|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05756 |
PRK05756 |
pyridoxal kinase PdxY; |
1-286 |
0e+00 |
|
pyridoxal kinase PdxY;
Pssm-ID: 235592 [Multi-domain] Cd Length: 286 Bit Score: 511.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737522547 1 MKNLISIQSHVVYGYAGNKSATFPMQLLGVDVWALNTVQFSNHTQYAKWTGMVLPKEQIGEIVRGIDEIGELHRCDAIIS 80
Cdd:PRK05756 1 MKNILSIQSHVVYGHVGNSAAVFPMQRLGVNVWPLNTVQFSNHTGYGKWTGCVMPPSHLTEIVQGIADIGWLGECDAVLS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737522547 81 GYIGSADQVEEIVNAVNYVKQRNPNAVYLCDPVMGHPDKGCIVADGVKEGLVKIAMKAADIITPNLVELRELSGLTVDNF 160
Cdd:PRK05756 81 GYLGSAEQGEAILDAVRRVKAANPQALYFCDPVMGDPEKGCIVAPGVAEFLRDRALPAADIITPNLFELEWLSGRPVETL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737522547 161 SQAIEAVKVILAQGPKKVLVKHLSKVGQDSTKFEMLLANQEGIWHISRPLHTFAKDPVGVGDLTAGLFMANLLNGKSDIE 240
Cdd:PRK05756 161 EDAVAAARALIARGPKIVLVTSLARAGYPADRFEMLLVTADGAWHISRPLVDFMRQPVGVGDLTSALFLARLLQGGSLEE 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 737522547 241 AFEHTANAVNEVMQITHDSGLYELQIIAAREFIVNPRSHYQAVKIA 286
Cdd:PRK05756 241 ALEHTTAAVYEVMARTKERGSYELQLVAAQDSIATPRAMFQARRLA 286
|
|
| pyridox_kin |
TIGR00687 |
pyridoxal kinase; E. coli has an enzyme PdxK that acts in vitro as a pyridoxine/pyridoxal ... |
1-286 |
2.78e-145 |
|
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: 409.22 E-value: 2.78e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737522547 1 MKNLISIQSHVVYGYAGNKSATFPMQLLGVDVWALNTVQFSNHTQYAKWTGMVLPKEQIGEIVRGIDEIGELHRCDAIIS 80
Cdd:TIGR00687 1 MKNVLSIQSHVVYGHVGNRAATFPLQRLGFEVWAVNTVQFSNHTGYGKWTGQVLPPDELHELVEGLEAINKLNQCDAVLS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737522547 81 GYIGSADQVEEIVNAVNYVKQRNPNAVYLCDPVMGHPDKGCIVADGVKEGLVKIAMKAADIITPNLVELRELSGLTVDNF 160
Cdd:TIGR00687 81 GYLGSAEQVAMVVGIVRQVKQANPQALYVCDPVMGDPWKGCYVAPDLLEVYREKAIPVADIITPNQFELELLTGRRINTE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737522547 161 SQAIEAVKVILAQGPKKVLVKHLSKVG-QDSTKFEMLLANQEGIWHISRPLHTFAKDPVGVGDLTAGLFMANLLNGKSDI 239
Cdd:TIGR00687 161 EEALAAADALIAMGPDIVLVTHLIRAGsQRDRSFEGLVATQEGRWHISRPLAVFDPPPVGTGDLIAALLLATLLHGNSLK 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 737522547 240 EAFEHTANAVNEVMQITHDSGLYELQIIAAREFIVNPRSHYQAVKIA 286
Cdd:TIGR00687 241 EALEKTVSAVYHVLRTTIQLGKYELQPVAAQLEIRMPQSKFDAEKVE 287
|
|
| PdxK |
COG2240 |
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal ... |
1-274 |
3.35e-130 |
|
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: 370.25 E-value: 3.35e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737522547 1 MKNLISIQSHVVYGYAGNKSATFPMQLLGVDVWALNTVQFSNHTQYAKWTGMVLPKEQIGEIVRGIDEIGELHRCDAIIS 80
Cdd:COG2240 1 MKRVLSIQSHVVYGHVGNSAAVPPLSALGVEVWPLPTVLLSNHTGYGTFTGRDLPTDDIADILDGWKELGVLLEFDAVLS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737522547 81 GYIGSADQVEEIVNAVNYVKQRNPNAVYLCDPVMGHPDKGCIVADGVKEGLVKIAMKAADIITPNLVELRELSGLTVDNF 160
Cdd:COG2240 81 GYLGSAEQGDIIADFVARVKAANPDALYLCDPVMGDNGKGYYVFPGIAEFIMRRLVPLADIITPNLTELALLTGRPYETL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737522547 161 SQAIEAVKVILAQGPKKVLVKHLSKVGQDSTKFEMLLANQEGIWHISRPLHTFAkdPVGVGDLTAGLFMANLLNGKSDIE 240
Cdd:COG2240 161 EEALAAARALLALGPKIVVVTSVPLDDTPADKIGNLAVTADGAWLVETPLLPFS--PNGTGDLFAALLLAHLLRGKSLEE 238
|
250 260 270
....*....|....*....|....*....|....
