|
Name |
Accession |
Description |
Interval |
E-value |
| PRK04180 |
PRK04180 |
pyridoxal 5'-phosphate synthase lyase subunit PdxS; |
13-303 |
0e+00 |
|
pyridoxal 5'-phosphate synthase lyase subunit PdxS;
Pssm-ID: 179769 Cd Length: 293 Bit Score: 602.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644039765 13 VGTARVKRGMADMLKGGVIMDVVTPEQAKIAEDAGAVAVMALERVPADIRAEGGVTRMSDPDMIEGIIDAVSIPVMAKAR 92
Cdd:PRK04180 3 TGTERVKRGFAEMLKGGVIMDVVNAEQAKIAEEAGAVAVMALERVPADIRAAGGVARMADPKMIEEIMDAVSIPVMAKAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644039765 93 IGHFVESQVLESVGVDYVDESEVLTPADEANHIDKWNFTVPFVCGATNLSEALRRISEGAAMIRSKGEAGTGNVVEATRH 172
Cdd:PRK04180 83 IGHFVEAQILEALGVDYIDESEVLTPADEEYHIDKWDFTVPFVCGARNLGEALRRIAEGAAMIRTKGEAGTGNVVEAVRH 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644039765 173 MRQIRADIGRLTTLDEAELFAAAKELRAPYELVAEIARTGTLPVVLFTAGGIATPADAAMMMQLGAQGVFVGSGIFKSGD 252
Cdd:PRK04180 163 MRQINGEIRRLTSMSEDELYTAAKELQAPYELVKEVAELGRLPVVNFAAGGIATPADAALMMQLGADGVFVGSGIFKSGD 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 644039765 253 PAKRAEAIVKATTFYDDPKVIADVSRGLGDAMVGINVDDLSEEEKLAKRGW 303
Cdd:PRK04180 243 PEKRARAIVEATTHYDDPEVLAEVSKGLGEAMVGIDIDELPPEERLQERGW 293
|
|
| PdxS |
COG0214 |
Pyridoxal 5'-phosphate synthase subunit PdxS [Coenzyme transport and metabolism]; Pyridoxal 5 ... |
14-303 |
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: 585.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644039765 14 GTARVKRGMADMLKGGVIMDVVTPEQAKIAEDAGAVAVMALERVPADIRAEGGVTRMSDPDMIEGIIDAVSIPVMAKARI 93
Cdd:COG0214 4 GTERVKRGLAEMLKGGVIMDVTNPEQAKIAEEAGAVAVMALERVPADIRAAGGVARMADPKMIKEIMEAVSIPVMAKVRI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644039765 94 GHFVESQVLESVGVDYVDESEVLTPADEANHIDKWNFTVPFVCGATNLSEALRRISEGAAMIRSKGEAGTGNVVEATRHM 173
Cdd:COG0214 84 GHFVEAQILEALGVDFIDESEVLTPADEEYHIDKHAFKVPFVCGARNLGEALRRIGEGAAMIRTKGEAGTGNVVEAVRHM 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644039765 174 RQIRADIGRLTTLDEAELFAAAKELRAPYELVAEIARTGTLPVVLFTAGGIATPADAAMMMQLGAQGVFVGSGIFKSGDP 253
Cdd:COG0214 164 RTINSEIRRLQGMDEEELMAAAKELGAPYELVKEVAELGRLPVVNFAAGGIATPADAALMMQLGADGVFVGSGIFKSEDP 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 644039765 254 AKRAEAIVKATTFYDDPKVIADVSRGLGDAMVGINVDDLSEEEKLAKRGW 303
Cdd:COG0214 244 EKRARAIVEATTHYDDPEVLAEVSEGLGEAMKGIDISTLPEEERLQERGW 293
|
|
| pdxS |
cd04727 |
PdxS is a subunit of the pyridoxal 5'-phosphate (PLP) synthase, an important enzyme in ... |
20-302 |
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: 522.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644039765 20 RGMADMLKGGVIMDVVTPEQAKIAEDAGAVAVMALERVPADIRAEGGVTRMSDPDMIEGIIDAVSIPVMAKARIGHFVES 99
Cdd:cd04727 1 RGFAQMLKGGVIMDVTNAEQARIAEEAGAVAVMALERVPADIRAAGGVARMADPKMIKEIMDAVSIPVMAKVRIGHFVEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644039765 100 QVLESVGVDYVDESEVLTPADEANHIDKWNFTVPFVCGATNLSEALRRISEGAAMIRSKGEAGTGNVVEATRHMRQIRAD 179
