|
Name |
Accession |
Description |
Interval |
E-value |
| PRK04180 |
PRK04180 |
pyridoxal 5'-phosphate synthase lyase subunit PdxS; |
1-293 |
0e+00 |
|
pyridoxal 5'-phosphate synthase lyase subunit PdxS;
Pssm-ID: 179769 Cd Length: 293 Bit Score: 604.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518367314 1 METGTSRVKKGMAEMQKGGVIMDVMSAEQAKIAEAAGASAVMALERVPSDIRAAGGVARMADPTIVEEVMKVVSIPVMAK 80
Cdd:PRK04180 1 LETGTERVKRGFAEMLKGGVIMDVVNAEQAKIAEEAGAVAVMALERVPADIRAAGGVARMADPKMIEEIMDAVSIPVMAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518367314 81 ARIGHFVEAKVLEALGVDYIDESEVLTPADEVFHINKREFTVPFVCGARDLGEALRRIGEGASMIRTKGEPGTGNIVEAV 160
Cdd:PRK04180 81 ARIGHFVEAQILEALGVDYIDESEVLTPADEEYHIDKWDFTVPFVCGARNLGEALRRIAEGAAMIRTKGEAGTGNVVEAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518367314 161 RHMRMMVSQIRKVQNMSKDELMNEAKLLGAPYELLLQVHETGRLPVVNFAAGGVATPADAALMMHLGADGVFVGSGIFKS 240
Cdd:PRK04180 161 RHMRQINGEIRRLTSMSEDELYTAAKELQAPYELVKEVAELGRLPVVNFAAGGIATPADAALMMQLGADGVFVGSGIFKS 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 518367314 241 DNPEKFAKAIVEATTHYEDYELIANISKNLGTPMKGIEISKLHASERMQERGW 293
Cdd:PRK04180 241 GDPEKRARAIVEATTHYDDPEVLAEVSKGLGEAMVGIDIDELPPEERLQERGW 293
|
|
| PdxS |
COG0214 |
Pyridoxal 5'-phosphate synthase subunit PdxS [Coenzyme transport and metabolism]; Pyridoxal 5 ... |
1-293 |
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: 595.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518367314 1 METGTSRVKKGMAEMQKGGVIMDVMSAEQAKIAEAAGASAVMALERVPSDIRAAGGVARMADPTIVEEVMKVVSIPVMAK 80
Cdd:COG0214 1 LETGTERVKRGLAEMLKGGVIMDVTNPEQAKIAEEAGAVAVMALERVPADIRAAGGVARMADPKMIKEIMEAVSIPVMAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518367314 81 ARIGHFVEAKVLEALGVDYIDESEVLTPADEVFHINKREFTVPFVCGARDLGEALRRIGEGASMIRTKGEPGTGNIVEAV 160
Cdd:COG0214 81 VRIGHFVEAQILEALGVDFIDESEVLTPADEEYHIDKHAFKVPFVCGARNLGEALRRIGEGAAMIRTKGEAGTGNVVEAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518367314 161 RHMRMMVSQIRKVQNMSKDELMNEAKLLGAPYELLLQVHETGRLPVVNFAAGGVATPADAALMMHLGADGVFVGSGIFKS 240
Cdd:COG0214 161 RHMRTINSEIRRLQGMDEEELMAAAKELGAPYELVKEVAELGRLPVVNFAAGGIATPADAALMMQLGADGVFVGSGIFKS 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 518367314 241 DNPEKFAKAIVEATTHYEDYELIANISKNLGTPMKGIEISKLHASERMQERGW 293
Cdd:COG0214 241 EDPEKRARAIVEATTHYDDPEVLAEVSEGLGEAMKGIDISTLPEEERLQERGW 293
|
|
| pdxS |
cd04727 |
PdxS is a subunit of the pyridoxal 5'-phosphate (PLP) synthase, an important enzyme in ... |
10-292 |
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: 532.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518367314 10 KGMAEMQKGGVIMDVMSAEQAKIAEAAGASAVMALERVPSDIRAAGGVARMADPTIVEEVMKVVSIPVMAKARIGHFVEA 89
Cdd:cd04727 1 RGFAQMLKGGVIMDVTNAEQARIAEEAGAVAVMALERVPADIRAAGGVARMADPKMIKEIMDAVSIPVMAKVRIGHFVEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518367314 90 KVLEALGVDYIDESEVLTPADEVFHINKREFTVPFVCGARDLGEALRRIGEGASMIRTKGEPGTGNIVEAVRHMRMMVSQ 169
