|
Name |
Accession |
Description |
Interval |
E-value |
| PdxS |
COG0214 |
Pyridoxal 5'-phosphate synthase subunit PdxS [Coenzyme transport and metabolism]; Pyridoxal 5 ... |
20-307 |
0e+00 |
|
Pyridoxal 5'-phosphate synthase subunit PdxS [Coenzyme transport and metabolism]; Pyridoxal 5'-phosphate synthase subunit PdxS is part of the Pathway/BioSystem: Pyridoxal phosphate biosynthesis
Pssm-ID: 439984 Cd Length: 293 Bit Score: 565.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224470 20 QKSPFSVKVGLAQMLRGGVIMDVVNAEQARIAEEAGACAVMALERVPADIRAQGGVARMSDPEMIKEIKNAVTIPVMAKA 99
Cdd:COG0214 2 ETGTERVKRGLAEMLKGGVIMDVTNPEQAKIAEEAGAVAVMALERVPADIRAAGGVARMADPKMIKEIMEAVSIPVMAKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224470 100 RIGHFVEAQILEAIGVDYVDESEVLTLADEDNHINKHNFKIPFVCGCRNLGEALRRIREGAAMIRTKGEAGTGNVVEAVR 179
Cdd:COG0214 82 RIGHFVEAQILEALGVDFIDESEVLTPADEEYHIDKHAFKVPFVCGARNLGEALRRIGEGAAMIRTKGEAGTGNVVEAVR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224470 180 HVRSVNGAIRLLRSMDDDEVFTYAKKIAAPYDLVVQTKELGRLPVVQFAAGGVATPADAALMMQLGCDGVFVGSGVFKSG 259
Cdd:COG0214 162 HMRTINSEIRRLQGMDEEELMAAAKELGAPYELVKEVAELGRLPVVNFAAGGIATPADAALMMQLGADGVFVGSGIFKSE 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 15224470 260 DPVKRAKAIVQAVTNYRDAAVLAEVSCGLGEAMVGLNLDD--KVERFASR 307
Cdd:COG0214 242 DPEKRARAIVEATTHYDDPEVLAEVSEGLGEAMKGIDISTlpEEERLQER 291
|
|
| PRK04180 |
PRK04180 |
pyridoxal 5'-phosphate synthase lyase subunit PdxS; |
26-307 |
0e+00 |
|
pyridoxal 5'-phosphate synthase lyase subunit PdxS;
Pssm-ID: 179769 Cd Length: 293 Bit Score: 562.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224470 26 VKVGLAQMLRGGVIMDVVNAEQARIAEEAGACAVMALERVPADIRAQGGVARMSDPEMIKEIKNAVTIPVMAKARIGHFV 105
Cdd:PRK04180 8 VKRGFAEMLKGGVIMDVVNAEQAKIAEEAGAVAVMALERVPADIRAAGGVARMADPKMIEEIMDAVSIPVMAKARIGHFV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224470 106 EAQILEAIGVDYVDESEVLTLADEDNHINKHNFKIPFVCGCRNLGEALRRIREGAAMIRTKGEAGTGNVVEAVRHVRSVN 185
Cdd:PRK04180 88 EAQILEALGVDYIDESEVLTPADEEYHIDKWDFTVPFVCGARNLGEALRRIAEGAAMIRTKGEAGTGNVVEAVRHMRQIN 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224470 186 GAIRLLRSMDDDEVFTYAKKIAAPYDLVVQTKELGRLPVVQFAAGGVATPADAALMMQLGCDGVFVGSGVFKSGDPVKRA 265
Cdd:PRK04180 168 GEIRRLTSMSEDELYTAAKELQAPYELVKEVAELGRLPVVNFAAGGIATPADAALMMQLGADGVFVGSGIFKSGDPEKRA 247
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 15224470 266 KAIVQAVTNYRDAAVLAEVSCGLGEAMVGLNLDD--KVERFASR 307
Cdd:PRK04180 248 RAIVEATTHYDDPEVLAEVSKGLGEAMVGIDIDElpPEERLQER 291
|
|
| pdxS |
cd04727 |
PdxS is a subunit of the pyridoxal 5'-phosphate (PLP) synthase, an important enzyme in ... |
28-308 |
0e+00 |
|
PdxS is a subunit of the pyridoxal 5'-phosphate (PLP) synthase, an important enzyme in deoxyxylulose 5-phosphate (DXP)-independent pathway for de novo biosynthesis of PLP, present in some eubacteria, in archaea, fungi, plants, plasmodia, and some metazoa. Together with PdxT, PdxS forms the PLP synthase, a heteromeric glutamine amidotransferase (GATase), whereby PdxT produces ammonia from glutamine and PdxS combines ammonia with five- and three-carbon phosphosugars to form PLP. PLP is the biologically active form of vitamin B6, an essential cofactor in many biochemical processes. PdxS subunits form two hexameric rings.