Cdd:cd04727 81 QILEALGVDMIDESEVLTPADEEHHIDKHKFKVPFVCGARNLGEALRRISEGAAMIRTKGEAGTGNVVEAVRHMRAVNGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644039765 180 IGRLTTLDEAELFAAAKELRAPYELVAEIARTGTLPVVLFTAGGIATPADAAMMMQLGAQGVFVGSGIFKSGDPAKRAEA 259
Cdd:cd04727 161 IRKLQSMSEEELYAVAKEIQAPYELVKETAKLGRLPVVNFAAGGVATPADAALMMQLGADGVFVGSGIFKSENPEKRARA 240
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 644039765 260 IVKATTFYDDPKVIADVSRGLGDAMVGINVDDLSEEEKLAKRG 302
Cdd:cd04727 241 IVEAVTHYDDPEILAEVSEGLGEAMVGIDIASLKEEERMQERG 283
|
|
| TIGR00343 |
TIGR00343 |
pyridoxal 5'-phosphate synthase, synthase subunit Pdx1; This protein had been believed to be a ... |
18-303 |
2.68e-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: 455.38 E-value: 2.68e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644039765 18 VKRGMADMLKGGVIMDVVTPEQAKIAEDAGAVAVMALERVPADIRAEGGVTRMSDPDMIEGIIDAVSIPVMAKARIGHFV 97
Cdd:TIGR00343 1 LKKGLAQMLKGGVIMDVVNPEQAKIAEEAGAVAVMALERVPADIRASGGVARMSDPKMIKEIMDAVSIPVMAKVRIGHFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644039765 98 ESQVLESVGVDYVDESEVLTPADEANHIDKWNFTVPFVCGATNLSEALRRISEGAAMIRSKGEAGTGNVVEATRHMRQIR 177
Cdd:TIGR00343 81 EAQILEALGVDYIDESEVLTPADWTFHIDKKKFKVPFVCGARDLGEALRRINEGAAMIRTKGEAGTGNIVEAVRHMRKIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644039765 178 ADIGRL-TTLDEAELFAAAKELRAPYELVAEIARTGTLPVVLFTAGGIATPADAAMMMQLGAQGVFVGSGIFKSGDPAKR 256
Cdd:TIGR00343 161 EEIRQIqNMLEEEDLAAVAKELRVPVELLLEVLKLGKLPVVNFAAGGVATPADAALMMQLGADGVFVGSGIFKSSNPEKL 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 644039765 257 AEAIVKATTFYDDPKVIADVSRGLGDAMVGINVDDLSEEEKLAKRGW 303
Cdd:TIGR00343 241 AKAIVEATTHYDNPEKLAEVSKDLGEAMKGISISSISEAERLQERGW 287
|
|
| SOR_SNZ |
pfam01680 |
SOR/SNZ family; Members of this family are enzymes involved in a new pathway of pyridoxine ... |
15-219 |
3.99e-146 |
|
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: 408.79 E-value: 3.99e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644039765 15 TARVKRGMADMLKGGVIMDVVTPEQAKIAEDAGAVAVMALERVPADIRAEGGVTRMSDPDMIEGIIDAVSIPVMAKARIG 94
Cdd:pfam01680 1 TFRVKRGLAQMLKGGVIMDVTNAEQAKIAEEAGAVAVMALERVPADIRKAGGVARMSDPKMIKEIMDAVSIPVMAKARIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644039765 95 HFVESQVLESVGVDYVDESEVLTPADEANHIDKWNFTVPFVCGATNLSEALRRISEGAAMIRSKGEAGTGNVVEATRHMR 174
Cdd:pfam01680 81 HFVEAQILEALGVDYIDESEVLTPADEEHHIDKHNFKVPFVCGARNLGEALRRIAEGAAMIRTKGEAGTGNVVEAVRHMR 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 644039765 175 QIRADIGRLTTLDEAELFAAAKELRAPYELVAEIARTGTLPVVLF 219
Cdd:pfam01680 161 TINGEIRRLQNMDEEELYAFAKELGAPYELVKEVAELGRLPVVNF 205
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK04180 |
PRK04180 |
pyridoxal 5'-phosphate synthase lyase subunit PdxS; |
13-303 |
0e+00 |
|
pyridoxal 5'-phosphate synthase lyase subunit PdxS;
Pssm-ID: 179769 Cd Length: 293 Bit Score: 602.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644039765 13 VGTARVKRGMADMLKGGVIMDVVTPEQAKIAEDAGAVAVMALERVPADIRAEGGVTRMSDPDMIEGIIDAVSIPVMAKAR 92