gi 737522547 241 AFEHTANAVNEVMQITHDSGLYELQIIAAREFIV 274
Cdd:COG2240 239 ALERAAAFVYEVLERTAAAGSDELLLEAALDELV 272
|
|
| pyridoxal_pyridoxamine_kinase |
cd01173 |
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ... |
3-258 |
4.66e-110 |
|
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: 318.76 E-value: 4.66e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737522547 3 NLISIQSHVVYGYAGNKSATFPMQLLGVDVWALNTVQFSNHTQYAKWTGMVLPKEQIGEIVRGIDEIGELHRCDAIISGY 82
Cdd:cd01173 1 RVLSIQSHVVHGYVGNSAAVFPLQRLGWDVDALPTVQFSNHTGYGTWTGFVLSAEELEDLLEGLEALGLLLEYDAVLTGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737522547 83 IGSADQVEEIVNAVNYVKQRNPNAVYLCDPVMGHPDKGCIVADGVKEGLVKIAMKAADIITPNLVELRELSGLTVDNFSQ 162
Cdd:cd01173 81 LGSAEQVEAVAEIVKRLKEKNPNLLYVCDPVMGDNGKLYVVAEEIVPVYRDLLVPLADIITPNQFELELLTGKKINDLED 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737522547 163 AIEAVKVILAQGPKKVLVKHLSkvGQDSTKFEMLLANQEGIWHISRPLHTFAKDPVGVGDLTAGLFMANLLNGKSDIEAF 242
Cdd:cd01173 161 AKAAARALHAKGPKTVVVTSVE--LADDDRIEMLGSTATEAWLVQRPKIPFPAYFNGTGDLFAALLLARLLKGKSLAEAL 238
|
250
....*....|....*.
gi 737522547 243 EHTANAVNEVMQITHD 258
Cdd:cd01173 239 EKALNFVHEVLEATYE 254
|
|
| Phos_pyr_kin |
pfam08543 |
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ... |
56-183 |
1.10e-15 |
|
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate (TPP) synthesis pathway, TPP is an essential cofactor for many enzymes.
Pssm-ID: 430062 [Multi-domain] Cd Length: 246 Bit Score: 74.44 E-value: 1.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737522547 56 KEQIGEIVRGIdeigelhRCDAIISGYIGSADQVEEIVNavnYVKQRNPNAVylCDPVM----GHPdkgcIVADGVKEGL 131
Cdd:pfam08543 49 AAQLDAVLEDI-------PVDAVKTGMLGSAEIIEAVAE---KLDKYGVPVV--LDPVMvaksGDS----LLDDEAIEAL 112
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 737522547 132 VKIAMKAADIITPNLVELRELSGLTVDNFSQAIEAVKVILAQGPKKVLVK--HL 183
Cdd:pfam08543 113 KEELLPLATLITPNLPEAEALTGRKIKTLEDMKEAAKKLLALGAKAVLIKggHL 166
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05756 |
PRK05756 |
pyridoxal kinase PdxY; |
1-286 |
0e+00 |
|
pyridoxal kinase PdxY;
Pssm-ID: 235592 [Multi-domain] Cd Length: 286 Bit Score: 511.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737522547 1 MKNLISIQSHVVYGYAGNKSATFPMQLLGVDVWALNTVQFSNHTQYAKWTGMVLPKEQIGEIVRGIDEIGELHRCDAIIS 80
Cdd:PRK05756 1 MKNILSIQSHVVYGHVGNSAAVFPMQRLGVNVWPLNTVQFSNHTGYGKWTGCVMPPSHLTEIVQGIADIGWLGECDAVLS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737522547 81 GYIGSADQVEEIVNAVNYVKQRNPNAVYLCDPVMGHPDKGCIVADGVKEGLVKIAMKAADIITPNLVELRELSGLTVDNF 160
Cdd:PRK05756 81 GYLGSAEQGEAILDAVRRVKAANPQALYFCDPVMGDPEKGCIVAPGVAEFLRDRALPAADIITPNLFELEWLSGRPVETL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737522547 161 SQAIEAVKVILAQGPKKVLVKHLSKVGQDSTKFEMLLANQEGIWHISRPLHTFAKDPVGVGDLTAGLFMANLLNGKSDIE 240
Cdd:PRK05756 161 EDAVAAARALIARGPKIVLVTSLARAGYPADRFEMLLVTADGAWHISRPLVDFMRQPVGVGDLTSALFLARLLQGGSLEE 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 737522547 241 AFEHTANAVNEVMQITHDSGLYELQIIAAREFIVNPRSHYQAVKIA 286
Cdd:PRK05756 241 ALEHTTAAVYEVMARTKERGSYELQLVAAQDSIATPRAMFQARRLA 286
|
|
| pyridox_kin |
TIGR00687 |