Cdd:cd04727 81 QILEALGVDMIDESEVLTPADEEHHIDKHKFKVPFVCGARNLGEALRRISEGAAMIRTKGEAGTGNVVEAVRHMRAVNGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518367314 170 IRKVQNMSKDELMNEAKLLGAPYELLLQVHETGRLPVVNFAAGGVATPADAALMMHLGADGVFVGSGIFKSDNPEKFAKA 249
Cdd:cd04727 161 IRKLQSMSEEELYAVAKEIQAPYELVKETAKLGRLPVVNFAAGGVATPADAALMMQLGADGVFVGSGIFKSENPEKRARA 240
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 518367314 250 IVEATTHYEDYELIANISKNLGTPMKGIEISKLHASERMQERG 292
Cdd:cd04727 241 IVEAVTHYDDPEILAEVSEGLGEAMVGIDIASLKEEERMQERG 283
|
|
| TIGR00343 |
TIGR00343 |
pyridoxal 5'-phosphate synthase, synthase subunit Pdx1; This protein had been believed to be a ... |
8-293 |
6.28e-180 |
|
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: 496.99 E-value: 6.28e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518367314 8 VKKGMAEMQKGGVIMDVMSAEQAKIAEAAGASAVMALERVPSDIRAAGGVARMADPTIVEEVMKVVSIPVMAKARIGHFV 87
Cdd:TIGR00343 1 LKKGLAQMLKGGVIMDVVNPEQAKIAEEAGAVAVMALERVPADIRASGGVARMSDPKMIKEIMDAVSIPVMAKVRIGHFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518367314 88 EAKVLEALGVDYIDESEVLTPADEVFHINKREFTVPFVCGARDLGEALRRIGEGASMIRTKGEPGTGNIVEAVRHMRMMV 167
Cdd:TIGR00343 81 EAQILEALGVDYIDESEVLTPADWTFHIDKKKFKVPFVCGARDLGEALRRINEGAAMIRTKGEAGTGNIVEAVRHMRKIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518367314 168 SQIRKVQNMSK-DELMNEAKLLGAPYELLLQVHETGRLPVVNFAAGGVATPADAALMMHLGADGVFVGSGIFKSDNPEKF 246
Cdd:TIGR00343 161 EEIRQIQNMLEeEDLAAVAKELRVPVELLLEVLKLGKLPVVNFAAGGVATPADAALMMQLGADGVFVGSGIFKSSNPEKL 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 518367314 247 AKAIVEATTHYEDYELIANISKNLGTPMKGIEISKLHASERMQERGW 293
Cdd:TIGR00343 241 AKAIVEATTHYDNPEKLAEVSKDLGEAMKGISISSISEAERLQERGW 287
|
|
| SOR_SNZ |
pfam01680 |
SOR/SNZ family; Members of this family are enzymes involved in a new pathway of pyridoxine ... |
5-210 |
2.23e-149 |
|
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: 416.49 E-value: 2.23e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518367314 5 TSRVKKGMAEMQKGGVIMDVMSAEQAKIAEAAGASAVMALERVPSDIRAAGGVARMADPTIVEEVMKVVSIPVMAKARIG 84
Cdd:pfam01680 1 TFRVKRGLAQMLKGGVIMDVTNAEQAKIAEEAGAVAVMALERVPADIRKAGGVARMSDPKMIKEIMDAVSIPVMAKARIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518367314 85 HFVEAKVLEALGVDYIDESEVLTPADEVFHINKREFTVPFVCGARDLGEALRRIGEGASMIRTKGEPGTGNIVEAVRHMR 164
Cdd:pfam01680 81 HFVEAQILEALGVDYIDESEVLTPADEEHHIDKHNFKVPFVCGARNLGEALRRIAEGAAMIRTKGEAGTGNVVEAVRHMR 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 518367314 165 MMVSQIRKVQNMSKDELMNEAKLLGAPYELLLQVHETGRLPVVNFA 210
Cdd:pfam01680 161 TINGEIRRLQNMDEEELYAFAKELGAPYELVKEVAELGRLPVVNFA 206
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK04180 |
PRK04180 |
pyridoxal 5'-phosphate synthase lyase subunit PdxS; |
1-293 |
0e+00 |
|
pyridoxal 5'-phosphate synthase lyase subunit PdxS;
Pssm-ID: 179769 Cd Length: 293 Bit Score: 604.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518367314 1 METGTSRVKKGMAEMQKGGVIMDVMSAEQAKIAEAAGASAVMALERVPSDIRAAGGVARMADPTIVEEVMKVVSIPVMAK 80