Cdd:PRK04180 3 TGTERVKRGFAEMLKGGVIMDVVNAEQAKIAEEAGAVAVMALERVPADIRAAGGVARMADPKMIEEIMDAVSIPVMAKAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644039765 93 IGHFVESQVLESVGVDYVDESEVLTPADEANHIDKWNFTVPFVCGATNLSEALRRISEGAAMIRSKGEAGTGNVVEATRH 172
Cdd:PRK04180 83 IGHFVEAQILEALGVDYIDESEVLTPADEEYHIDKWDFTVPFVCGARNLGEALRRIAEGAAMIRTKGEAGTGNVVEAVRH 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644039765 173 MRQIRADIGRLTTLDEAELFAAAKELRAPYELVAEIARTGTLPVVLFTAGGIATPADAAMMMQLGAQGVFVGSGIFKSGD 252
Cdd:PRK04180 163 MRQINGEIRRLTSMSEDELYTAAKELQAPYELVKEVAELGRLPVVNFAAGGIATPADAALMMQLGADGVFVGSGIFKSGD 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 644039765 253 PAKRAEAIVKATTFYDDPKVIADVSRGLGDAMVGINVDDLSEEEKLAKRGW 303
Cdd:PRK04180 243 PEKRARAIVEATTHYDDPEVLAEVSKGLGEAMVGIDIDELPPEERLQERGW 293
|
|
| PdxS |
COG0214 |
Pyridoxal 5'-phosphate synthase subunit PdxS [Coenzyme transport and metabolism]; Pyridoxal 5 ... |
14-303 |
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: 585.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644039765 14 GTARVKRGMADMLKGGVIMDVVTPEQAKIAEDAGAVAVMALERVPADIRAEGGVTRMSDPDMIEGIIDAVSIPVMAKARI 93
Cdd:COG0214 4 GTERVKRGLAEMLKGGVIMDVTNPEQAKIAEEAGAVAVMALERVPADIRAAGGVARMADPKMIKEIMEAVSIPVMAKVRI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644039765 94 GHFVESQVLESVGVDYVDESEVLTPADEANHIDKWNFTVPFVCGATNLSEALRRISEGAAMIRSKGEAGTGNVVEATRHM 173
Cdd:COG0214 84 GHFVEAQILEALGVDFIDESEVLTPADEEYHIDKHAFKVPFVCGARNLGEALRRIGEGAAMIRTKGEAGTGNVVEAVRHM 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644039765 174 RQIRADIGRLTTLDEAELFAAAKELRAPYELVAEIARTGTLPVVLFTAGGIATPADAAMMMQLGAQGVFVGSGIFKSGDP 253
Cdd:COG0214 164 RTINSEIRRLQGMDEEELMAAAKELGAPYELVKEVAELGRLPVVNFAAGGIATPADAALMMQLGADGVFVGSGIFKSEDP 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 644039765 254 AKRAEAIVKATTFYDDPKVIADVSRGLGDAMVGINVDDLSEEEKLAKRGW 303
Cdd:COG0214 244 EKRARAIVEATTHYDDPEVLAEVSEGLGEAMKGIDISTLPEEERLQERGW 293
|
|
| pdxS |
cd04727 |
PdxS is a subunit of the pyridoxal 5'-phosphate (PLP) synthase, an important enzyme in ... |
20-302 |
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: 522.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644039765 20 RGMADMLKGGVIMDVVTPEQAKIAEDAGAVAVMALERVPADIRAEGGVTRMSDPDMIEGIIDAVSIPVMAKARIGHFVES 99
Cdd:cd04727 1 RGFAQMLKGGVIMDVTNAEQARIAEEAGAVAVMALERVPADIRAAGGVARMADPKMIKEIMDAVSIPVMAKVRIGHFVEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644039765 100 QVLESVGVDYVDESEVLTPADEANHIDKWNFTVPFVCGATNLSEALRRISEGAAMIRSKGEAGTGNVVEATRHMRQIRAD 179
Cdd:cd04727 81 QILEALGVDMIDESEVLTPADEEHHIDKHKFKVPFVCGARNLGEALRRISEGAAMIRTKGEAGTGNVVEAVRHMRAVNGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644039765 180 IGRLTTLDEAELFAAAKELRAPYELVAEIARTGTLPVVLFTAGGIATPADAAMMMQLGAQGVFVGSGIFKSGDPAKRAEA 259
Cdd:cd04727 161 IRKLQSMSEEELYAVAKEIQAPYELVKETAKLGRLPVVNFAAGGVATPADAALMMQLGADGVFVGSGIFKSENPEKRARA 240
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 644039765 260 IVKATTFYDDPKVIADVSRGLGDAMVGINVDDLSEEEKLAKRG 302
Cdd:cd04727 241 IVEAVTHYDDPEILAEVSEGLGEAMVGIDIASLKEEERMQERG 283