pyridoxal kinase; E. coli has an enzyme PdxK that acts in vitro as a pyridoxine/pyridoxal ... |
1-286 |
2.78e-145 |
|
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: 409.22 E-value: 2.78e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737522547 1 MKNLISIQSHVVYGYAGNKSATFPMQLLGVDVWALNTVQFSNHTQYAKWTGMVLPKEQIGEIVRGIDEIGELHRCDAIIS 80
Cdd:TIGR00687 1 MKNVLSIQSHVVYGHVGNRAATFPLQRLGFEVWAVNTVQFSNHTGYGKWTGQVLPPDELHELVEGLEAINKLNQCDAVLS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737522547 81 GYIGSADQVEEIVNAVNYVKQRNPNAVYLCDPVMGHPDKGCIVADGVKEGLVKIAMKAADIITPNLVELRELSGLTVDNF 160
Cdd:TIGR00687 81 GYLGSAEQVAMVVGIVRQVKQANPQALYVCDPVMGDPWKGCYVAPDLLEVYREKAIPVADIITPNQFELELLTGRRINTE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737522547 161 SQAIEAVKVILAQGPKKVLVKHLSKVG-QDSTKFEMLLANQEGIWHISRPLHTFAKDPVGVGDLTAGLFMANLLNGKSDI 239
Cdd:TIGR00687 161 EEALAAADALIAMGPDIVLVTHLIRAGsQRDRSFEGLVATQEGRWHISRPLAVFDPPPVGTGDLIAALLLATLLHGNSLK 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 737522547 240 EAFEHTANAVNEVMQITHDSGLYELQIIAAREFIVNPRSHYQAVKIA 286
Cdd:TIGR00687 241 EALEKTVSAVYHVLRTTIQLGKYELQPVAAQLEIRMPQSKFDAEKVE 287
|
|
| PdxK |
COG2240 |
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal ... |
1-274 |
3.35e-130 |
|
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: 370.25 E-value: 3.35e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737522547 1 MKNLISIQSHVVYGYAGNKSATFPMQLLGVDVWALNTVQFSNHTQYAKWTGMVLPKEQIGEIVRGIDEIGELHRCDAIIS 80
Cdd:COG2240 1 MKRVLSIQSHVVYGHVGNSAAVPPLSALGVEVWPLPTVLLSNHTGYGTFTGRDLPTDDIADILDGWKELGVLLEFDAVLS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737522547 81 GYIGSADQVEEIVNAVNYVKQRNPNAVYLCDPVMGHPDKGCIVADGVKEGLVKIAMKAADIITPNLVELRELSGLTVDNF 160
Cdd:COG2240 81 GYLGSAEQGDIIADFVARVKAANPDALYLCDPVMGDNGKGYYVFPGIAEFIMRRLVPLADIITPNLTELALLTGRPYETL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737522547 161 SQAIEAVKVILAQGPKKVLVKHLSKVGQDSTKFEMLLANQEGIWHISRPLHTFAkdPVGVGDLTAGLFMANLLNGKSDIE 240
Cdd:COG2240 161 EEALAAARALLALGPKIVVVTSVPLDDTPADKIGNLAVTADGAWLVETPLLPFS--PNGTGDLFAALLLAHLLRGKSLEE 238
|
250 260 270
....*....|....*....|....*....|....
gi 737522547 241 AFEHTANAVNEVMQITHDSGLYELQIIAAREFIV 274
Cdd:COG2240 239 ALERAAAFVYEVLERTAAAGSDELLLEAALDELV 272
|
|
| pyridoxal_pyridoxamine_kinase |
cd01173 |
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ... |
3-258 |
4.66e-110 |
|
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: 318.76 E-value: 4.66e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737522547 3 NLISIQSHVVYGYAGNKSATFPMQLLGVDVWALNTVQFSNHTQYAKWTGMVLPKEQIGEIVRGIDEIGELHRCDAIISGY 82
Cdd:cd01173 1 RVLSIQSHVVHGYVGNSAAVFPLQRLGWDVDALPTVQFSNHTGYGTWTGFVLSAEELEDLLEGLEALGLLLEYDAVLTGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737522547 83 IGSADQVEEIVNAVNYVKQRNPNAVYLCDPVMGHPDKGCIVADGVKEGLVKIAMKAADIITPNLVELRELSGLTVDNFSQ 162
Cdd:cd01173 81 LGSAEQVEAVAEIVKRLKEKNPNLLYVCDPVMGDNGKLYVVAEEIVPVYRDLLVPLADIITPNQFELELLTGKKINDLED 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737522547 163 AIEAVKVILAQGPKKVLVKHLSkvGQDSTKFEMLLANQEGIWHISRPLHTFAKDPVGVGDLTAGLFMANLLNGKSDIEAF 242
Cdd:cd01173 161 AKAAARALHAKGPKTVVVTSVE--LADDDRIEMLGSTATEAWLVQRPKIPFPAYFNGTGDLFAALLLARLLKGKSLAEAL 238
|
250
....*....|....*.
