGYIGSVSFLDTILEVINKLRSVNpnltYVCDPVM----GDEGklyVPEELVHVYREKVVPLASMLTPNQFEAEKLTGLR 202
Cdd:PRK06427  79 IGMLASAEIIETVAEALKRYPIPP----VVLDPVMiaksGDPL---LADDAVAALRERLLPLATLITPNLPEAEALTGLP 151

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 145358598 203 INSEEDG-REACAILHAAGPSKVVITsitiGGILL 236
Cdd:PRK06427 152 IADTEDEmKAAARALHALGCKAVLIK----GGHLL 182
PRK08573 PRK08573
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
127-226 2.23e-14

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 236297 [Multi-domain]  Cd Length: 448  Bit Score: 73.61  E-value: 2.23e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145358598 127 TGYIGSVSFLDTILEVINKLrsvnpNLTYVCDPVM-GDEGKLYVPEELVHVYREKVVPLASMLTPNQFEAEKLTGLRINS 205
Cdd:PRK08573  77 TGMLSNREIIEAVAKTVSKY-----GFPLVVDPVMiAKSGAPLLREDAVDALIKRLLPLATVVTPNRPEAEKLTGMKIRS 151

                         90       100
                 ....*....|....*....|.
gi 145358598 206 EEDGREACAILHAAGPSKVVI 226
Cdd:PRK08573 152 VEDARKAAKYIVEELGAEAVV 172
PRK12412 PRK12412
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
105-226 1.06e-13

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 183512 [Multi-domain]  Cd Length: 268  Bit Score: 70.38  E-value: 1.06e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145358598 105 QQLCDLIEGLEANDLLfythvlTGYIGSVSFLDTILEVINKLRSVNpnltYVCDPVM---GDEGKLYvPEELVhVYREKV 181
Cdd:PRK12412  62 PQLETTIEGVGVDALK------TGMLGSVEIIEMVAETIEKHNFKN----VVVDPVMvckGADEALH-PETND-CLRDVL 129

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 145358598 182 VPLASMLTPNQFEAEKLTGLRINSEEDGREACAILHAAGPSKVVI 226
Cdd:PRK12412 130 VPKALVVTPNLFEAYQLSGVKINSLEDMKEAAKKIHALGAKYVLI 174
ribokinase_pfkB_like cd00287
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ...
 140-277 1.53e-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: 65.58  E-value: 1.53e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145358598 140 LEVINKLRSvnPNLTYVCDPVMGdeGKLYVPEELvhvyrEKVVPLASMLTPNQFEAEKLTGLRINSEEDGREACAILHAA 219
Cdd:cd00287   74 LDALEEARR--RGVPVVLDPGPR--AVRLDGEEL-----EKLLPGVDILTPNEEEAEALTGRRDLEVKEAAEAAALLLSK 144

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 145358598 220 GPSKVVITSITIGGILLLIGSHQKEKGLKPEQfkilihkiPAYFTGTGDLMTALLLGW 277
Cdd:cd00287  145 GPKVVIVTLGEKGAIVATRGGTEVHVPAFPVK--------VVDTTGAGDAFLAALAAG 194
PRK11142 PRK11142
ribokinase; Provisional
 187-276 1.09e-10

ribokinase; Provisional


Pssm-ID: 236858 [Multi-domain]  Cd Length: 306  Bit Score: 61.81  E-value: 1.09e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145358598 187 MLTPNQFEAEKLTGLRINSEEDGREACAILHAAGPSKVVitsITIG--GILLligSHQKEKGLKPeQFKI-LIHKIPAYF 263
Cdd:PRK11142 181 IITPNETEAEKLTGIRVEDDDDAAKAAQVLHQKGIETVL---ITLGsrGVWL---SENGEGQRVP-GFRVqAVDTIAAGD 253

                         90
                 ....*....|...
gi 145358598 264 TGTGDLMTALLLG 276
Cdd:PRK11142 254 TFNGALVTALLEG 266
PRK12616 PRK12616
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
80-243 2.92e-10

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 183624  Cd Length: 270  Bit Score: 60.06  E-value: 2.92e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145358598  80 VDPINSvqfSNHTGYPTFKGQVLngQQLCDLIEGLEANDLLfythvlTGYIGSVSFLDTILEVINKLRSVNpnltYVCDP 159
Cdd:PRK12616  44 MDPENS---WDHQVFPIDTDTIR--AQLSTIVDGIGVDAMK------TGMLPTVDIIELAADTIKEKQLKN----VVIDP 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145358598 160 VM---GDEGKLYvPEElVHVYREKVVPLASMLTPNQFEAEKLTGL-RINSEEDGREACAILHAAGPSKVVITSitiGGIL 235
Cdd:PRK12616 109 VMvckGANEVLY-PEH-AEALREQLAPLATVITPNLFEAGQLSGMgEIKTVEQMKEAAKKIHELGAQYVVITG---GGKL 183


                 ....*...
gi 145358598 236 lligSHQK 243
Cdd:PRK12616 184 ----KHEK 187
ribokinase cd01174
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ...
 178-227 4.73e-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: 4.73e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 145358598 178 REKVVPLASMLTPNQFEAEKLTGLRINSEEDGREACAILHAAGPSKVVIT 227
Cdd:cd01174  169 PAELLALVDILVPNETEAALLTGIEVTDEEDAEKAARLLLAKGVKNVIVT 218
PLN02898 PLN02898
HMP-P kinase/thiamin-monophosphate pyrophosphorylase
 125-226 5.08e-08