Cdd:PRK04180 1 LETGTERVKRGFAEMLKGGVIMDVVNAEQAKIAEEAGAVAVMALERVPADIRAAGGVARMADPKMIEEIMDAVSIPVMAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518367314 81 ARIGHFVEAKVLEALGVDYIDESEVLTPADEVFHINKREFTVPFVCGARDLGEALRRIGEGASMIRTKGEPGTGNIVEAV 160
Cdd:PRK04180 81 ARIGHFVEAQILEALGVDYIDESEVLTPADEEYHIDKWDFTVPFVCGARNLGEALRRIAEGAAMIRTKGEAGTGNVVEAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518367314 161 RHMRMMVSQIRKVQNMSKDELMNEAKLLGAPYELLLQVHETGRLPVVNFAAGGVATPADAALMMHLGADGVFVGSGIFKS 240
Cdd:PRK04180 161 RHMRQINGEIRRLTSMSEDELYTAAKELQAPYELVKEVAELGRLPVVNFAAGGIATPADAALMMQLGADGVFVGSGIFKS 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 518367314 241 DNPEKFAKAIVEATTHYEDYELIANISKNLGTPMKGIEISKLHASERMQERGW 293
Cdd:PRK04180 241 GDPEKRARAIVEATTHYDDPEVLAEVSKGLGEAMVGIDIDELPPEERLQERGW 293
|
|
| PdxS |
COG0214 |
Pyridoxal 5'-phosphate synthase subunit PdxS [Coenzyme transport and metabolism]; Pyridoxal 5 ... |
1-293 |
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: 595.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518367314 1 METGTSRVKKGMAEMQKGGVIMDVMSAEQAKIAEAAGASAVMALERVPSDIRAAGGVARMADPTIVEEVMKVVSIPVMAK 80
Cdd:COG0214 1 LETGTERVKRGLAEMLKGGVIMDVTNPEQAKIAEEAGAVAVMALERVPADIRAAGGVARMADPKMIKEIMEAVSIPVMAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518367314 81 ARIGHFVEAKVLEALGVDYIDESEVLTPADEVFHINKREFTVPFVCGARDLGEALRRIGEGASMIRTKGEPGTGNIVEAV 160
Cdd:COG0214 81 VRIGHFVEAQILEALGVDFIDESEVLTPADEEYHIDKHAFKVPFVCGARNLGEALRRIGEGAAMIRTKGEAGTGNVVEAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518367314 161 RHMRMMVSQIRKVQNMSKDELMNEAKLLGAPYELLLQVHETGRLPVVNFAAGGVATPADAALMMHLGADGVFVGSGIFKS 240
Cdd:COG0214 161 RHMRTINSEIRRLQGMDEEELMAAAKELGAPYELVKEVAELGRLPVVNFAAGGIATPADAALMMQLGADGVFVGSGIFKS 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 518367314 241 DNPEKFAKAIVEATTHYEDYELIANISKNLGTPMKGIEISKLHASERMQERGW 293
Cdd:COG0214 241 EDPEKRARAIVEATTHYDDPEVLAEVSEGLGEAMKGIDISTLPEEERLQERGW 293
|
|
| pdxS |
cd04727 |
PdxS is a subunit of the pyridoxal 5'-phosphate (PLP) synthase, an important enzyme in ... |
10-292 |
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: 532.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518367314 10 KGMAEMQKGGVIMDVMSAEQAKIAEAAGASAVMALERVPSDIRAAGGVARMADPTIVEEVMKVVSIPVMAKARIGHFVEA 89
Cdd:cd04727 1 RGFAQMLKGGVIMDVTNAEQARIAEEAGAVAVMALERVPADIRAAGGVARMADPKMIKEIMDAVSIPVMAKVRIGHFVEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518367314 90 KVLEALGVDYIDESEVLTPADEVFHINKREFTVPFVCGARDLGEALRRIGEGASMIRTKGEPGTGNIVEAVRHMRMMVSQ 169
Cdd:cd04727 81 QILEALGVDMIDESEVLTPADEEHHIDKHKFKVPFVCGARNLGEALRRISEGAAMIRTKGEAGTGNVVEAVRHMRAVNGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518367314 170 IRKVQNMSKDELMNEAKLLGAPYELLLQVHETGRLPVVNFAAGGVATPADAALMMHLGADGVFVGSGIFKSDNPEKFAKA 249
Cdd:cd04727 161 IRKLQSMSEEELYAVAKEIQAPYELVKETAKLGRLPVVNFAAGGVATPADAALMMQLGADGVFVGSGIFKSENPEKRARA 240
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 518367314 250 IVEATTHYEDYELIANISKNLGTPMKGIEISKLHASERMQERG 292
Cdd:cd04727 241 IVEAVTHYDDPEILAEVSEGLGEAMVGIDIASLKEEERMQERG 283