gi 737522547 243 EHTANAVNEVMQITHD 258
Cdd:cd01173 239 EKALNFVHEVLEATYE 254
|
|
| PTZ00344 |
PTZ00344 |
pyridoxal kinase; Provisional |
2-285 |
8.83e-63 |
|
pyridoxal kinase; Provisional
Pssm-ID: 240372 [Multi-domain] Cd Length: 296 Bit Score: 199.92 E-value: 8.83e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737522547 2 KNLISIQSHVVYGYAGNKSATFPMQLLGVDVWALNTVQFSNHTQYAKWTGMVLPKEQIGEIVRGIDEIGELHRCDAIISG 81
Cdd:PTZ00344 5 KKVLSIQSHVTHGYVGNRAATFPLQLLGFDVDFVNTVQLSNHTGYPVIKGHRLDLNELITLMDGLRANNLLSDYTYVLTG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737522547 82 YIGSADQVEEIVNAVNYVKQRNPNAVYLCDPVMGhpDKGCIVadgVKEGLVKI---AMKAADIITPNLVELRELSGLTVD 158
Cdd:PTZ00344 85 YINSADILREVLATVKEIKELRPKLIFLCDPVMG--DDGKLY---VKEEVVDAyreLIPYADVITPNQFEASLLSGVEVK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737522547 159 NFSQAIEAVKVILAQGPKKVLVKHLsKVGQDSTKFEMLLANQEGI------WHISRPLHTFakDPVGVGDLTAGLFMANL 232
Cdd:PTZ00344 160 DLSDALEAIDWFHEQGIPVVVITSF-REDEDPTHLRFLLSCRDKDtknnkrFTGKVPYIEG--RYTGTGDLFAALLLAFS 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 737522547 233 LNGKSDiEAFEHTANAVNEVMQITHDSGL--------YELQIIAAREFIVNPRSHYQAVKI 285
Cdd:PTZ00344 237 HQHPMD-LAVGKAMGVLQDIIKATRESGGsgssslmsRELRLIQSPRDLLNPETVFKVTPL 296
|
|
| PLN02978 |
PLN02978 |
pyridoxal kinase |
5-285 |
5.92e-52 |
|
pyridoxal kinase
Pssm-ID: 215529 [Multi-domain] Cd Length: 308 Bit Score: 172.23 E-value: 5.92e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737522547 5 ISIQSHVVYGYAGNKSATFPMQLLGVDVWALNTVQFSNHTQYAKWTGMVLPKEQIGEIVRGIDEIGELHRCDaIISGYIG 84
Cdd:PLN02978 18 LSIQSHTVHGYVGNKSAVFPLQLLGFDVDPINSVQFSNHTGYPTFKGQVLDGEQLWALIEGLEANGLLFYTH-LLTGYIG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737522547 85 SADQVEEIVNAVNYVKQRNPNAVYLCDPVMGhpDKGCIVadgVKEGLVKI----AMKAADIITPNLVELRELSGLTVDNF 160
Cdd:PLN02978 97 SVSFLRTVLRVVKKLRSVNPNLTYVCDPVLG--DEGKLY---VPPELVPVyrekVVPLATMLTPNQFEAEQLTGIRIVTE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737522547 161 SQAIEAVKVILAQGPKKVLV------KHLSKVGqdSTKFEMLLANQEgiWHISRPlhtfaKDP---VGVGDLTAGLFMAN 231
Cdd:PLN02978 172 EDAREACAILHAAGPSKVVItsididGKLLLVG--SHRKEKGARPEQ--FKIVIP-----KIPayfTGTGDLMAALLLGW 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 737522547 232 LLNGKSDIE-AFEHTANAVNEVMQITHD----------SGLYELQIIAAREFIVNPRSHYQAVKI 285
Cdd:PLN02978 243 SHKYPDNLDkAAELAVSSLQAVLRRTLAdykragadpkSSSLELRLVQSQDDIRHPQVRFKAERY 307
|
|
| pdxK |
PRK08176 |
pyridoxine/pyridoxal/pyridoxamine kinase; |
3-266 |
2.58e-38 |
|
pyridoxine/pyridoxal/pyridoxamine kinase;
Pssm-ID: 181269 [Multi-domain] Cd Length: 281 Bit Score: 135.94 E-value: 2.58e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737522547 3 NLISIQSHVVYGYAGNKSATFPMQLLGVDVWALNTVQFSNHTQYAKWTGMVLPKEQIGEIVRGIDEIGELHRCDAIISGY 82
Cdd:PRK08176 17 DIVAVQSQVVYGSVGNSIAVPAIKANGLRVFAVPTVLLSNTPHYPTFYGGAIPDEWFSGYLRALQERDALRQLRAVTTGY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737522547 83 IGSADQVEEIVNAVNYVKQRNPNAVYLCDPVMGHPDKGCIVADGVKEGLVKIAMKAADIITPNLVELRELSGLTVDNFSQ 162
Cdd:PRK08176 97 MGSASQIKILAEWLTALRADHPDLLIMVDPVIGDIDSGIYVKPDLPEAYRQHLLPLAQGLTPNIFELEILTGKPCRTLDS 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737522547 163 AIEAVKVILAQGPKKVLVKhlSKVGQDST-KFEMLLANQEGIWHISRPLHtfAKDPVGVGDLTAGLFMANLLNGKSDIEA 241
Cdd:PRK08176 177 AIAAAKSLLSDTLKWVVIT--SAAGNEENqEMQVVVVTADSVNVISHPRV--DTDLKGTGDLFCAELVSGLLKGKALTDA 252
|
250 260
....*....|....*....|....*
gi 737522547 242 FEHTANAVNEVMQITHDSGLYELQI 266
Cdd:PRK08176 253 AHRAGLRVLEVMRYTQQAGSDELIL 277
|
|
| Phos_pyr_kin |
pfam08543 |
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ... |
56-183 |
1.10e-15 |
|
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate (TPP) synthesis pathway, TPP is an essential cofactor for many enzymes.
