|
Name |
Accession |
Description |
Interval |
E-value |
| TrpA |
COG0159 |
Tryptophan synthase alpha chain [Amino acid transport and metabolism]; Tryptophan synthase ... |
2-268 |
2.89e-136 |
|
Tryptophan synthase alpha chain [Amino acid transport and metabolism]; Tryptophan synthase alpha chain is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
Pssm-ID: 439929 Cd Length: 262 Bit Score: 385.19 E-value: 2.89e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225035406 2 SRIAATFDALKKDGRRALIPYVTAGFPFADITPELMHGMVEAGADVIELGVPFSDPMADGPVIQKAGEAALALGIGMKQV 81
Cdd:COG0159 1 SRIDAAFAALKAEGRKALIPYLTAGDPDLETTLEIIKALVEAGADIIELGIPFSDPVADGPVIQAASERALANGVTLDDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225035406 82 LAIVAAFRqKDSTTPVVLMGYANPVERYdlvhGKKAFIRDAVAAGVDGLLVVDYPPEECEDFAAELKAAGIDLIFLLAPT 161
Cdd:COG0159 81 FELVREFR-EDPDTPLVLMGYYNPVFRY----GVERFAADAAEAGVDGLIVPDLPPEEAEELRAAADAHGLDLIFLVAPT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225035406 162 STDERMAQVARIASGYVYYVSLKGVTGAGHLDTEAVGQMVPRIRQHLSIPVGVGFGIRDARTAQAVGSAADAVIIGTKII 241
Cdd:COG0159 156 TSDERIKKIAAAASGFVYYVSVTGVTGARTAVSDDLAELVARIRAHTDLPVAVGFGISTPEQAAEVAAYADGVIVGSALV 235
|
250 260
....*....|....*....|....*..
gi 1225035406 242 QLIEDQPRERVVPAVREFLAGIREALD 268
Cdd:COG0159 236 KLIEEGGDDEALEALAAFVRELKAALR 262
|
|
| trpA |
PRK13111 |
tryptophan synthase subunit alpha; Provisional |
6-269 |
6.61e-133 |
|
tryptophan synthase subunit alpha; Provisional
Pssm-ID: 237285 Cd Length: 258 Bit Score: 376.37 E-value: 6.61e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225035406 6 ATFDALKKDGRRALIPYVTAGFPFADITPELMHGMVEAGADVIELGVPFSDPMADGPVIQKAGEAALALGIGMKQVLAIV 85
Cdd:PRK13111 1 ALFAALKAEGRKALIPYITAGDPDLETSLEIIKALVEAGADIIELGIPFSDPVADGPVIQAASLRALAAGVTLADVFELV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225035406 86 AAFRQKDSTTPVVLMGYANPVERYdlvhGKKAFIRDAVAAGVDGLLVVDYPPEECEDFAAELKAAGIDLIFLLAPTSTDE 165
Cdd:PRK13111 81 REIREKDPTIPIVLMTYYNPIFQY----GVERFAADAAEAGVDGLIIPDLPPEEAEELRAAAKKHGLDLIFLVAPTTTDE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225035406 166 RMAQVARIASGYVYYVSLKGVTGAGHLDTEAVGQMVPRIRQHLSIPVGVGFGIRDARTAQAVGSAADAVIIGTKIIQLIE 245
Cdd:PRK13111 157 RLKKIASHASGFVYYVSRAGVTGARSADAADLAELVARLKAHTDLPVAVGFGISTPEQAAAIAAVADGVIVGSALVKIIE 236
|
250 260
....*....|....*....|....
gi 1225035406 246 DQPreRVVPAVREFLAGIREALDA 269
Cdd:PRK13111 237 ENP--EALEALAAFVKELKAALRS 258
|
|
| Tryptophan_synthase_alpha |
cd04724 |
Ttryptophan synthase (TRPS) alpha subunit (TSA). TPRS is a bifunctional tetrameric enzyme (2 ... |
18-264 |
1.99e-112 |
|
Ttryptophan synthase (TRPS) alpha subunit (TSA). TPRS is a bifunctional tetrameric enzyme (2 alpha and 2 beta subunits) that catalyzes the last two steps of L-tryptophan biosynthesis. Alpha and beta subunit catalyze two distinct reactions which are both strongly stimulated by the formation of the complex. The alpha subunit catalyzes the cleavage of indole 3-glycerol phosphate (IGP) to indole and d-glyceraldehyde 3-phosphate (G3P). Indole is then channeled to the active site of the beta subunit, a PLP-dependent enzyme that catalyzes a replacement reaction to convert L-serine into L-tryptophan.