|
|
| TIGR00343 |
TIGR00343 |
pyridoxal 5'-phosphate synthase, synthase subunit Pdx1; This protein had been believed to be a ... |
8-293 |
6.28e-180 |
|
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: 496.99 E-value: 6.28e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518367314 8 VKKGMAEMQKGGVIMDVMSAEQAKIAEAAGASAVMALERVPSDIRAAGGVARMADPTIVEEVMKVVSIPVMAKARIGHFV 87
Cdd:TIGR00343 1 LKKGLAQMLKGGVIMDVVNPEQAKIAEEAGAVAVMALERVPADIRASGGVARMSDPKMIKEIMDAVSIPVMAKVRIGHFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518367314 88 EAKVLEALGVDYIDESEVLTPADEVFHINKREFTVPFVCGARDLGEALRRIGEGASMIRTKGEPGTGNIVEAVRHMRMMV 167
Cdd:TIGR00343 81 EAQILEALGVDYIDESEVLTPADWTFHIDKKKFKVPFVCGARDLGEALRRINEGAAMIRTKGEAGTGNIVEAVRHMRKIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518367314 168 SQIRKVQNMSK-DELMNEAKLLGAPYELLLQVHETGRLPVVNFAAGGVATPADAALMMHLGADGVFVGSGIFKSDNPEKF 246
Cdd:TIGR00343 161 EEIRQIQNMLEeEDLAAVAKELRVPVELLLEVLKLGKLPVVNFAAGGVATPADAALMMQLGADGVFVGSGIFKSSNPEKL 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 518367314 247 AKAIVEATTHYEDYELIANISKNLGTPMKGIEISKLHASERMQERGW 293
Cdd:TIGR00343 241 AKAIVEATTHYDNPEKLAEVSKDLGEAMKGISISSISEAERLQERGW 287
|
|
| SOR_SNZ |
pfam01680 |
SOR/SNZ family; Members of this family are enzymes involved in a new pathway of pyridoxine ... |
5-210 |
2.23e-149 |
|
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: 416.49 E-value: 2.23e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518367314 5 TSRVKKGMAEMQKGGVIMDVMSAEQAKIAEAAGASAVMALERVPSDIRAAGGVARMADPTIVEEVMKVVSIPVMAKARIG 84
Cdd:pfam01680 1 TFRVKRGLAQMLKGGVIMDVTNAEQAKIAEEAGAVAVMALERVPADIRKAGGVARMSDPKMIKEIMDAVSIPVMAKARIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518367314 85 HFVEAKVLEALGVDYIDESEVLTPADEVFHINKREFTVPFVCGARDLGEALRRIGEGASMIRTKGEPGTGNIVEAVRHMR 164
Cdd:pfam01680 81 HFVEAQILEALGVDYIDESEVLTPADEEHHIDKHNFKVPFVCGARNLGEALRRIAEGAAMIRTKGEAGTGNVVEAVRHMR 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 518367314 165 MMVSQIRKVQNMSKDELMNEAKLLGAPYELLLQVHETGRLPVVNFA 210
Cdd:pfam01680 161 TINGEIRRLQNMDEEELYAFAKELGAPYELVKEVAELGRLPVVNFA 206
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
22-235 |
1.67e-10 |
|
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: 59.14 E-value: 1.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518367314 22 MDVMSAEQAKIAEAAGASAVMALERVPSDIRAAGgvarmADPTIVEEVMKVVSIPVMAKARIGHFVE-----AKVLEALG 96
Cdd:cd04722 10 PSGDPVELAKAAAEAGADAIIVGTRSSDPEEAET-----DDKEVLKEVAAETDLPLGVQLAINDAAAavdiaAAAARAAG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518367314 97 VDYIDESEVLTPADEVFHINKREF-----TVPFVCGARDLGEALRR--IGEGASMIRTKGEPGTGNIVEAVRHMRMMVSQ 169
Cdd:cd04722 85 ADGVEIHGAVGYLAREDLELIRELreavpDVKVVVKLSPTGELAAAaaEEAGVDEVGLGNGGGGGGGRDAVPIADLLLIL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518367314 170 IRkvqnmskdelmneakllgapyelllqvhetGRLPVVNFAAGGVATPADAALMMHLGADGVFVGS 235
Cdd:cd04722 165 AK------------------------------RGSKVPVIAGGGINDPEDAAEALALGADGVIVGS 200
|
|