Pssm-ID: 240078 Cd Length: 283 Bit Score: 539.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224470 28 VGLAQMLRGGVIMDVVNAEQARIAEEAGACAVMALERVPADIRAQGGVARMSDPEMIKEIKNAVTIPVMAKARIGHFVEA 107
Cdd:cd04727 1 RGFAQMLKGGVIMDVTNAEQARIAEEAGAVAVMALERVPADIRAAGGVARMADPKMIKEIMDAVSIPVMAKVRIGHFVEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224470 108 QILEAIGVDYVDESEVLTLADEDNHINKHNFKIPFVCGCRNLGEALRRIREGAAMIRTKGEAGTGNVVEAVRHVRSVNGA 187
Cdd:cd04727 81 QILEALGVDMIDESEVLTPADEEHHIDKHKFKVPFVCGARNLGEALRRISEGAAMIRTKGEAGTGNVVEAVRHMRAVNGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224470 188 IRLLRSMDDDEVFTYAKKIAAPYDLVVQTKELGRLPVVQFAAGGVATPADAALMMQLGCDGVFVGSGVFKSGDPVKRAKA 267
Cdd:cd04727 161 IRKLQSMSEEELYAVAKEIQAPYELVKETAKLGRLPVVNFAAGGVATPADAALMMQLGADGVFVGSGIFKSENPEKRARA 240
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 15224470 268 IVQAVTNYRDAAVLAEVSCGLGEAMVGLNLDD--KVERFASRS 308
Cdd:cd04727 241 IVEAVTHYDDPEILAEVSEGLGEAMVGIDIASlkEEERMQERG 283
|
|
| TIGR00343 |
TIGR00343 |
pyridoxal 5'-phosphate synthase, synthase subunit Pdx1; This protein had been believed to be a ... |
26-297 |
2.72e-163 |
|
pyridoxal 5'-phosphate synthase, synthase subunit Pdx1; This protein had been believed to be a singlet oxygen resistance protein. Subsequent work showed that it is a protein of pyridoxine (vitamin B6) biosynthesis, and that pyridoxine quenches the highly toxic singlet form of oxygen produced by light in the presence of certain chemicals. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridoxine]
Pssm-ID: 129443 Cd Length: 287 Bit Score: 455.77 E-value: 2.72e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224470 26 VKVGLAQMLRGGVIMDVVNAEQARIAEEAGACAVMALERVPADIRAQGGVARMSDPEMIKEIKNAVTIPVMAKARIGHFV 105
Cdd:TIGR00343 1 LKKGLAQMLKGGVIMDVVNPEQAKIAEEAGAVAVMALERVPADIRASGGVARMSDPKMIKEIMDAVSIPVMAKVRIGHFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224470 106 EAQILEAIGVDYVDESEVLTLADEDNHINKHNFKIPFVCGCRNLGEALRRIREGAAMIRTKGEAGTGNVVEAVRHVRSVN 185
Cdd:TIGR00343 81 EAQILEALGVDYIDESEVLTPADWTFHIDKKKFKVPFVCGARDLGEALRRINEGAAMIRTKGEAGTGNIVEAVRHMRKIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224470 186 GAIRLLRSMDDDEVF-TYAKKIAAPYDLVVQTKELGRLPVVQFAAGGVATPADAALMMQLGCDGVFVGSGVFKSGDPVKR 264
Cdd:TIGR00343 161 EEIRQIQNMLEEEDLaAVAKELRVPVELLLEVLKLGKLPVVNFAAGGVATPADAALMMQLGADGVFVGSGIFKSSNPEKL 240
|
250 260 270
....*....|....*....|....*....|...
gi 15224470 265 AKAIVQAVTNYRDAAVLAEVSCGLGEAMVGLNL 297
Cdd:TIGR00343 241 AKAIVEATTHYDNPEKLAEVSKDLGEAMKGISI 273
|
|
| SOR_SNZ |
pfam01680 |
SOR/SNZ family; Members of this family are enzymes involved in a new pathway of pyridoxine ... |
23-228 |
3.01e-159 |
|
SOR/SNZ family; Members of this family are enzymes involved in a new pathway of pyridoxine/pyridoxal 5-phosphate biosynthesis. This family was formerly known as UPF0019.
Pssm-ID: 460291 Cd Length: 206 Bit Score: 442.30 E-value: 3.01e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224470 23 PFSVKVGLAQMLRGGVIMDVVNAEQARIAEEAGACAVMALERVPADIRAQGGVARMSDPEMIKEIKNAVTIPVMAKARIG 102
Cdd:pfam01680 1 TFRVKRGLAQMLKGGVIMDVTNAEQAKIAEEAGAVAVMALERVPADIRKAGGVARMSDPKMIKEIMDAVSIPVMAKARIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224470 103 HFVEAQILEAIGVDYVDESEVLTLADEDNHINKHNFKIPFVCGCRNLGEALRRIREGAAMIRTKGEAGTGNVVEAVRHVR 182
Cdd:pfam01680 81 HFVEAQILEALGVDYIDESEVLTPADEEHHIDKHNFKVPFVCGARNLGEALRRIAEGAAMIRTKGEAGTGNVVEAVRHMR 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15224470 183 SVNGAIRLLRSMDDDEVFTYAKKIAAPYDLVVQTKELGRLPVVQFA 228