Pssm-ID: 240075 Cd Length: 242 Bit Score: 324.04 E-value: 1.99e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225035406 18 ALIPYVTAGFPFADITPELMHGMVEAGADVIELGVPFSDPMADGPVIQKAGEAALALGIGMKQVLAIVAAFRQKDsTTPV 97
Cdd:cd04724 1 ALIPYITAGDPDLETTLEILKALVEAGADIIELGIPFSDPVADGPVIQAASERALANGVTLKDVLELVKEIRKKN-TIPI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225035406 98 VLMGYANPVERYdlvhGKKAFIRDAVAAGVDGLLVVDYPPEECEDFAAELKAAGIDLIFLLAPTSTDERMAQVARIASGY 177
Cdd:cd04724 80 VLMGYYNPILQY----GLERFLRDAKEAGVDGLIIPDLPPEEAEEFREAAKEYGLDLIFLVAPTTPDERIKKIAELASGF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225035406 178 VYYVSLKGVTGAGHLDTEAVGQMVPRIRQHLSIPVGVGFGIRDARTAQAVGSAADAVIIGTKIIQLIEDQPRERVVPAVR 257
Cdd:cd04724 156 IYYVSRTGVTGARTELPDDLKELIKRIRKYTDLPIAVGFGISTPEQAAEVAKYADGVIVGSALVKIIEEGGEEEALEALK 235
|
....*..
gi 1225035406 258 EFLAGIR 264
Cdd:cd04724 236 ELAESLK 242
|
|
| Trp_syntA |
pfam00290 |
Tryptophan synthase alpha chain; |
8-258 |
1.40e-90 |
|
Tryptophan synthase alpha chain;
Pssm-ID: 395227 Cd Length: 258 Bit Score: 269.18 E-value: 1.40e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225035406 8 FDALKKDGRRALIPYVTAGFPFADITPELMHGMVEAGADVIELGVPFSDPMADGPVIQKAGEAALALGIGMKQVLAIVAA 87
Cdd:pfam00290 1 FANLKAENRAAFVPYVTAGDPDLEQSLEILKTLEKAGADAIELGVPFSDPLADGPTIQRANLRALASGVTLQSTLEMVRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225035406 88 FRQKDSTTPVVLMGYANPVERYdlvhGKKAFIRDAVAAGVDGLLVVDYPPEECEDFAAELKAAGIDLIFLLAPTSTDERM 167
Cdd:pfam00290 81 VRSKGVEVPIVLMTYYNPVLNY----GIERFYALAAEAGVDGLIVPDLPPEEADSLRQAAKDHGLELVFLVAPTTSDERL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225035406 168 AQVARIASGYVYYVSLKGVTGAGHLDTEAVGQMVPRIRQHLSIPVGVGFGIRDARTAQAVGSAADAVIIGTKIIQLIEDQ 247
Cdd:pfam00290 157 KTVVEQAEGFVYLVSRAGVTGAENAVNAQVDELVERLKKYTAVPVAVGFGISTPEHVKQAAAGADGVIVGSALVRIIEEA 236
|
250
....*....|.
gi 1225035406 248 PRERVVPAVRE 258
Cdd:pfam00290 237 ADGPEQGLARL 247
|
|
| trpA |
TIGR00262 |
tryptophan synthase, alpha subunit; Tryptophan synthase catalyzes the last step in the ... |
8-264 |
1.43e-75 |
|
tryptophan synthase, alpha subunit; Tryptophan synthase catalyzes the last step in the biosynthesis of tryptophan. The alpha chain is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. In bacteria and plants each domain is found on a separate subunit (alpha and beta chains), while in fungi the two domains are fused together on a single multifunctional protein. The signature pattern for trpA contains three conserved acidic residues. [LIVM]-E-[LIVM]-G-x(2)-[FYC]-[ST]-[DE]-[PA]-[LIVMY]-[AGLI]-[DE]-G and this is located between residues 43-58 of the model. The Sulfolobus solfataricus trpA is known to be quite divergent from other known trpA sequences. [Amino acid biosynthesis, Aromatic amino acid family]
Pssm-ID: 161792 Cd Length: 256 Bit Score: 231.08 E-value: 1.43e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225035406 8 FDALKKDGRRALIPYVTAGFPFADITPELMHGMVEAGADVIELGVPFSDPMADGPVIQKAGEAALALGIGMKQVLAIVAA 87