Pssm-ID: 430062 [Multi-domain] Cd Length: 246 Bit Score: 74.44 E-value: 1.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737522547 56 KEQIGEIVRGIdeigelhRCDAIISGYIGSADQVEEIVNavnYVKQRNPNAVylCDPVM----GHPdkgcIVADGVKEGL 131
Cdd:pfam08543 49 AAQLDAVLEDI-------PVDAVKTGMLGSAEIIEAVAE---KLDKYGVPVV--LDPVMvaksGDS----LLDDEAIEAL 112
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 737522547 132 VKIAMKAADIITPNLVELRELSGLTVDNFSQAIEAVKVILAQGPKKVLVK--HL 183
Cdd:pfam08543 113 KEELLPLATLITPNLPEAEALTGRKIKTLEDMKEAAKKLLALGAKAVLIKggHL 166
|
|
| ThiD |
COG0351 |
Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; ... |
76-209 |
2.30e-13 |
|
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: 68.14 E-value: 2.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737522547 76 DAIISGYIGSADQVEEIVNAVNyvKQRNPNAVylCDPVM----GHPdkgcIVADGVKEGLVKIAMKAADIITPNLVELRE 151
Cdd:COG0351 68 DAIKIGMLGSAEIIEAVAEILA--DYPLVPVV--LDPVMvaksGDR----LLDEDAVEALRELLLPLATVVTPNLPEAEA 139
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 737522547 152 LSGLTVDNFSQAIEAVKVILAQGPKKVLVK--HLSkvGQDSTKfemLLANQEGIWHISRP 209
Cdd:COG0351 140 LLGIEITTLDDMREAAKALLELGAKAVLVKggHLP--GDEAVD---VLYDGDGVREFSAP 194
|
|
| PRK07105 |
PRK07105 |
pyridoxamine kinase; Validated |
25-256 |
1.08e-12 |
|
pyridoxamine kinase; Validated
Pssm-ID: 180840 [Multi-domain] Cd Length: 284 Bit Score: 66.86 E-value: 1.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737522547 25 MQLLGVDVWALNTVQFSNHT----QYAKWTGMVlpkeqigEIVRGIDEIGELH-RCDAIISGYIGSADQVEEIVNAVNYV 99
Cdd:PRK07105 28 MSSMGLQVCPLPTALLSSHTggfqNPSIIDLTD-------GMQAFLTHWKSLNlKFDAIYSGYLGSPRQIQIVSDFIKYF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737522547 100 KQrnPNAVYLCDPVMGhpDKGCiVADGVKEGLVKiAMK----AADIITPNLVE---LRELSGLTVDNFSQAIEAVKVILA 172
Cdd:PRK07105 101 KK--KDLLVVVDPVMG--DNGK-LYQGFDQEMVE-EMRkliqKADVITPNLTEaclLLDKPYLEKSYSEEEIKQLLRKLA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737522547 173 Q-GPKKVLVKHLSkVGQDSTKFEMLLANQEGIWHISR---PLHTFakdpvGVGDLTAGLFMANLLNGKSDIEAFEHTANA 248
Cdd:PRK07105 175 DlGPKIVIITSVP-FEDGKIGVAYYDRATDRFWKVFCkyiPAHYP-----GTGDIFTSVITGSLLQGDSLPIALDRAVQF 248
|
....*...