Cdd:pfam01680 161 TINGEIRRLQNMDEEELYAFAKELGAPYELVKEVAELGRLPVVNFA 206
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PdxS |
COG0214 |
Pyridoxal 5'-phosphate synthase subunit PdxS [Coenzyme transport and metabolism]; Pyridoxal 5 ... |
20-307 |
0e+00 |
|
Pyridoxal 5'-phosphate synthase subunit PdxS [Coenzyme transport and metabolism]; Pyridoxal 5'-phosphate synthase subunit PdxS is part of the Pathway/BioSystem: Pyridoxal phosphate biosynthesis
Pssm-ID: 439984 Cd Length: 293 Bit Score: 565.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224470 20 QKSPFSVKVGLAQMLRGGVIMDVVNAEQARIAEEAGACAVMALERVPADIRAQGGVARMSDPEMIKEIKNAVTIPVMAKA 99
Cdd:COG0214 2 ETGTERVKRGLAEMLKGGVIMDVTNPEQAKIAEEAGAVAVMALERVPADIRAAGGVARMADPKMIKEIMEAVSIPVMAKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224470 100 RIGHFVEAQILEAIGVDYVDESEVLTLADEDNHINKHNFKIPFVCGCRNLGEALRRIREGAAMIRTKGEAGTGNVVEAVR 179
Cdd:COG0214 82 RIGHFVEAQILEALGVDFIDESEVLTPADEEYHIDKHAFKVPFVCGARNLGEALRRIGEGAAMIRTKGEAGTGNVVEAVR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224470 180 HVRSVNGAIRLLRSMDDDEVFTYAKKIAAPYDLVVQTKELGRLPVVQFAAGGVATPADAALMMQLGCDGVFVGSGVFKSG 259
Cdd:COG0214 162 HMRTINSEIRRLQGMDEEELMAAAKELGAPYELVKEVAELGRLPVVNFAAGGIATPADAALMMQLGADGVFVGSGIFKSE 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 15224470 260 DPVKRAKAIVQAVTNYRDAAVLAEVSCGLGEAMVGLNLDD--KVERFASR 307
Cdd:COG0214 242 DPEKRARAIVEATTHYDDPEVLAEVSEGLGEAMKGIDISTlpEEERLQER 291
|
|
| PRK04180 |
PRK04180 |
pyridoxal 5'-phosphate synthase lyase subunit PdxS; |
26-307 |
0e+00 |
|
pyridoxal 5'-phosphate synthase lyase subunit PdxS;
Pssm-ID: 179769 Cd Length: 293 Bit Score: 562.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224470 26 VKVGLAQMLRGGVIMDVVNAEQARIAEEAGACAVMALERVPADIRAQGGVARMSDPEMIKEIKNAVTIPVMAKARIGHFV 105
Cdd:PRK04180 8 VKRGFAEMLKGGVIMDVVNAEQAKIAEEAGAVAVMALERVPADIRAAGGVARMADPKMIEEIMDAVSIPVMAKARIGHFV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224470 106 EAQILEAIGVDYVDESEVLTLADEDNHINKHNFKIPFVCGCRNLGEALRRIREGAAMIRTKGEAGTGNVVEAVRHVRSVN 185
Cdd:PRK04180 88 EAQILEALGVDYIDESEVLTPADEEYHIDKWDFTVPFVCGARNLGEALRRIAEGAAMIRTKGEAGTGNVVEAVRHMRQIN 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224470 186 GAIRLLRSMDDDEVFTYAKKIAAPYDLVVQTKELGRLPVVQFAAGGVATPADAALMMQLGCDGVFVGSGVFKSGDPVKRA 265
Cdd:PRK04180 168 GEIRRLTSMSEDELYTAAKELQAPYELVKEVAELGRLPVVNFAAGGIATPADAALMMQLGADGVFVGSGIFKSGDPEKRA 247
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 15224470 266 KAIVQAVTNYRDAAVLAEVSCGLGEAMVGLNLDD--KVERFASR 307
Cdd:PRK04180 248 RAIVEATTHYDDPEVLAEVSKGLGEAMVGIDIDElpPEERLQER 291
|
|
| pdxS |
cd04727 |
PdxS is a subunit of the pyridoxal 5'-phosphate (PLP) synthase, an important enzyme in ... |
28-308 |
0e+00 |
|
PdxS is a subunit of the pyridoxal 5'-phosphate (PLP) synthase, an important enzyme in deoxyxylulose 5-phosphate (DXP)-independent pathway for de novo biosynthesis of PLP, present in some eubacteria, in archaea, fungi, plants, plasmodia, and some metazoa. Together with PdxT, PdxS forms the PLP synthase, a heteromeric glutamine amidotransferase (GATase), whereby PdxT produces ammonia from glutamine and PdxS combines ammonia with five- and three-carbon phosphosugars to form PLP. PLP is the biologically active form of vitamin B6, an essential cofactor in many biochemical processes. PdxS subunits form two hexameric rings.