| thiG |
CHL00162 |
thiamin biosynthesis protein G; Validated |
200-250 |
8.02e-07 |
|
thiamin biosynthesis protein G; Validated
Pssm-ID: 214380 Cd Length: 267 Bit Score: 49.32 E-value: 8.02e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 518367314 200 ETGRLPVVNFAagGVATPADAALMMHLGADGVFVGSGIFKSDNPEKFAKAI 250
Cdd:CHL00162 186 ENAKIPVIIDA--GIGTPSEASQAMELGASGVLLNTAVAQAKNPEQMAKAM 234
|
|
| TMP_TenI |
cd00564 |
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step ... |
193-252 |
3.01e-06 |
|
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: 46.74 E-value: 3.01e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 518367314 193 ELLLQVHETGRLPVVnfAAGGVaTPADAALMMHLGADGVFVGSGIFKSDNPEKFAKAIVE 252
Cdd:cd00564 140 ELLREIAELVEIPVV--AIGGI-TPENAAEVLAAGADGVAVISAITGADDPAAAARELLA 196
|
|
| DusA |
COG0042 |
tRNA-dihydrouridine synthase [Translation, ribosomal structure and biogenesis]; ... |
27-243 |
3.87e-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: 47.40 E-value: 3.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518367314 27 AEQAKIAEAAGASAVmalervpsDI----------RAAGGVARMADP----TIVEEVMKVVSIPVMAKARIGhfveakvl 92
Cdd:COG0042 77 AEAARIAEELGADEI--------DInmgcpvkkvtKGGAGAALLRDPelvaEIVKAVVEAVDVPVTVKIRLG-------- 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518367314 93 ealgvdyIDESevltpadevfHINkreftvpfvcgARDLGEALRRigEGASMIrtkgepgtgnIVEAvrhmrmmvsqiRK 172
Cdd:COG0042 141 -------WDDD----------DEN-----------ALEFARIAED--AGAAAL----------TVHG-----------RT 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518367314 173 VQNMSKdelmNEAKllgapYELLLQVHETGRLPVVnfAAGGVATPADAALMM-HLGADGVFVGSGIFKsdNP 243
Cdd:COG0042 170 REQRYK----GPAD-----WDAIARVKEAVSIPVI--GNGDIFSPEDAKRMLeETGCDGVMIGRGALG--NP 228
|
|
| PRK11840 |
PRK11840 |
bifunctional sulfur carrier protein/thiazole synthase protein; Provisional |
191-253 |
1.64e-05 |
|
bifunctional sulfur carrier protein/thiazole synthase protein; Provisional
Pssm-ID: 236998 [Multi-domain] Cd Length: 326 Bit Score: 45.51 E-value: 1.64e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518367314 191 PYELLLQVhETGRLPVVNFAagGVATPADAALMMHLGADGVFVGSGIFKSDNPEKFAKAI---VEA 253
Cdd:PRK11840 238 PYTIRLIV-EGATVPVLVDA--GVGTASDAAVAMELGCDGVLMNTAIAEAKNPVLMARAMklaVEA 300
|
|
| IGPS |
cd00331 |
Indole-3-glycerol phosphate synthase (IGPS); an enzyme in the tryptophan biosynthetic pathway, ... |
210-250 |
3.03e-05 |
|
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: 43.99 E-value: 3.03e-05
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 518367314 210 AAGGVATPADAALMMHLGADGVFVGSGIFKSDNPEKFAKAI 250
Cdd:cd00331 177 SESGISTPEDVKRLAEAGADAVLIGESLMRAPDPGAALREL 217
|
|
| ThiG |
cd04728 |
Thiazole synthase (ThiG) is the tetrameric enzyme that is involved in the formation of the ... |
213-253 |
4.93e-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: 4.93e-05
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 518367314 213 GVATPADAALMMHLGADGVFVGSGIFKSDNPEKFAKAI---VEA 253