gi 737522547 249 VNEVMQIT 256
Cdd:PRK07105 249 IEKGIRAT 256
|
|
| PRK06427 |
PRK06427 |
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed |
61-184 |
8.59e-12 |
|
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed
Pssm-ID: 180561 [Multi-domain] Cd Length: 266 Bit Score: 63.99 E-value: 8.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737522547 61 EIVRG-IDEIGELHRCDAIISGYIGSADQVEEIVNAVnyvkQRNPNAVYLCDPVM----GHPdkgcIVADGVKEGLVKIA 135
Cdd:PRK06427 59 EFVAAqLDAVFSDIRIDAVKIGMLASAEIIETVAEAL----KRYPIPPVVLDPVMiaksGDP----LLADDAVAALRERL 130
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 737522547 136 MKAADIITPNLVELRELSGLTVDNF-SQAIEAVKVILAQGPKKVLVK--HLS 184
Cdd:PRK06427 131 LPLATLITPNLPEAEALTGLPIADTeDEMKAAARALHALGCKAVLIKggHLL 182
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
139-249 |
2.15e-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: 63.13 E-value: 2.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737522547 139 ADIITPNLVELRELSGLTVDNFSQAIEAVKVILAQGPKKVLVKHlskvGQDSTkfemLLANQEGIWHISRPLHTFAKDPV 218
Cdd:pfam00294 181 ADLLKPNEEELEALTGAKLDDIEEALAALHKLLAKGIKTVIVTL----GADGA----LVVEGDGEVHVPAVPKVKVVDTT 252
|
90 100 110
....*....|....*....|....*....|.
gi 737522547 219 GVGDLTAGLFMANLLNGKSDIEAFEHtANAV 249
Cdd:pfam00294 253 GAGDSFVGGFLAGLLAGKSLEEALRF-ANAA 282
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
135-242 |
3.79e-11 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 62.46 E-value: 3.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737522547 135 AMKAA-----DIITPNLVELRELSGLTVDNFSQAIEAVKVILAQGPKKVLVKhLSKVGqdstkfeMLLANQEGIWHIsRP 209
Cdd:COG1105 169 ALKAAleagpDLIKPNLEELEELLGRPLETLEDIIAAARELLERGAENVVVS-LGADG-------ALLVTEDGVYRA-KP 239
|
90 100 110
....*....|....*....|....*....|....
gi 737522547 210 LHTFAKDPVGVGD-LTAGlFMANLLNGKSDIEAF 242
Cdd:COG1105 240 PKVEVVSTVGAGDsMVAG-FLAGLARGLDLEEAL 272
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
136-249 |
6.84e-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: 58.72 E-value: 6.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737522547 136 MKAADIITPNLVELRELSGLTVDNFSQAIEAVKVILAQGPKKVLVKhLSKVGqdstkfemLLANQEGIWHISRPLHTFAK 215
Cdd:cd01174 173 LALVDILVPNETEAALLTGIEVTDEEDAEKAARLLLAKGVKNVIVT-LGAKG--------ALLASGGEVEHVPAFKVKAV 243
|
90 100 110
....*....|....*....|....*....|....
gi 737522547 216 DPVGVGDLTAGLFMANLLNGKSDIEAFEHtANAV 249
Cdd:cd01174 244 DTTGAGDTFIGALAAALARGLSLEEAIRF-ANAA 276
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
140-242 |
3.04e-09 |
|
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. FruK plays an important role in the predominant pathway for fructose utilisation.This group also contains tagatose-6-phophate kinase, an enzyme of the tagatose 6-phosphate pathway, which responsible for breakdown of the galactose moiety during lactose metabolism by bacteria such as L. lactis.
Pssm-ID: 238570 [Multi-domain] Cd Length: 289 Bit Score: 56.77 E-value: 3.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737522547 140 DIITPNLVELRELSGLTVDNFSQAIEAVKVILAQGPKKVLVkhlsKVGQDstkfEMLLANQEGIWHiSRPLHTFAKDPVG 219
Cdd:cd01164 179 FLIKPNREELEELFGRPLGDEEDVIAAARKLIERGAENVLV----SLGAD----GALLVTKDGVYR-ASPPKVKVVSTVG 249
|
90 100
....*....|....*....|...