Pssm-ID: 240078 Cd Length: 283 Bit Score: 539.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224470 28 VGLAQMLRGGVIMDVVNAEQARIAEEAGACAVMALERVPADIRAQGGVARMSDPEMIKEIKNAVTIPVMAKARIGHFVEA 107
Cdd:cd04727 1 RGFAQMLKGGVIMDVTNAEQARIAEEAGAVAVMALERVPADIRAAGGVARMADPKMIKEIMDAVSIPVMAKVRIGHFVEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224470 108 QILEAIGVDYVDESEVLTLADEDNHINKHNFKIPFVCGCRNLGEALRRIREGAAMIRTKGEAGTGNVVEAVRHVRSVNGA 187
Cdd:cd04727 81 QILEALGVDMIDESEVLTPADEEHHIDKHKFKVPFVCGARNLGEALRRISEGAAMIRTKGEAGTGNVVEAVRHMRAVNGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224470 188 IRLLRSMDDDEVFTYAKKIAAPYDLVVQTKELGRLPVVQFAAGGVATPADAALMMQLGCDGVFVGSGVFKSGDPVKRAKA 267
Cdd:cd04727 161 IRKLQSMSEEELYAVAKEIQAPYELVKETAKLGRLPVVNFAAGGVATPADAALMMQLGADGVFVGSGIFKSENPEKRARA 240
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 15224470 268 IVQAVTNYRDAAVLAEVSCGLGEAMVGLNLDD--KVERFASRS 308
Cdd:cd04727 241 IVEAVTHYDDPEILAEVSEGLGEAMVGIDIASlkEEERMQERG 283
|
|
| TIGR00343 |
TIGR00343 |
pyridoxal 5'-phosphate synthase, synthase subunit Pdx1; This protein had been believed to be a ... |
26-297 |
2.72e-163 |
|
pyridoxal 5'-phosphate synthase, synthase subunit Pdx1; This protein had been believed to be a singlet oxygen resistance protein. Subsequent work showed that it is a protein of pyridoxine (vitamin B6) biosynthesis, and that pyridoxine quenches the highly toxic singlet form of oxygen produced by light in the presence of certain chemicals. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridoxine]
Pssm-ID: 129443 Cd Length: 287 Bit Score: 455.77 E-value: 2.72e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224470 26 VKVGLAQMLRGGVIMDVVNAEQARIAEEAGACAVMALERVPADIRAQGGVARMSDPEMIKEIKNAVTIPVMAKARIGHFV 105
Cdd:TIGR00343 1 LKKGLAQMLKGGVIMDVVNPEQAKIAEEAGAVAVMALERVPADIRASGGVARMSDPKMIKEIMDAVSIPVMAKVRIGHFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224470 106 EAQILEAIGVDYVDESEVLTLADEDNHINKHNFKIPFVCGCRNLGEALRRIREGAAMIRTKGEAGTGNVVEAVRHVRSVN 185
Cdd:TIGR00343 81 EAQILEALGVDYIDESEVLTPADWTFHIDKKKFKVPFVCGARDLGEALRRINEGAAMIRTKGEAGTGNIVEAVRHMRKIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224470 186 GAIRLLRSMDDDEVF-TYAKKIAAPYDLVVQTKELGRLPVVQFAAGGVATPADAALMMQLGCDGVFVGSGVFKSGDPVKR 264
Cdd:TIGR00343 161 EEIRQIQNMLEEEDLaAVAKELRVPVELLLEVLKLGKLPVVNFAAGGVATPADAALMMQLGADGVFVGSGIFKSSNPEKL 240
|
250 260 270
....*....|....*....|....*....|...
gi 15224470 265 AKAIVQAVTNYRDAAVLAEVSCGLGEAMVGLNL 297
Cdd:TIGR00343 241 AKAIVEATTHYDNPEKLAEVSKDLGEAMKGISI 273
|
|
| SOR_SNZ |
pfam01680 |
SOR/SNZ family; Members of this family are enzymes involved in a new pathway of pyridoxine ... |
23-228 |
3.01e-159 |
|
SOR/SNZ family; Members of this family are enzymes involved in a new pathway of pyridoxine/pyridoxal 5-phosphate biosynthesis. This family was formerly known as UPF0019.
Pssm-ID: 460291 Cd Length: 206 Bit Score: 442.30 E-value: 3.01e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224470 23 PFSVKVGLAQMLRGGVIMDVVNAEQARIAEEAGACAVMALERVPADIRAQGGVARMSDPEMIKEIKNAVTIPVMAKARIG 102
Cdd:pfam01680 1 TFRVKRGLAQMLKGGVIMDVTNAEQAKIAEEAGAVAVMALERVPADIRKAGGVARMSDPKMIKEIMDAVSIPVMAKARIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224470 103 HFVEAQILEAIGVDYVDESEVLTLADEDNHINKHNFKIPFVCGCRNLGEALRRIREGAAMIRTKGEAGTGNVVEAVRHVR 182
Cdd:pfam01680 81 HFVEAQILEALGVDYIDESEVLTPADEEHHIDKHNFKVPFVCGARNLGEALRRIAEGAAMIRTKGEAGTGNVVEAVRHMR 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15224470 183 SVNGAIRLLRSMDDDEVFTYAKKIAAPYDLVVQTKELGRLPVVQFA 228
Cdd:pfam01680 161 TINGEIRRLQNMDEEELYAFAKELGAPYELVKEVAELGRLPVVNFA 206
|
|
| PRK11840 |
PRK11840 |
bifunctional sulfur carrier protein/thiazole synthase protein; Provisional |
217-278 |
1.97e-07 |
|
bifunctional sulfur carrier protein/thiazole synthase protein; Provisional
Pssm-ID: 236998 [Multi-domain] Cd Length: 326 Bit Score: 51.67 E-value: 1.97e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15224470 217 KELGRLPVVQFAagGVATPADAALMMQLGCDGVFVGSGVFKSGDPVKRAKAIVQAVTNYRDA 278
Cdd:PRK11840 245 VEGATVPVLVDA--GVGTASDAAVAMELGCDGVLMNTAIAEAKNPVLMARAMKLAVEAGRLA 304
|
|
| ThiG |
pfam05690 |
Thiazole biosynthesis protein ThiG; This family consists of several bacterial thiazole ... |
206-278 |
2.53e-07 |
|
Thiazole biosynthesis protein ThiG; This family consists of several bacterial thiazole biosynthesis protein G sequences. ThiG, together with ThiF and ThiH, is proposed to be involved in the synthesis of 4-methyl-5-(b-hydroxyethyl)thiazole (THZ) which is an intermediate in the thiazole production pathway. This family also includes triosephosphate isomerase and pyridoxal 5'-phosphate synthase subunit PdxS.