Cdd:TIGR00262 1 FETLKQRGEGAFIPFVTAGDPTLETSLEIIKTLIEAGADALELGVPFSDPLADGPTIQAADLRALRAGMTPEKCFELLKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225035406 88 FRQKDSTTPVVLMGYANPVERYdlvhGKKAFIRDAVAAGVDGLLVVDYPPEECEDFAAELKAAGIDLIFLLAPTSTDERM 167
Cdd:TIGR00262 81 VRQKHPNIPIGLLTYYNLIFRK----GVEEFYAKCKEVGVDGVLVADLPLEESGDLVEAAKKHGVKPIFLVAPNADDERL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225035406 168 AQVARIASGYVYYVSLKGVTGAGHLDTEAVGQMVPRIRQHLSIPVGVGFGIRDARTA-QAVGSAADAVIIGTKIIQLIED 246
Cdd:TIGR00262 157 KQIAEKSQGFVYLVSRAGVTGARNRAASALNELVKRLKAYSAKPVLVGFGISKPEQVkQAIDAGADGVIVGSAIVKIIEE 236
|
250 260
....*....|....*....|
gi 1225035406 247 --QPRERVVPAVREFLAGIR 264
Cdd:TIGR00262 237 nlNTPEKMLQALEEFVQNLK 256
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| TrpA |
COG0159 |
Tryptophan synthase alpha chain [Amino acid transport and metabolism]; Tryptophan synthase ... |
2-268 |
2.89e-136 |
|
Tryptophan synthase alpha chain [Amino acid transport and metabolism]; Tryptophan synthase alpha chain is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
Pssm-ID: 439929 Cd Length: 262 Bit Score: 385.19 E-value: 2.89e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225035406 2 SRIAATFDALKKDGRRALIPYVTAGFPFADITPELMHGMVEAGADVIELGVPFSDPMADGPVIQKAGEAALALGIGMKQV 81
Cdd:COG0159 1 SRIDAAFAALKAEGRKALIPYLTAGDPDLETTLEIIKALVEAGADIIELGIPFSDPVADGPVIQAASERALANGVTLDDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225035406 82 LAIVAAFRqKDSTTPVVLMGYANPVERYdlvhGKKAFIRDAVAAGVDGLLVVDYPPEECEDFAAELKAAGIDLIFLLAPT 161
Cdd:COG0159 81 FELVREFR-EDPDTPLVLMGYYNPVFRY----GVERFAADAAEAGVDGLIVPDLPPEEAEELRAAADAHGLDLIFLVAPT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225035406 162 STDERMAQVARIASGYVYYVSLKGVTGAGHLDTEAVGQMVPRIRQHLSIPVGVGFGIRDARTAQAVGSAADAVIIGTKII 241
Cdd:COG0159 156 TSDERIKKIAAAASGFVYYVSVTGVTGARTAVSDDLAELVARIRAHTDLPVAVGFGISTPEQAAEVAAYADGVIVGSALV 235
|
250 260
....*....|....*....|....*..
gi 1225035406 242 QLIEDQPRERVVPAVREFLAGIREALD 268
Cdd:COG0159 236 KLIEEGGDDEALEALAAFVRELKAALR 262
|
|
| trpA |
PRK13111 |
tryptophan synthase subunit alpha; Provisional |
6-269 |
6.61e-133 |
|
tryptophan synthase subunit alpha; Provisional
Pssm-ID: 237285 Cd Length: 258 Bit Score: 376.37 E-value: 6.61e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225035406 6 ATFDALKKDGRRALIPYVTAGFPFADITPELMHGMVEAGADVIELGVPFSDPMADGPVIQKAGEAALALGIGMKQVLAIV 85
Cdd:PRK13111 1 ALFAALKAEGRKALIPYITAGDPDLETSLEIIKALVEAGADIIELGIPFSDPVADGPVIQAASLRALAAGVTLADVFELV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225035406 86 AAFRQKDSTTPVVLMGYANPVERYdlvhGKKAFIRDAVAAGVDGLLVVDYPPEECEDFAAELKAAGIDLIFLLAPTSTDE 165
Cdd:PRK13111 81 REIREKDPTIPIVLMTYYNPIFQY----GVERFAADAAEAGVDGLIIPDLPPEEAEELRAAAKKHGLDLIFLVAPTTTDE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225035406 166 RMAQVARIASGYVYYVSLKGVTGAGHLDTEAVGQMVPRIRQHLSIPVGVGFGIRDARTAQAVGSAADAVIIGTKIIQLIE 245
Cdd:PRK13111 157 RLKKIASHASGFVYYVSRAGVTGARSADAADLAELVARLKAHTDLPVAVGFGISTPEQAAAIAAVADGVIVGSALVKIIE 236
|
250 260
....*....|....*....|....