|
|
| TIGR00343 |
TIGR00343 |
pyridoxal 5'-phosphate synthase, synthase subunit Pdx1; This protein had been believed to be a ... |
18-303 |
2.68e-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: 455.38 E-value: 2.68e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644039765 18 VKRGMADMLKGGVIMDVVTPEQAKIAEDAGAVAVMALERVPADIRAEGGVTRMSDPDMIEGIIDAVSIPVMAKARIGHFV 97
Cdd:TIGR00343 1 LKKGLAQMLKGGVIMDVVNPEQAKIAEEAGAVAVMALERVPADIRASGGVARMSDPKMIKEIMDAVSIPVMAKVRIGHFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644039765 98 ESQVLESVGVDYVDESEVLTPADEANHIDKWNFTVPFVCGATNLSEALRRISEGAAMIRSKGEAGTGNVVEATRHMRQIR 177
Cdd:TIGR00343 81 EAQILEALGVDYIDESEVLTPADWTFHIDKKKFKVPFVCGARDLGEALRRINEGAAMIRTKGEAGTGNIVEAVRHMRKIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644039765 178 ADIGRL-TTLDEAELFAAAKELRAPYELVAEIARTGTLPVVLFTAGGIATPADAAMMMQLGAQGVFVGSGIFKSGDPAKR 256
Cdd:TIGR00343 161 EEIRQIqNMLEEEDLAAVAKELRVPVELLLEVLKLGKLPVVNFAAGGVATPADAALMMQLGADGVFVGSGIFKSSNPEKL 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 644039765 257 AEAIVKATTFYDDPKVIADVSRGLGDAMVGINVDDLSEEEKLAKRGW 303
Cdd:TIGR00343 241 AKAIVEATTHYDNPEKLAEVSKDLGEAMKGISISSISEAERLQERGW 287
|
|
| SOR_SNZ |
pfam01680 |
SOR/SNZ family; Members of this family are enzymes involved in a new pathway of pyridoxine ... |
15-219 |
3.99e-146 |
|
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: 408.79 E-value: 3.99e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644039765 15 TARVKRGMADMLKGGVIMDVVTPEQAKIAEDAGAVAVMALERVPADIRAEGGVTRMSDPDMIEGIIDAVSIPVMAKARIG 94
Cdd:pfam01680 1 TFRVKRGLAQMLKGGVIMDVTNAEQAKIAEEAGAVAVMALERVPADIRKAGGVARMSDPKMIKEIMDAVSIPVMAKARIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644039765 95 HFVESQVLESVGVDYVDESEVLTPADEANHIDKWNFTVPFVCGATNLSEALRRISEGAAMIRSKGEAGTGNVVEATRHMR 174
Cdd:pfam01680 81 HFVEAQILEALGVDYIDESEVLTPADEEHHIDKHNFKVPFVCGARNLGEALRRIAEGAAMIRTKGEAGTGNVVEAVRHMR 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 644039765 175 QIRADIGRLTTLDEAELFAAAKELRAPYELVAEIARTGTLPVVLF 219
Cdd:pfam01680 161 TINGEIRRLQNMDEEELYAFAKELGAPYELVKEVAELGRLPVVNF 205
|
|
| ThiE |
COG0352 |
Thiamine monophosphate synthase [Coenzyme transport and metabolism]; Thiamine monophosphate ... |
203-263 |
9.78e-07 |
|
Thiamine monophosphate synthase [Coenzyme transport and metabolism]; Thiamine monophosphate synthase is part of the Pathway/BioSystem: Thiamine biosynthesis
Pssm-ID: 440121 [Multi-domain] Cd Length: 206 Bit Score: 48.64 E-value: 9.78e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 644039765 203 ELVAEIARTGTLPVVLFtaGGIaTPADAAMMMQLGAQGVFVGSGIFKSGDPAKRAEAIVKA 263
Cdd:COG0352 145 EGLAWWAELVEIPVVAI--GGI-TPENAAEVLAAGADGVAVISAIWGAPDPAAAARELRAA 202
|
|
| TMP_TenI |
cd00564 |
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step ... |
203-262 |
1.09e-05 |
|