Pssm-ID: 428589 Cd Length: 247 Bit Score: 50.71 E-value: 2.53e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15224470 206 IAAPYDLVVQTKELgRLPVVQFAagGVATPADAALMMQLGCDGVFVGSGVFKSGDPVKRAKAIVQAVTNYRDA 278
Cdd:pfam05690 161 LLNPYNLKIIIEEA-DVPVIVDA--GIGTPSDAAQAMELGADAVLLNTAIARAKDPVAMARAFKLAVEAGRLA 230
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
45-253 |
3.45e-07 |
|
TIM barrel proteins share a structurally conserved phosphate binding motif and in general share an eight beta/alpha closed barrel structure. Specific for this family is the conserved phosphate binding site at the edges of strands 7 and 8. The phosphate comes either from the substrate, as in the case of inosine monophosphate dehydrogenase (IMPDH), or from ribulose-5-phosphate 3-epimerase (RPE) or from cofactors, like FMN.
Pssm-ID: 240073 [Multi-domain] Cd Length: 200 Bit Score: 49.89 E-value: 3.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224470 45 AEQARIAEEAGACAVMALERVPADIRAqggvaRMSDPEMIKEIKNAVTIPVMAKARIGHFVEAQ-----ILEAIGVDYVD 119
Cdd:cd04722 15 VELAKAAAEAGADAIIVGTRSSDPEEA-----ETDDKEVLKEVAAETDLPLGVQLAINDAAAAVdiaaaAARAAGADGVE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224470 120 ESEVLTLADEDNHIN-----KHNFKIPFVCGCRNLGEALRR--IREGAAMIRTKGEAGTGNVVEAVRHVRSVNGAIRLLR 192
Cdd:cd04722 90 IHGAVGYLAREDLELirelrEAVPDVKVVVKLSPTGELAAAaaEEAGVDEVGLGNGGGGGGGRDAVPIADLLLILAKRGS 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15224470 193 smdddevftyakkiaapydlvvqtkelgRLPVvqFAAGGVATPADAALMMQLGCDGVFVGS 253
Cdd:cd04722 170 ----------------------------KVPV--IAGGGINDPEDAAEALALGADGVIVGS 200
|
|
| ThiG |
COG2022 |
Thiazole synthase ThiGH, ThiG subunit (thiamin biosynthesis) [Coenzyme transport and ... |
221-272 |
3.88e-07 |
|
Thiazole synthase ThiGH, ThiG subunit (thiamin biosynthesis) [Coenzyme transport and metabolism]; Thiazole synthase ThiGH, ThiG subunit (thiamin biosynthesis) is part of the Pathway/BioSystem: Thiamine biosynthesis
Pssm-ID: 441625 Cd Length: 259 Bit Score: 50.42 E-value: 3.88e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 15224470 221 RLPVVQFAagGVATPADAALMMQLGCDGVFVGSGVFKSGDPVKRAKAIVQAV 272
Cdd:COG2022 180 DVPVIVDA--GIGTPSDAAEAMELGADAVLLNTAIARAGDPVAMARAFKLAV 229
|
|
| thiG |
PRK00208 |
thiazole synthase; Reviewed |
231-272 |
4.72e-07 |
|
thiazole synthase; Reviewed
Pssm-ID: 234687 Cd Length: 250 Bit Score: 50.06 E-value: 4.72e-07
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 15224470 231 GVATPADAALMMQLGCDGVFVGSGVFKSGDPVKRAKAIVQAV 272
Cdd:PRK00208 183 GIGTPSDAAQAMELGADAVLLNTAIAVAGDPVAMARAFKLAV 224
|
|
| ThiG |
cd04728 |
Thiazole synthase (ThiG) is the tetrameric enzyme that is involved in the formation of the ... |
231-272 |
1.13e-06 |
|
Thiazole synthase (ThiG) is the tetrameric enzyme that is involved in the formation of the thiazole moiety of thiamin pyrophosphate, an essential ubiquitous cofactor that plays an important role in carbohydrate and amino acid metabolism. ThiG catalyzes the formation of thiazole from 1-deoxy-D-xylulose 5-phosphate (DXP) and dehydroglycine, with the help of the sulfur carrier protein ThiS that carries the sulfur needed for thiazole assembly on its carboxy terminus (ThiS-COSH).