gi 737522547 220 VGDLTAGLFMANLLNGKSDIEAF 242
Cdd:cd01164 250 AGDSMVAGFVAGLAQGLSLEEAL 272
|
|
| PRK12412 |
PRK12412 |
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; |
1-189 |
6.38e-08 |
|
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
Pssm-ID: 183512 [Multi-domain] Cd Length: 268 Bit Score: 52.66 E-value: 6.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737522547 1 MKNLISIQSHVVYGYAGNKSATFPMQLLGV-DVWALNT-VQFSNHTQyakWTGMVLP------KEQIGEIVRGIDeigel 72
Cdd:PRK12412 1 LNKALTIAGSDTSGGAGIQADLKTFQELGVyGMTSLTTiVTMDPHNG---WAHNVFPipastlKPQLETTIEGVG----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737522547 73 hrCDAIISGYIGSADQVEEIVNAVNyvKQRNPNAVylCDPVMG--------HPDKgcivADGVKEGLVKiamkAADIITP 144
Cdd:PRK12412 73 --VDALKTGMLGSVEIIEMVAETIE--KHNFKNVV--VDPVMVckgadealHPET----NDCLRDVLVP----KALVVTP 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 737522547 145 NLVELRELSGLTVDNFSQAIEAVKVILAQGPKKVLVKHLSKVGQD 189
Cdd:PRK12412 139 NLFEAYQLSGVKINSLEDMKEAAKKIHALGAKYVLIKGGSKLGTE 183
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
77-228 |
1.54e-07 |
|
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: 50.56 E-value: 1.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737522547 77 AIISGYIGSADQVEEIVNAVnyvkqRNPNAVYLCDPVMGhpdkgciVADGVKEGLVKiAMKAADIITPNLVELRELSGLT 156
Cdd:cd00287 61 VVISGLSPAPEAVLDALEEA-----RRRGVPVVLDPGPR-------AVRLDGEELEK-LLPGVDILTPNEEEAEALTGRR 127
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 737522547 157 VDNFSQAIEAVKVILAQGPKKVLVKHLSKVGqdstkfemLLANQEGIWHISRPLHTFAKDPVGVGD-LTAGLF 228
Cdd:cd00287 128 DLEVKEAAEAAALLLSKGPKVVIVTLGEKGA--------IVATRGGTEVHVPAFPVKVVDTTGAGDaFLAALA 192
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
135-249 |
1.85e-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: 51.42 E-value: 1.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737522547 135 AMKAADIITPNLVELRELSGLTvdnfsQAIEAVKVILAQGPKKVLVKHlskvGQDStkfeMLLANQEGIWHI-SRPLHtf 213
Cdd:COG0524 182 LLALVDILFPNEEEAELLTGET-----DPEEAAAALLARGVKLVVVTL----GAEG----ALLYTGGEVVHVpAFPVE-- 246
|
90 100 110
....*....|....*....|....*....|....*.
gi 737522547 214 AKDPVGVGDLTAGLFMANLLNGKSDIEAFEHtANAV 249
Cdd:COG0524 247 VVDTTGAGDAFAAGFLAGLLEGLDLEEALRF-ANAA 281
|
|
| ribokinase_group_C |
cd01946 |
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase ... |
125-241 |
1.92e-06 |
|
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238921 [Multi-domain] Cd Length: 277 Bit Score: 48.23 E-value: 1.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737522547 125 DGVKEGLVKIaMKAADIITPNLVELRELSGLtvdnfSQAIEAVKVILAQGPKKVLVKHlskvgqdsTKFEMLLANQEGIW 204
Cdd:cd01946 151 SIKPEKLKKV-LAKVDVVIINDGEARQLTGA-----ANLVKAARLILAMGPKALIIKR--------GEYGALLFTDDGYF 216
|
90 100 110
....*....|....*....|....*....|....*...
gi 737522547 205 HI-SRPLHTFAkDPVGVGDLTAGLFMANLLNGKSDIEA 241
Cdd:cd01946 217 AApAYPLESVF-DPTGAGDTFAGGFIGYLASQKDTSEA 253
|
|
| PRK12413 |
PRK12413 |
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; |
95-260 |
2.69e-05 |
|
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
Pssm-ID: 183513 [Multi-domain] Cd Length: 253 Bit Score: 44.67 E-value: 2.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737522547 95 AVNYVKQRNPNAVYLcDPVMGHPDKGCIVADGVKEGLVKIaMKAADIITPNLVELRELSGLTVDNFSQAIEAVKVILAQG 174
Cdd:PRK12413 88 ALDFIKGHPGIPVVL-DPVLVCKETHDVEVSELRQELIQF-FPYVTVITPNLVEAELLSGKEIKTLEDMKEAAKKLYDLG 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737522547 175 PKKVLVKHLSKVGQ--------DSTKFEMLlanqegiwhiSRPLhtFAKDPVGVGDLTAGLFMANLLNGKSDIEAFEHTA 246
Cdd:PRK12413 166 AKAVVIKGGNRLSQkkaidlfyDGKEFVIL----------ESPV--LEKNNIGAGCTFASSIASQLVKGKSPLEAVKNSK 233
|
170
....*....|....
gi 737522547 247 NAVNEVMQITHDSG 260
Cdd:PRK12413 234 DFVYQAIQQSDQYG 247
|
|
| PRK08573 |
PRK08573 |
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; |
54-184 |
2.76e-05 |
|
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
Pssm-ID: 236297 [Multi-domain] Cd Length: 448 Bit Score: 45.10 E-value: 2.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737522547 54 LPKEQIGEIVRGI-DEIGelhrCDAIISGYIGSADQVEEIVNAVNyvKQRNPNAVylcDPVM----GHPdkgcIVADGVK 128
Cdd:PRK08573 54 LPPEVVAAQIEAVwEDMG----IDAAKTGMLSNREIIEAVAKTVS--KYGFPLVV---DPVMiaksGAP----LLREDAV 120
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 737522547 129 EGLVKIAMKAADIITPNLVELRELSGLTVDNFSQAIEAVKVILAQ-GPKKVLVK--HLS 184
Cdd:PRK08573 121 DALIKRLLPLATVVTPNRPEAEKLTGMKIRSVEDARKAAKYIVEElGAEAVVVKggHLE 179
|
|
| PRK09517 |
PRK09517 |
multifunctional thiamine-phosphate pyrophosphorylase/synthase/phosphomethylpyrimidine kinase; ... |
76-184 |
6.53e-05 |
|
multifunctional thiamine-phosphate pyrophosphorylase/synthase/phosphomethylpyrimidine kinase; Provisional
Pssm-ID: 169939 [Multi-domain] Cd Length: 755 Bit Score: 44.19 E-value: 6.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737522547 76 DAIISGYIGSADQVEEIvnaVNYVKQRNPNAVYLcDPVMGHPDKGCIVADGVKEGLVKIAMkAADIITPNLVELRELSG- 154
Cdd:PRK09517 312 DAVKLGMLGSADTVDLV---ASWLGSHEHGPVVL-DPVMVATSGDRLLDADATEALRRLAV-HVDVVTPNIPELAVLCGe 386
|
90 100 110
....*....|....*....|....*....|..