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step in the thiamine biosynthesis pathway, the substitution of the pyrophosphate of 2-methyl-4-amino-5- hydroxymethylpyrimidine pyrophosphate by 4-methyl-5- (beta-hydroxyethyl) thiazole phosphate to yield thiamine phosphate. TenI is a enzymatically inactive regulatory protein involved in the regulation of several extracellular enzymes. This superfamily also contains other enzymatically inactive proteins with unknown functions.
Pssm-ID: 238317 [Multi-domain] Cd Length: 196 Bit Score: 45.20 E-value: 1.09e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 644039765 203 ELVAEIARTGTLPVVlftA-GGIaTPADAAMMMQLGAQGVFVGSGIFKSGDPAKRAEAIVK 262
Cdd:cd00564 140 ELLREIAELVEIPVV---AiGGI-TPENAAEVLAAGADGVAVISAITGADDPAAAARELLA 196
|
|
| ThiG |
pfam05690 |
Thiazole biosynthesis protein ThiG; This family consists of several bacterial thiazole ... |
198-264 |
1.18e-05 |
|
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: 45.70 E-value: 1.18e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 644039765 198 LRAPYELVAEIARTgTLPVVLftAGGIATPADAAMMMQLGAQGVFVGSGIFKSGDPAKRAEAIVKAT 264
Cdd:pfam05690 161 LLNPYNLKIIIEEA-DVPVIV--DAGIGTPSDAAQAMELGADAVLLNTAIARAKDPVAMARAFKLAV 224
|
|
| NPD_like |
cd04730 |
2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes ... |
198-245 |
1.41e-05 |
|
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: 45.55 E-value: 1.41e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 644039765 198 LRAPYELVAEIARTGTLPVVLftAGGIATPADAAMMMQLGAQGVFVGS 245
Cdd:cd04730 141 DIGTFALVPEVRDAVDIPVIA--AGGIADGRGIAAALALGADGVQMGT 186
|
|
| thiG |
PRK00208 |
thiazole synthase; Reviewed |
198-263 |
3.42e-05 |
|
thiazole synthase; Reviewed
Pssm-ID: 234687 Cd Length: 250 Bit Score: 44.28 E-value: 3.42e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 644039765 198 LRAPYELVAEIARTgTLPVVLftAGGIATPADAAMMMQLGAQGVFVGSGIFKSGDPAKRAEAIVKA 263
Cdd:PRK00208 161 LLNPYNLRIIIEQA-DVPVIV--DAGIGTPSDAAQAMELGADAVLLNTAIAVAGDPVAMARAFKLA 223
|
|
| ThiG |
cd04728 |
Thiazole synthase (ThiG) is the tetrameric enzyme that is involved in the formation of the ... |
223-264 |
6.53e-05 |
|
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: 43.63 E-value: 6.53e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 644039765 223 GIATPADAAMMMQLGAQGVFVGSGIFKSGDPAKRAEAIVKAT 264
Cdd:cd04728 183 GIGTPSDAAQAMELGADAVLLNTAIAKAKDPVAMARAFKLAV 224
|
|
| YrpB |
COG2070 |
NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General ... |
197-245 |
9.50e-05 |
|
NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General function prediction only];
Pssm-ID: 441673 [Multi-domain] Cd Length: 302 Bit Score: 43.18 E-value: 9.50e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 644039765 197 ELRAPYELVAEIARTGTLPVVLftAGGIATPADAAMMMQLGAQGVFVGS 245
Cdd:COG2070 142 DEVSTFALVPEVRDAVDIPVIA--AGGIADGRGIAAALALGADGVQMGT 188
|
|
| thiG |
CHL00162 |
thiamin biosynthesis protein G; Validated |
223-260 |
9.60e-05 |
|
thiamin biosynthesis protein G; Validated
Pssm-ID: 214380 Cd Length: 267 Bit Score: 43.16 E-value: 9.60e-05
10 20 30
....*....|....*....|....*....|....*...