Pssm-ID: 240079 Cd Length: 248 Bit Score: 48.64 E-value: 1.13e-06
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 15224470 231 GVATPADAALMMQLGCDGVFVGSGVFKSGDPVKRAKAIVQAV 272
Cdd:cd04728 183 GIGTPSDAAQAMELGADAVLLNTAIAKAKDPVAMARAFKLAV 224
|
|
| DusA |
COG0042 |
tRNA-dihydrouridine synthase [Translation, ribosomal structure and biogenesis]; ... |
45-261 |
1.42e-06 |
|
tRNA-dihydrouridine synthase [Translation, ribosomal structure and biogenesis]; tRNA-dihydrouridine synthase is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 439812 [Multi-domain] Cd Length: 310 Bit Score: 48.94 E-value: 1.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224470 45 AEQARIAEEAGA--------CavmalervPAD--IRAQGGVARMSDPE----MIKEIKNAVTIPVMAKARIGhfveaqil 110
Cdd:COG0042 77 AEAARIAEELGAdeidinmgC--------PVKkvTKGGAGAALLRDPElvaeIVKAVVEAVDVPVTVKIRLG-------- 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224470 111 eaigvdyVDESEvltladednhinkhnfkipfvcgcRNLGEALRRIRE-GAAMI----RTK--GEAGTgnvveavrhvrs 183
Cdd:COG0042 141 -------WDDDD------------------------ENALEFARIAEDaGAAALtvhgRTReqRYKGP------------ 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15224470 184 vngairllrsmdddevftyakkiaAPYDLVVQTKELGRLPVVqfAAGGVATPADAALMMQL-GCDGVFVGSGVFksGDP 261
Cdd:COG0042 178 ------------------------ADWDAIARVKEAVSIPVI--GNGDIFSPEDAKRMLEEtGCDGVMIGRGAL--GNP 228
|
|
| DUS_like_FMN |
cd02801 |
Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze ... |
45-261 |
2.83e-05 |
|
Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze the reduction of the 5,6-double bond of a uridine residue on tRNA. Dihydrouridine modification of tRNA is widely observed in prokaryotes and eukaryotes, and also in some archaea. Most dihydrouridines are found in the D loop of t-RNAs. The role of dihydrouridine in tRNA is currently unknown, but may increase conformational flexibility of the tRNA. It is likely that different family members have different substrate specificities, which may overlap. 1VHN, a putative flavin oxidoreductase, has high sequence similarity to DUS. The enzymatic mechanism of 1VHN is not known at the present.
Pssm-ID: 239200 [Multi-domain] Cd Length: 231 Bit Score: 44.41 E-value: 2.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224470 45 AEQARIAEEAGACAVmalervpaDI----------RAQGGVARMSDPE----MIKEIKNAVTIPVMAKARIGHfveaqil 110
Cdd:cd02801 70 AEAAKIVEELGADGI--------DLnmgcpspkvtKGGAGAALLKDPElvaeIVRAVREAVPIPVTVKIRLGW------- 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224470 111 eaigvdyvdesevltladeDNHINKHNFkipfvcgCRNLGEAlrrireGAAMI----RTKGEAGTGNvveavrhvrsvng 186
Cdd:cd02801 135 -------------------DDEEETLEL-------AKALEDA------GASALtvhgRTREQRYSGP------------- 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15224470 187 airllrsmdddevftyakkiaAPYDLVVQTKELGRLPVvqFAAGGVATPADAALMMQL-GCDGVFVGSGVFksGDP 261
Cdd:cd02801 170 ---------------------ADWDYIAEIKEAVSIPV--IANGDIFSLEDALRCLEQtGVDGVMIGRGAL--GNP 220
|
|
| thiG |
CHL00162 |
thiamin biosynthesis protein G; Validated |
218-272 |
4.81e-05 |
|
thiamin biosynthesis protein G; Validated
Pssm-ID: 214380 Cd Length: 267 Bit Score: 43.93 E-value: 4.81e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 15224470 218 ELGRLPVVQFAagGVATPADAALMMQLGCDGVFVGSGVFKSGDPVKRAKAIVQAV 272
Cdd:CHL00162 186 ENAKIPVIIDA--GIGTPSEASQAMELGASGVLLNTAVAQAKNPEQMAKAMKLAV 238
|
|
| NPD_like |
cd04730 |
2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes ... |
206-253 |
3.89e-04 |
|
2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes oxidative denitrification of nitroalkanes to their corresponding carbonyl compounds and nitrites. NDP is a member of the NAD(P)H-dependent flavin oxidoreductase family that reduce a range of alternative electron acceptors. Most use FAD/FMN as a cofactor and NAD(P)H as electron donor. Some contain 4Fe-4S cluster to transfer electron from FAD to FMN.