gi 737522547 155 LTVDNFSQAIEAVKVILAQGPKKVLVK--HLS 184
Cdd:PRK09517 387 APAITMDEAIAQARGFARTHGTIVIVKggHLT 418
|
|
| PRK12616 |
PRK12616 |
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; |
49-189 |
6.79e-05 |
|
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
Pssm-ID: 183624 Cd Length: 270 Bit Score: 43.50 E-value: 6.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737522547 49 WTGMVLP------KEQIGEIVRGIDeigelhrCDAIISGYIGSADQVEEivnAVNYVKQRNPNAVYLcDPVMghpdkgci 122
Cdd:PRK12616 50 WDHQVFPidtdtiRAQLSTIVDGIG-------VDAMKTGMLPTVDIIEL---AADTIKEKQLKNVVI-DPVM-------- 110
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 737522547 123 VADGVKEGLVKIAMKA--------ADIITPNLVELRELSGL-TVDNFSQAIEAVKVILAQGPKKVLVKHLSKVGQD 189
Cdd:PRK12616 111 VCKGANEVLYPEHAEAlreqlaplATVITPNLFEAGQLSGMgEIKTVEQMKEAAKKIHELGAQYVVITGGGKLKHE 186
|
|
| PLN02898 |
PLN02898 |
HMP-P kinase/thiamin-monophosphate pyrophosphorylase |
76-181 |
4.22e-04 |
|
HMP-P kinase/thiamin-monophosphate pyrophosphorylase
Pssm-ID: 215486 [Multi-domain] Cd Length: 502 Bit Score: 41.68 E-value: 4.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737522547 76 DAIISGYIGSAdqveEIVNAVNYVKQRNPNAVYLCDPVM----GHPDKGCIVADGVKEGLVKIAmkaaDIITPNLVELRE 151
Cdd:PLN02898 80 DVVKTGMLPSA----EIVKVLCQALKEFPVKALVVDPVMvstsGDVLAGPSILSALREELLPLA----TIVTPNVKEASA 151
|
90 100 110
....*....|....*....|....*....|.
gi 737522547 152 L-SGLTVDNFSQAIEAVKVILAQGPKKVLVK 181
Cdd:PLN02898 152 LlGGDPLETVADMRSAAKELHKLGPRYVLVK 182
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
137-241 |
5.73e-04 |
|
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: 40.76 E-value: 5.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737522547 137 KAADIITPNLVELRELSGLTVDNFSQAIEAVKVILAQGPKKVLVKHLSKvgqdstkfEMLLANQEG---IWHISRPLHTF 213
Cdd:cd01941 175 HAIDLLTPNRAELEALAGALIENNEDENKAAKILLLPGIKNVIVTLGAK--------GVLLSSREGgveTKLFPAPQPET 246
|
90 100
....*....|....*....|....*....
gi 737522547 214 AKDPVGVGD-LTAGLFMAnLLNGKSDIEA 241
Cdd:cd01941 247 VVNVTGAGDaFVAGLVAG-LLEGMSLDDS 274
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
139-232 |
6.59e-04 |
|
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the lipopolysaccharide (LPS) core precursor ADP-L-glycero-D-manno-heptose. LPS plays an important role in maintaining the structural integrity of the bacterial outer membrane of gram-negative bacteria. RfaE consists of two domains, a sugar kinase domain, represented here, and a domain belonging to the cytidylyltransferase superfamily.
Pssm-ID: 238577 [Multi-domain] Cd Length: 304 Bit Score: 40.62 E-value: 6.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737522547 139 ADIITPNLVELRELSGLTVDNFSQAIEAVKVILAQ-GPKKVLVKHlskvgqdSTKFEMLLANQEGIWHIsrPlhTFAKDP 217
Cdd:cd01172 182 ATLLTPNEKEAREALGDEINDDDELEAAGEKLLELlNLEALLVTL-------GEEGMTLFERDGEVQHI--P--ALAKEV 250
|
90 100 110
....*....|....*....|....*....|...
gi 737522547 218 V---GVGD-----LTAGL----------FMANL 232
Cdd:cd01172 251 YdvtGAGDtviatLALALaagadleeaaFLANA 283
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