Cdd:cd04728 183 GIGTPSDAAQAMELGADAVLLNTAIAKAKDPVAMARAFklaVEA 226
|
|
| thiE |
PRK00043 |
thiamine phosphate synthase; |
193-257 |
5.43e-05 |
|
thiamine phosphate synthase;
Pssm-ID: 234590 [Multi-domain] Cd Length: 212 Bit Score: 43.25 E-value: 5.43e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518367314 193 ELLLQVHETGR-LPVVnfAAGGVaTPADAALMMHLGADGVFVGSGIFKSDNPEKFAKAIVEATTHY 257
Cdd:PRK00043 149 EGLREIRAAVGdIPIV--AIGGI-TPENAPEVLEAGADGVAVVSAITGAEDPEAAARALLAAFRAA 211
|
|
| thiG |
PRK00208 |
thiazole synthase; Reviewed |
213-253 |
6.75e-05 |
|
thiazole synthase; Reviewed
Pssm-ID: 234687 Cd Length: 250 Bit Score: 43.51 E-value: 6.75e-05
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 518367314 213 GVATPADAALMMHLGADGVFVGSGIFKSDNPEKFAKAI---VEA 253
Cdd:PRK00208 183 GIGTPSDAAQAMELGADAVLLNTAIAVAGDPVAMARAFklaVEA 226
|
|
| NPD_like |
cd04730 |
2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes ... |
190-254 |
7.46e-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: 43.24 E-value: 7.46e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518367314 190 APYELLLQVHETGRLPVVnfAAGGVATPADAALMMHLGADGVFVGSgIF----KSDNPEKFAKAIVEAT 254
Cdd:cd04730 143 GTFALVPEVRDAVDIPVI--AAGGIADGRGIAAALALGADGVQMGT-RFlateESGASPAYKQALLAAT 208
|
|
| PRK07028 |
PRK07028 |
bifunctional hexulose-6-phosphate synthase/ribonuclease regulator; Validated |
191-253 |
9.76e-05 |
|
bifunctional hexulose-6-phosphate synthase/ribonuclease regulator; Validated
Pssm-ID: 235912 [Multi-domain] Cd Length: 430 Bit Score: 43.47 E-value: 9.76e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518367314 191 PYELLLQVHETGRLPVVnfAAGGVaTPADAALMMHLGADGVFVGSGIFKSDNPEKFAKAIVEA 253
Cdd:PRK07028 150 PLELLKEVSEEVSIPIA--VAGGL-DAETAAKAVAAGADIVIVGGNIIKSADVTEAARKIREA 209
|
|
| ThiG |
pfam05690 |
Thiazole biosynthesis protein ThiG; This family consists of several bacterial thiazole ... |
203-253 |
1.58e-04 |
|
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: 42.24 E-value: 1.58e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 518367314 203 RLPVVNFAagGVATPADAALMMHLGADGVFVGSGIFKSDNPEKFAKAI---VEA 253
Cdd:pfam05690 175 DVPVIVDA--GIGTPSDAAQAMELGADAVLLNTAIARAKDPVAMARAFklaVEA 226
|
|
| PRK01130 |
PRK01130 |
putative N-acetylmannosamine-6-phosphate 2-epimerase; |
192-237 |
3.74e-04 |
|
putative N-acetylmannosamine-6-phosphate 2-epimerase;
Pssm-ID: 234907 Cd Length: 221 Bit Score: 40.90 E-value: 3.74e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 518367314 192 YELLLQVHETGRLPVVnfAAGGVATPADAALMMHLGADGVFVGSGI 237
Cdd:PRK01130 162 FALLKELLKAVGCPVI--AEGRINTPEQAKKALELGAHAVVVGGAI 205
|
|
| PRK07695 |
PRK07695 |
thiazole tautomerase TenI; |
193-253 |
5.75e-04 |
|
thiazole tautomerase TenI;
Pssm-ID: 181086 [Multi-domain] Cd Length: 201 Bit Score: 40.00 E-value: 5.75e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518367314 193 ELLLQVHETGRLPVVnfAAGGVaTPADAALMMHLGADGVFVGSGIFKSDNPEKFAKAIVEA 253
Cdd:PRK07695 139 EELSDIARALSIPVI--AIGGI-TPENTRDVLAAGVSGIAVMSGIFSSANPYSKAKRYAES 196
|
|