Pssm-ID: 240081 [Multi-domain] Cd Length: 236 Bit Score: 40.93 E-value: 3.89e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 15224470 206 IAAPYDLVVQTKELGRLPVVqfAAGGVATPADAALMMQLGCDGVFVGS 253
Cdd:cd04730 141 DIGTFALVPEVRDAVDIPVI--AAGGIADGRGIAAALALGADGVQMGT 186
|
|
| PRK01130 |
PRK01130 |
putative N-acetylmannosamine-6-phosphate 2-epimerase; |
48-253 |
1.03e-03 |
|
putative N-acetylmannosamine-6-phosphate 2-epimerase;
Pssm-ID: 234907 Cd Length: 221 Bit Score: 39.75 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224470 48 ARIAEEAGACAvmalervpadIRAQGgvarmsdPEMIKEIKNAVTIPVmakarIGhfveaqileAIGVDYVDES------ 121
Cdd:PRK01130 29 ALAAVQGGAVG----------IRANG-------VEDIKAIRAVVDVPI-----IG---------IIKRDYPDSEvyitpt 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224470 122 --EVLTLADEDNHInkhnfkIPFVCGCR------NLGEALRRIREGA---AMirtkgeAGTGNVVEAVRHVRSvnGAirl 190
Cdd:PRK01130 78 lkEVDALAAAGADI------IALDATLRprpdgeTLAELVKRIKEYPgqlLM------ADCSTLEEGLAAQKL--GF--- 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15224470 191 lrsmddDEVFT-------YAKKIAAP-YDLVVQTKELGRLPVVqfAAGGVATPADAALMMQLGCDGVFVGS 253
Cdd:PRK01130 141 ------DFIGTtlsgyteETKKPEEPdFALLKELLKAVGCPVI--AEGRINTPEQAKKALELGAHAVVVGG 203
|
|
| thiE |
PRK00043 |
thiamine phosphate synthase; |
204-276 |
1.44e-03 |
|
thiamine phosphate synthase;
Pssm-ID: 234590 [Multi-domain] Cd Length: 212 Bit Score: 39.01 E-value: 1.44e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15224470 204 KKIAAPY---DLVVQTKELGR-LPVVqfAAGGVaTPADAALMMQLGCDGVFVGSGVFKSGDPVKRAKAIVQAVTNYR 276
Cdd:PRK00043 139 KKDAKAPqglEGLREIRAAVGdIPIV--AIGGI-TPENAPEVLEAGADGVAVVSAITGAEDPEAAARALLAAFRAAR 212
|
|
| PRK07565 |
PRK07565 |
dihydroorotate dehydrogenase-like protein; |
48-116 |
1.44e-03 |
|
dihydroorotate dehydrogenase-like protein;
Pssm-ID: 236051 Cd Length: 334 Bit Score: 39.85 E-value: 1.44e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15224470 48 ARIAEEAGAcavMALE----RVPADIRAQGGVARMSDPEMIKEIKNAVTIPVMAK-----ARIGHFVEAqiLEAIGVD 116
Cdd:PRK07565 120 ARQIEQAGA---DALElniyYLPTDPDISGAEVEQRYLDILRAVKSAVSIPVAVKlspyfSNLANMAKR--LDAAGAD 192
|
|
| IGPS |
cd00331 |
Indole-3-glycerol phosphate synthase (IGPS); an enzyme in the tryptophan biosynthetic pathway, ... |
17-268 |
1.45e-03 |
|
Indole-3-glycerol phosphate synthase (IGPS); an enzyme in the tryptophan biosynthetic pathway, catalyzing the ring closure reaction of 1-(o-carboxyphenylamino)-1-deoxyribulose-5-phosphate (CdRP) to indole-3-glycerol phosphate (IGP), accompanied by the release of carbon dioxide and water. IGPS is active as a separate monomer in most organisms, but is also found fused to other enzymes as part of a bifunctional or multifunctional enzyme involved in tryptophan biosynthesis.
Pssm-ID: 238203 Cd Length: 217 Bit Score: 39.37 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224470 17 ETKQKSPFsvkvglaqmlRGGVIMDVVNAEQARIAEEAGACAVMALervpADIRAQGGvarmsDPEMIKEIKNAVTIPVM 96
Cdd:cd00331 16 EVKRASPS----------KGLIREDFDPVEIAKAYEKAGAAAISVL----TEPKYFQG-----SLEDLRAVREAVSLPVL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224470 97 AKarigHFV--EAQILEA--IGVDYV-------DESEVLTLADEdnhinkhnfkipfvcgCRNLG-----------EALR 154
Cdd:cd00331 77 RK----DFIidPYQIYEAraAGADAVllivaalDDEQLKELYEL----------------ARELGmevlvevhdeeELER 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224470 155 RIREGAAMIrtkgeaGTGNvveavrhvrsvngaiRLLRSMD-DDEVFTYAKKIAAPYDLVVqtkelgrlpvvqfAAGGVA 233
Cdd:cd00331 137 ALALGAKII------GINN---------------RDLKTFEvDLNTTERLAPLIPKDVILV-------------SESGIS 182
|
250 260 270
....*....|....*....|....*....|....*
gi 15224470 234 TPADAALMMQLGCDGVFVGSGVFKSGDPVKRAKAI 268
Cdd:cd00331 183 TPEDVKRLAEAGADAVLIGESLMRAPDPGAALREL 217
|
|
| NanE |
cd04729 |
N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to ... |
48-253 |
1.57e-03 |
|
N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to N-acetylglucosamine-6-phosphate. This reaction is part of the pathway that allows the usage of sialic acid as a carbohydrate source. Sialic acids are a family of related sugars that are found as a component of glycoproteins, gangliosides, and other sialoglycoconjugates.