gi 644039765 223 GIATPADAAMMMQLGAQGVFVGSGIFKSGDPAKRAEAI 260
Cdd:CHL00162 197 GIGTPSEASQAMELGASGVLLNTAVAQAKNPEQMAKAM 234
|
|
| IGPS |
cd00331 |
Indole-3-glycerol phosphate synthase (IGPS); an enzyme in the tryptophan biosynthetic pathway, ... |
216-260 |
1.58e-04 |
|
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: 42.07 E-value: 1.58e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 644039765 216 VVLFTAGGIATPADAAMMMQLGAQGVFVGSGIFKSGDPAKRAEAI 260
Cdd:cd00331 173 VILVSESGISTPEDVKRLAEAGADAVLIGESLMRAPDPGAALREL 217
|
|
| PyrD |
COG0167 |
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate ... |
203-284 |
2.38e-04 |
|
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate dehydrogenase is part of the Pathway/BioSystem: Pyrimidine biosynthesis
Pssm-ID: 439937 [Multi-domain] Cd Length: 296 Bit Score: 41.98 E-value: 2.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644039765 203 ELVAEIART--GTLPVVlfTAGGIATPADAAMMMQLGAQGVFVGSGIfksgdpakraeaivkattFYDDPKVIADVSRGL 280
Cdd:COG0167 224 RMVREVAQAvgGDIPII--GVGGISTAEDALEFILAGASAVQVGTAL------------------FYEGPGLVRRIIRGL 283
|
....
gi 644039765 281 GDAM 284
Cdd:COG0167 284 EAYL 287
|
|
| PRK11840 |
PRK11840 |
bifunctional sulfur carrier protein/thiazole synthase protein; Provisional |
179-263 |
2.57e-04 |
|
bifunctional sulfur carrier protein/thiazole synthase protein; Provisional
Pssm-ID: 236998 [Multi-domain] Cd Length: 326 Bit Score: 42.04 E-value: 2.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644039765 179 DIGRLTTLDEAELFAAAKELRAPYElVAEIARTGTLPVVLftAGGIATPADAAMMMQLGAQGVFVGSGIFKSGDPAKRAE 258
Cdd:PRK11840 216 DAGAVAVMPLGAPIGSGLGIQNPYT-IRLIVEGATVPVLV--DAGVGTASDAAVAMELGCDGVLMNTAIAEAKNPVLMAR 292
|
....*
gi 644039765 259 AIVKA 263
Cdd:PRK11840 293 AMKLA 297
|
|
| thiE |
PRK00043 |
thiamine phosphate synthase; |
174-264 |
2.70e-04 |
|
thiamine phosphate synthase;
Pssm-ID: 234590 [Multi-domain] Cd Length: 212 Bit Score: 41.32 E-value: 2.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644039765 174 RQIRAD---IGrLTTLDEAELFAAA-----------------KELRAPY---ELVAEI-ARTGTLPVVlftA-GGIaTPA 228
Cdd:PRK00043 98 RALLGPdaiIG-LSTHTLEEAAAALaagadyvgvgpifptptKKDAKAPqglEGLREIrAAVGDIPIV---AiGGI-TPE 172
|
90 100 110
....*....|....*....|....*....|....*.