| Dus |
pfam01207 |
Dihydrouridine synthase (Dus); Members of this family catalyze the reduction of the 5,6-double ... |
27-236 |
5.90e-04 |
|
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: 40.77 E-value: 5.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518367314 27 AEQAKIAEAAGASAVMALERVPSD--IRAAGGVARMADP----TIVEEVMKVVSIPVMAKARIGhfveakvlealgvdyI 100
Cdd:pfam01207 69 AEAAKLVEDRGADGIDINMGCPSKkvTRGGGGAALLRNPdlvaQIVKAVVKAVGIPVTVKIRIG---------------W 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518367314 101 DESEvltpaDEVFHINKReftvpfVCGArdlgealrrigeGASMI----RTKGEPGTGNiveavrhmrmmvsqirkvqnm 176
Cdd:pfam01207 134 DDSH-----ENAVEIAKI------VEDA------------GAQALtvhgRTRAQNYEGT--------------------- 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518367314 177 skdelmneakllgAPYELLLQVHEtgRLPVVNFAAGGVATPADA-ALMMHLGADGVFVGSG 236
Cdd:pfam01207 170 -------------ADWDAIKQVKQ--AVSIPVIANGDITDPEDAqRCLAYTGADGVMIGRG 215
|
|
| DUS_like_FMN |
cd02801 |
Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze ... |
27-100 |
7.76e-04 |
|
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: 40.17 E-value: 7.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518367314 27 AEQAKIAEAAGASAV---MAlerVPSD--IRAAGGVARMADP----TIVEEVMKVVSIPVMAKARIG-----HFVE-AKV 91
Cdd:cd02801 70 AEAAKIVEELGADGIdlnMG---CPSPkvTKGGAGAALLKDPelvaEIVRAVREAVPIPVTVKIRLGwddeeETLElAKA 146
|
....*....
gi 518367314 92 LEALGVDYI 100
Cdd:cd02801 147 LEDAGASAL 155
|
|
| trpC |
PRK00278 |
indole-3-glycerol phosphate synthase TrpC; |
213-253 |
8.04e-04 |
|
indole-3-glycerol phosphate synthase TrpC;
Pssm-ID: 234710 Cd Length: 260 Bit Score: 40.14 E-value: 8.04e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 518367314 213 GVATPADAALMMHLGADGVFVGSGIFKSDNPEKFAKAIVEA 253
Cdd:PRK00278 219 GIFTPEDLKRLAKAGADAVLVGESLMRADDPGAALRELLGA 259
|
|
| NanE |
cd04729 |
N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to ... |
192-237 |
1.11e-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: 39.48 E-value: 1.11e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 518367314 192 YELLLQVHETGRLPVVnfAAGGVATPADAALMMHLGADGVFVGSGI 237
Cdd:cd04729 166 FELLKELRKALGIPVI--AEGRINSPEQAAKALELGADAVVVGSAI 209
|
|
| YrpB |
COG2070 |
NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General ... |
191-254 |
1.81e-03 |
|
NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General function prediction only];
Pssm-ID: 441673 [Multi-domain] Cd Length: 302 Bit Score: 39.32 E-value: 1.81e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518367314 191 PYELLLQVHETGRLPVVnfAAGGVATPADAALMMHLGADGVFVGSGiF----KSDNPEKFAKAIVEAT 254
Cdd:COG2070 146 TFALVPEVRDAVDIPVI--AAGGIADGRGIAAALALGADGVQMGTR-FlateESPAHEAYKQALVDAK 210
|
|
| DUF561 |
pfam04481 |
Protein of unknown function (DUF561); Protein of unknown function found in a cyanobacterium, ... |
30-270 |
1.88e-03 |
|
Protein of unknown function (DUF561); Protein of unknown function found in a cyanobacterium, and the chloroplasts of algae.