Pssm-ID: 240080 [Multi-domain] Cd Length: 219 Bit Score: 39.10 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224470 48 ARIAEEAGACAvmalervpadIRAQGgvarmsdPEMIKEIKNAVTIPVmakarIG---------------HFVEAQILEA 112
Cdd:cd04729 33 ALAAVQGGAVG----------IRANG-------VEDIRAIRARVDLPI-----IGlikrdypdsevyitpTIEEVDALAA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224470 113 IGVDYV-------DESEVLTLADEDNHInKHNFKIPFVCGCRNLGEALRRIREGAAMIRTKGEAGTGnvveavrhvrsvn 185
Cdd:cd04729 91 AGADIIaldatdrPRPDGETLAELIKRI-HEEYNCLLMADISTLEEALNAAKLGFDIIGTTLSGYTE------------- 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15224470 186 gairllrsmdddevftYAKKIAAP-YDLVVQTKELGRLPVVqfAAGGVATPADAALMMQLGCDGVFVGS 253
Cdd:cd04729 157 ----------------ETAKTEDPdFELLKELRKALGIPVI--AEGRINSPEQAAKALELGADAVVVGS 207
|
|
| PRK07695 |
PRK07695 |
thiazole tautomerase TenI; |
211-272 |
2.85e-03 |
|
thiazole tautomerase TenI;
Pssm-ID: 181086 [Multi-domain] Cd Length: 201 Bit Score: 38.08 E-value: 2.85e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15224470 211 DLVVQTKELGRLPVVqfAAGGVaTPADAALMMQLGCDGVFVGSGVFKSGDPVKRAKAIVQAV 272
Cdd:PRK07695 139 EELSDIARALSIPVI--AIGGI-TPENTRDVLAAGVSGIAVMSGIFSSANPYSKAKRYAESI 197
|
|
| IGPS |
pfam00218 |
Indole-3-glycerol phosphate synthase; |
13-118 |
3.07e-03 |
|
Indole-3-glycerol phosphate synthase;
Pssm-ID: 395163 Cd Length: 252 Bit Score: 38.43 E-value: 3.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224470 13 GAMTETKQKSPfsvkvglaqmlRGGVI-MDVVNAEQARIAEEAGACAVMALERVPadiRAQGgvarmsDPEMIKEIKNAV 91
Cdd:pfam00218 48 ALIAEVKKASP-----------SKGLIrEDFDPAEIARVYEAAGASAISVLTDPK---YFQG------SIEYLRAVRQAV 107
|
90 100
....*....|....*....|....*....
gi 15224470 92 TIPVMAKARIghFVEAQILEA--IGVDYV 118
Cdd:pfam00218 108 SLPVLRKDFI--IDEYQIDEArlAGADAI 134
|
|
| Dus |
pfam01207 |
Dihydrouridine synthase (Dus); Members of this family catalyze the reduction of the 5,6-double ... |
45-254 |
7.29e-03 |
|
Dihydrouridine synthase (Dus); Members of this family catalyze the reduction of the 5,6-double bond of a uridine residue on tRNA. Dihydrouridine modification of tRNA is widely observed in prokaryotes and eukaryotes, and also in some archae. Most dihydrouridines are found in the D loop of t-RNAs. The role of dihydrouridine in tRNA is currently unknown, but may increase conformational flexibility of the tRNA. It is likely that different family members have different substrate specificities, which may overlap. Dus 1 from Saccharomyces cerevisiae acts on pre-tRNA-Phe, while Dus 2 acts on pre-tRNA-Tyr and pre-tRNA-Leu. Dus 1 is active as a single subunit, requiring NADPH or NADH, and is stimulated by the presence of FAD. Some family members may be targeted to the mitochondria and even have a role in mitochondria.
Pssm-ID: 426126 Cd Length: 309 Bit Score: 37.69 E-value: 7.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224470 45 AEQARIAEEAGACAVMALERVPAD--IRAQGGVARMSDPE----MIKEIKNAVTIPVMAKARIGhfveaqileaigvdyv 118
Cdd:pfam01207 69 AEAAKLVEDRGADGIDINMGCPSKkvTRGGGGAALLRNPDlvaqIVKAVVKAVGIPVTVKIRIG---------------- 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224470 119 desevltlaDEDNHINKHNFkIPFVCGCrnlgealrrireGAAMI----RTKGEAGTGnvveavrhvrsvngairllrsm 194
Cdd:pfam01207 133 ---------WDDSHENAVEI-AKIVEDA------------GAQALtvhgRTRAQNYEG---------------------- 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15224470 195 dddevftyakkiAAPYDLVVQTKElgRLPVVQFAAGGVATPADA-ALMMQLGCDGVFVGSG 254
Cdd:pfam01207 169 ------------TADWDAIKQVKQ--AVSIPVIANGDITDPEDAqRCLAYTGADGVMIGRG 215
|
|
| DHOD_like |
cd04739 |
Dihydroorotate dehydrogenase (DHOD) like proteins. DHOD catalyzes the oxidation of (S) ... |
48-116 |
8.87e-03 |
|
Dihydroorotate dehydrogenase (DHOD) like proteins. DHOD catalyzes the oxidation of (S)-dihydroorotate to orotate. This is the fourth step and the only redox reaction in the de novo biosynthesis of UMP, the precursor of all pyrimidine nucleotides. DHOD requires FMN as co-factor. DHOD divides into class 1 and class 2 based on their amino acid sequences and cellular location. Members of class 1 are cytosolic enzymes and multimers while class 2 enzymes are membrane associated and monomeric. The class 1 enzymes can be further divided into subtypes 1A and 1B which are homodimers and heterotetrameric proteins, respectively. This subgroup has the conserved FMN binding site, but lacks some catalytic residues and may therefore be inactive.
Pssm-ID: 240090 Cd Length: 325 Bit Score: 37.21 E-value: 8.87e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15224470 48 ARIAEEAGACAvmaLE----RVPADIRAQGGVARMSDPEMIKEIKNAVTIPVMAK-----ARIGHFVEAqiLEAIGVD 116
Cdd:cd04739 118 ARQIEEAGADA---LElniyALPTDPDISGAEVEQRYLDILRAVKSAVTIPVAVKlspffSALAHMAKQ--LDAAGAD 190
|
|
| |