HMP-P kinase/thiamin-monophosphate pyrophosphorylase


Pssm-ID: 215486 [Multi-domain]  Cd Length: 502  Bit Score: 54.39  E-value: 5.08e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145358598 125 VLTGYIGSVSFLDTILEVINKLRSVNpnltYVCDPVM----GDEgkLYVPEELvHVYREKVVPLASMLTPNQFEAEKLTG 200
Cdd:PLN02898  82 VKTGMLPSAEIVKVLCQALKEFPVKA----LVVDPVMvstsGDV--LAGPSIL-SALREELLPLATIVTPNVKEASALLG 154

                         90       100
                 ....*....|....*....|....*..
gi 145358598 201 L-RINSEEDGREACAILHAAGPSKVVI 226
Cdd:PLN02898 155 GdPLETVADMRSAAKELHKLGPRYVLV 181
PfkB pfam00294
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ...
 114-293 2.50e-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: 51.57  E-value: 2.50e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145358598  114 LEANDLLfythVLTGYIGSVSFLDTILEVINKLRSVNPNLTYVCDPVMGDEGKLyvpeelvhvyrEKVVPLASMLTPNQF 193
Cdd:pfam00294 125 LENADLL----YISGSLPLGLPEATLEELIEAAKNGGTFDPNLLDPLGAAREAL-----------LELLPLADLLKPNEE 189

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145358598  194 EAEKLTGLRINSEEDGREACAILHAAGPSKVVITSITIGGILLLIGSHQKEKGLKPEQfkilihkiPAYFTGTGDLMTA- 272
Cdd:pfam00294 190 ELEALTGAKLDDIEEALAALHKLLAKGIKTVIVTLGADGALVVEGDGEVHVPAVPKVK--------VVDTTGAGDSFVGg 261

                         170       180
                  ....*....|....*....|.
gi 145358598  273 LLLGWSNKYPdnLDKAAELAV 293
Cdd:pfam00294 262 FLAGLLAGKS--LEEALRFAN 280
PRK12413 PRK12413
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
139-226 3.87e-07

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 183513 [Multi-domain]  Cd Length: 253  Bit Score: 50.45  E-value: 3.87e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145358598 139 ILEVINKLRSVNPNLTYVCDPVM-----GDEGKLYVPEELVhvyreKVVPLASMLTPNQFEAEKLTGLRINSEEDGREAC 213
Cdd:PRK12413  84 IAEQALDFIKGHPGIPVVLDPVLvcketHDVEVSELRQELI-----QFFPYVTVITPNLVEAELLSGKEIKTLEDMKEAA 158

                         90
                 ....*....|...
gi 145358598 214 AILHAAGPSKVVI 226
Cdd:PRK12413 159 KKLYDLGAKAVVI 171
RbsK COG0524
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ...
 136-293 6.43e-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: 6.43e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145358598 136 LDTILEVINKLRSvnPNLTYVCDPVMGDEGKLYVPEELvhvyrEKVVPLASMLTPNQFEAEKLTGlrinsEEDGREACAI 215
Cdd:COG0524  144 REALLAALEAARA--AGVPVSLDPNYRPALWEPARELL-----RELLALVDILFPNEEEAELLTG-----ETDPEEAAAA 211

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145358598 216 LHAAGPSKVVitsITIG--GILLLIGSHqkekglkpeqfkilIHKIPAYF------TGTGD-----LMTALLLGWSnkyp 282
Cdd:COG0524  212 LLARGVKLVV---VTLGaeGALLYTGGE--------------VVHVPAFPvevvdtTGAGDafaagFLAGLLEGLD---- 270

                        170
                 ....*....|.
gi 145358598 283 dnLDKAAELAV 293
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 ...
 188-297 1.19e-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: 49.23  E-value: 1.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145358598 188 LTPNQFEAEKLTGLRINSEEDGREACAILHAAGPSKVVitsITIG--GILLLIGSHQKEKGLKPEqfkILIHKIpAYFTG 265
Cdd:cd01941  180 LTPNRAELEALAGALIENNEDENKAAKILLLPGIKNVI---VTLGakGVLLSSREGGVETKLFPA---PQPETV-VNVTG 252

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 145358598 266 TGD-LMTALLLGWSNKYP--DNLDKAAELAVSTLQ 297
Cdd:cd01941  253 AGDaFVAGLVAGLLEGMSldDSLRFAQAAAALTLE 287
PTZ00347 PTZ00347
phosphomethylpyrimidine kinase; Provisional
 142-226 3.34e-04

phosphomethylpyrimidine kinase; Provisional


Pssm-ID: 240375 [Multi-domain]  Cd Length: 504  Bit Score: 42.26  E-value: 3.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145358598 142 VINKLRsvnpNLTYVCDPVM----GDE-GKLYVPEELVHVYREKVVPLASMLTPNQFEAEKLTGLR-INSEEDGREACAI 215
Cdd:PTZ00347 317 VIEKLK----NLPMVVDPVLvatsGDDlVAQKNADDVLAMYKERIFPMATIITPNIPEAERILGRKeITGVYEARAAAQA 392

                         90
                 ....*....|.
gi 145358598 216 LHAAGPSKVVI 226
Cdd:PTZ00347 393 LAQYGSRYVLV 403
 
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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