Pssm-ID: 113257 Cd Length: 243 Bit Score: 38.96 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518367314 30 AKIAEAAGASAVmalervpsDIraaggvarMADPTIVEEVMKVVSIPVMAKArighfVEAKVL---EALGVDYID----- 101
Cdd:pfam04481 33 ARASQIAKATYV--------DI--------AADPQLVKVVKSVSNIPICVSA-----VEPELLyeaVLAGADLVEignfd 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518367314 102 ---ESEVLTPADEVFHINKR----------EFTVPFVCGARD---LGEALRRIgeGASMIRTKGepGTGNIVEAVRHMRM 165
Cdd:pfam04481 92 sfyKQGRVLSVCEIIALVKEtrkllphtplCVTIPHILKLKEqinLAKQLESL--GIDLIQTEG--KITSISKNHCVNDL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518367314 166 mvsqIRKVqnmskdelmneAKLLGAPYELLLQVhetgRLPVVnfAAGGVaTPADAALMMHLGADGVFVGSGIFKSDNPEK 245
Cdd:pfam04481 168 ----IEKS-----------ASTLASTYEISKHV----QLPVI--CASGL-SDVTVPLAFSYGASGIGIGSAVSKLNDIEK 225
|
250 260
....*....|....*....|....*
gi 518367314 246 FAKAIveatthyedYELIANISKNL 270
Cdd:pfam04481 226 MVNYI---------SEIKKAISGTR 241
|
|
| KGPDC_HPS |
cd04726 |
3-Keto-L-gulonate 6-phosphate decarboxylase (KGPDC) and D-arabino-3-hexulose-6-phosphate ... |
152-250 |
2.37e-03 |
|
3-Keto-L-gulonate 6-phosphate decarboxylase (KGPDC) and D-arabino-3-hexulose-6-phosphate synthase (HPS). KGPDC catalyzes the formation of L-xylulose 5-phosphate and carbon dioxide from 3-keto-L-gulonate 6-phosphate as part of the anaerobic pathway for L-ascorbate utilization in some eubacteria. HPS catalyzes the formation of D-arabino-3-hexulose-6-phosphate from D-ribulose 5-phosphate and formaldehyde in microorganisms that can use formaldehyde as a carbon source. Both catalyze reactions that involve the Mg2+-assisted formation and stabilization of 1,2-enediolate reaction intermediates.
Pssm-ID: 240077 [Multi-domain] Cd Length: 202 Bit Score: 38.33 E-value: 2.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518367314 152 GTGNIVEAVRHMRMMVSQIrkVQNMSKDElmnEAKLLGAPYELLLQVHETGRLPVVnfAAGGVaTPADAALMMHLGADGV 231
Cdd:cd04726 112 GVEDPEKRAKLLKLGVDIV--ILHRGIDA---QAAGGWWPEDDLKKVKKLLGVKVA--VAGGI-TPDTLPEFKKAGADIV 183
|
90
....*....|....*....
gi 518367314 232 FVGSGIFKSDNPEKFAKAI 250
Cdd:cd04726 184 IVGRAITGAADPAEAAREF 202
|
|
| HisA_HisF |
cd04723 |
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase (HisA) ... |
193-237 |
6.28e-03 |
|
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase (HisA) and the cyclase subunit of imidazoleglycerol phosphate synthase (HisF). The ProFAR isomerase catalyzes the fourth step in histidine biosynthesis, an isomerisation of the aminoaldose moiety of ProFAR to the aminoketose of PRFAR (N-(5'-phospho-D-1'-ribulosylformimino)-5-amino-1-(5''-phospho-ribosyl)-4-imidazolecarboxamide). In bacteria and archaea, ProFAR isomerase is encoded by the HisA gene. The Imidazole glycerol phosphate synthase (IGPS) catalyzes the fifth step of histidine biosynthesis, the formation of the imidazole ring. IGPS converts N1-(5'-phosphoribulosyl)-formimino-5-aminoimidazole-4-carboxamide ribonucleotide (PRFAR) to imidazole glycerol phosphate (ImGP) and 5'-(5-aminoimidazole-4-carboxamide) ribonucleotide (AICAR). This conversion involves two tightly coupled reactions in distinct active sites of IGPS. The two catalytic domains can be fused, like in fungi and plants, or peformed by a heterodimer (HisH-glutaminase and HisF-cyclase), like in bacteria.
Pssm-ID: 240074 [Multi-domain] Cd Length: 233 Bit Score: 37.25 E-value: 6.28e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 518367314 193 ELLLQVHETGRLPVVnfAAGGVATPADAALMMHLGADGVFVGSGI 237
Cdd:cd04723 179 ELLERLAARADIPVI--AAGGVRSVEDLELLKKLGASGALVASAL 221
|
|
| |