gi 644039765 229 DAAMMMQLGAQGVFVGSGIFKSGDPAKRAEAIVKAT 264
Cdd:PRK00043 173 NAPEVLEAGADGVAVVSAITGAEDPEAAARALLAAF 208
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
38-245 |
3.02e-04 |
|
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: 41.03 E-value: 3.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644039765 38 EQAKIAEDAGAVAVMALERVPADIRAEGGvtrmsDPDMIEGIIDAVSIPVMAKARIGHFVE-----SQVLESVGVDYV-- 110
Cdd:cd04722 16 ELAKAAAEAGADAIIVGTRSSDPEEAETD-----DKEVLKEVAAETDLPLGVQLAINDAAAavdiaAAAARAAGADGVei 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644039765 111 DESEVLTPADEANHID---KWNFTVPFVCGATNLSEALRRISEgaamirskgEAGTGnvveatrhmrQIRADIGRLTTLD 187
Cdd:cd04722 91 HGAVGYLAREDLELIRelrEAVPDVKVVVKLSPTGELAAAAAE---------EAGVD----------EVGLGNGGGGGGG 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 644039765 188 EAELFAAAKELRAPYELVAeiartgtlpVVLFTAGGIATPADAAMMMQLGAQGVFVGS 245
Cdd:cd04722 152 RDAVPIADLLLILAKRGSK---------VPVIAGGGINDPEDAAEALALGADGVIVGS 200
|
|
| IGPS |
pfam00218 |
Indole-3-glycerol phosphate synthase; |
16-255 |
3.49e-04 |
|
Indole-3-glycerol phosphate synthase;
Pssm-ID: 395163 Cd Length: 252 Bit Score: 41.13 E-value: 3.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644039765 16 ARVKRgmADMLKGGVIMDVVTPEQAKIAEDAGAVAVMALervpadiraeggvtrmSDPDMIEGIID-------AVSIPVM 88
Cdd:pfam00218 51 AEVKK--ASPSKGLIREDFDPAEIARVYEAAGASAISVL----------------TDPKYFQGSIEylravrqAVSLPVL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644039765 89 AKARIghFVESQVLES--VGVDYV-------DESEVLTPADEANhidKWNFTVpfVCGATNLSEALRRISEGAAMIrskg 159
Cdd:pfam00218 113 RKDFI--IDEYQIDEArlAGADAIllivavlDDELLEELYAYAR---SLGMEV--LVEVHNEEELERALALGAKII---- 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644039765 160 eaGTGNvveatRHMRQIRADIGRLTTLdeaelfaaAKELRAPYELVAEiartgtlpvvlftaGGIATPADAAMMMQLGAQ 239
Cdd:pfam00218 182 --GVNN-----RNLKTFEVDLNTTRRL--------APLIPADVLLVAE--------------SGIYTPADVRELKEHGAN 232
|
250
....*....|....*.
gi 644039765 240 GVFVGSGIFKSGDPAK 255
Cdd:pfam00218 233 AFLVGESLMRQEDVRA 248
|
|
| PRK01130 |
PRK01130 |
putative N-acetylmannosamine-6-phosphate 2-epimerase; |
202-247 |
3.75e-03 |
|
putative N-acetylmannosamine-6-phosphate 2-epimerase;
Pssm-ID: 234907 Cd Length: 221 Bit Score: 37.82 E-value: 3.75e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 644039765 202 YELVAEIARTGTLPVVlfTAGGIATPADAAMMMQLGAQGVFVGSGI 247
Cdd:PRK01130 162 FALLKELLKAVGCPVI--AEGRINTPEQAKKALELGAHAVVVGGAI 205
|
|
| PRK07259 |
PRK07259 |
dihydroorotate dehydrogenase; |
205-294 |
4.30e-03 |
|
dihydroorotate dehydrogenase;
Pssm-ID: 235982 Cd Length: 301 Bit Score: 38.21 E-value: 4.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644039765 205 VAEIARTGTLPVVlfTAGGIATPADAAMMMQLGAQGVFVGSGIFksgdpakraeaivkattfyDDPKVIADVSRGLGDAM 284
Cdd:PRK07259 226 VYQVYQAVDIPII--GMGGISSAEDAIEFIMAGASAVQVGTANF-------------------YDPYAFPKIIEGLEAYL 284
|
90
....*....|
gi 644039765 285 VGINVDDLSE 294
Cdd:PRK07259 285 DKYGIKSIEE 294
|
|
| PRK04302 |
PRK04302 |
triosephosphate isomerase; Provisional |
216-263 |
5.62e-03 |
|
triosephosphate isomerase; Provisional
Pssm-ID: 235274 Cd Length: 223 Bit Score: 37.54 E-value: 5.62e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 644039765 216 VVLFTAGGIATPADAAMMMQLGAQGVFVGSGIFKSGDPAKRAEAIVKA 263
Cdd:PRK04302 174 VKVLCGAGISTGEDVKAALELGADGVLLASGVVKAKDPEAALRDLVSP 221
|
|
| trpC |
PRK00278 |
indole-3-glycerol phosphate synthase TrpC; |
223-263 |
6.13e-03 |
|
indole-3-glycerol phosphate synthase TrpC;
Pssm-ID: 234710 Cd Length: 260 Bit Score: 37.44 E-value: 6.13e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 644039765 223 GIATPADAAMMMQLGAQGVFVGSGIFKSGDPAKRAEAIVKA 263
Cdd:PRK00278 219 GIFTPEDLKRLAKAGADAVLVGESLMRADDPGAALRELLGA 259
|
|
| NanE |
cd04729 |
N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to ... |
202-247 |
7.70e-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: 37.17 E-value: 7.70e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 644039765 202 YELVAEIARTGTLPVVlfTAGGIATPADAAMMMQLGAQGVFVGSGI 247
Cdd:cd04729 166 FELLKELRKALGIPVI--AEGRINSPEQAAKALELGADAVVVGSAI 209
|
|
| Dus |
pfam01207 |
Dihydrouridine synthase (Dus); Members of this family catalyze the reduction of the 5,6-double ... |
38-246 |
8.75e-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: 37.31 E-value: 8.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644039765 38 EQAKIAEDAGAVAVMALERVPAD--IRAEGGVTRMSDPDMIEGII----DAVSIPVMAKARIGhfvesqvlesvgvdyVD 111
Cdd:pfam01207 70 EAAKLVEDRGADGIDINMGCPSKkvTRGGGGAALLRNPDLVAQIVkavvKAVGIPVTVKIRIG---------------WD 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644039765 112 ESevltpadeanHIDKWNFtVPFVCGAtnlsealrriseGAAMI----RSKGEagtgnvveatrhMRQIRADIgrlttld 187
Cdd:pfam01207 135 DS----------HENAVEI-AKIVEDA------------GAQALtvhgRTRAQ------------NYEGTADW------- 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 644039765 188 eaelfAAAKELRApyelvaeiartgTLPVVLFTAGGIATPADA-AMMMQLGAQGVFVGSG 246
Cdd:pfam01207 173 -----DAIKQVKQ------------AVSIPVIANGDITDPEDAqRCLAYTGADGVMIGRG 215
|
|
| His_biosynth |
pfam00977 |
Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine ... |
148-303 |
9.36e-03 |
|
Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine biosynthesis pathway are contained in this family. Histidine is formed by several complex and distinct biochemical reactions catalyzed by eight enzymes. The enzymes in this Pfam entry are called His6 and His7 in eukaryotes and HisA and HisF in prokaryotes. The structure of HisA is known to be a TIM barrel fold. In some archaeal HisA proteins the TIM barrel is composed of two tandem repeats of a half barrel. This family belong to the common phosphate binding site TIM barrel family.
Pssm-ID: 425971 Cd Length: 228 Bit Score: 36.69 E-value: 9.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644039765 148 ISEGAAMIRSKGEAGT-----GNVVEATRHMRQIRADigRLTTLDeaeLFAAAKELRAPYELVAEIARTGTLPVVLftAG 222
Cdd:pfam00977 8 LKDGRVVRLVKGDYFQntvyaGDPVELAKRYEEEGAD--ELHFVD---LDAAKEGRPVNLDVVEEIAEEVFIPVQV--GG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644039765 223 GIATPADAAMMMQLGAQGVFVGSgifksgdpakraEAIvkattfyDDPKVIADVSRGLGDAMVGINVDdlSEEEKLAKRG 302
Cdd:pfam00977 81 GIRSLEDVERLLSAGADRVIIGT------------AAV-------KNPELIKEAAEKFGSQCIVVAID--ARRGKVAING 139
|
.
gi 644039765 303 W 303
Cdd:pfam00977 140 W 140
|
|
| |