gi 1225035406 246 DQPreRVVPAVREFLAGIREALDA 269
Cdd:PRK13111 237 ENP--EALEALAAFVKELKAALRS 258
|
|
| Tryptophan_synthase_alpha |
cd04724 |
Ttryptophan synthase (TRPS) alpha subunit (TSA). TPRS is a bifunctional tetrameric enzyme (2 ... |
18-264 |
1.99e-112 |
|
Ttryptophan synthase (TRPS) alpha subunit (TSA). TPRS is a bifunctional tetrameric enzyme (2 alpha and 2 beta subunits) that catalyzes the last two steps of L-tryptophan biosynthesis. Alpha and beta subunit catalyze two distinct reactions which are both strongly stimulated by the formation of the complex. The alpha subunit catalyzes the cleavage of indole 3-glycerol phosphate (IGP) to indole and d-glyceraldehyde 3-phosphate (G3P). Indole is then channeled to the active site of the beta subunit, a PLP-dependent enzyme that catalyzes a replacement reaction to convert L-serine into L-tryptophan.
Pssm-ID: 240075 Cd Length: 242 Bit Score: 324.04 E-value: 1.99e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225035406 18 ALIPYVTAGFPFADITPELMHGMVEAGADVIELGVPFSDPMADGPVIQKAGEAALALGIGMKQVLAIVAAFRQKDsTTPV 97
Cdd:cd04724 1 ALIPYITAGDPDLETTLEILKALVEAGADIIELGIPFSDPVADGPVIQAASERALANGVTLKDVLELVKEIRKKN-TIPI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225035406 98 VLMGYANPVERYdlvhGKKAFIRDAVAAGVDGLLVVDYPPEECEDFAAELKAAGIDLIFLLAPTSTDERMAQVARIASGY 177
Cdd:cd04724 80 VLMGYYNPILQY----GLERFLRDAKEAGVDGLIIPDLPPEEAEEFREAAKEYGLDLIFLVAPTTPDERIKKIAELASGF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225035406 178 VYYVSLKGVTGAGHLDTEAVGQMVPRIRQHLSIPVGVGFGIRDARTAQAVGSAADAVIIGTKIIQLIEDQPRERVVPAVR 257
Cdd:cd04724 156 IYYVSRTGVTGARTELPDDLKELIKRIRKYTDLPIAVGFGISTPEQAAEVAKYADGVIVGSALVKIIEEGGEEEALEALK 235
|
....*..
gi 1225035406 258 EFLAGIR 264
Cdd:cd04724 236 ELAESLK 242
|
|
| Trp_syntA |
pfam00290 |
Tryptophan synthase alpha chain; |
8-258 |
1.40e-90 |
|
Tryptophan synthase alpha chain;
Pssm-ID: 395227 Cd Length: 258 Bit Score: 269.18 E-value: 1.40e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225035406 8 FDALKKDGRRALIPYVTAGFPFADITPELMHGMVEAGADVIELGVPFSDPMADGPVIQKAGEAALALGIGMKQVLAIVAA 87
Cdd:pfam00290 1 FANLKAENRAAFVPYVTAGDPDLEQSLEILKTLEKAGADAIELGVPFSDPLADGPTIQRANLRALASGVTLQSTLEMVRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225035406 88 FRQKDSTTPVVLMGYANPVERYdlvhGKKAFIRDAVAAGVDGLLVVDYPPEECEDFAAELKAAGIDLIFLLAPTSTDERM 167
Cdd:pfam00290 81 VRSKGVEVPIVLMTYYNPVLNY----GIERFYALAAEAGVDGLIVPDLPPEEADSLRQAAKDHGLELVFLVAPTTSDERL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225035406 168 AQVARIASGYVYYVSLKGVTGAGHLDTEAVGQMVPRIRQHLSIPVGVGFGIRDARTAQAVGSAADAVIIGTKIIQLIEDQ 247
Cdd:pfam00290 157 KTVVEQAEGFVYLVSRAGVTGAENAVNAQVDELVERLKKYTAVPVAVGFGISTPEHVKQAAAGADGVIVGSALVRIIEEA 236
|
250
....*....|.
gi 1225035406 248 PRERVVPAVRE 258
Cdd:pfam00290 237 ADGPEQGLARL 247
|
|
| trpA |
TIGR00262 |
tryptophan synthase, alpha subunit; Tryptophan synthase catalyzes the last step in the ... |
8-264 |
1.43e-75 |
|
tryptophan synthase, alpha subunit; Tryptophan synthase catalyzes the last step in the biosynthesis of tryptophan. The alpha chain is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. In bacteria and plants each domain is found on a separate subunit (alpha and beta chains), while in fungi the two domains are fused together on a single multifunctional protein. The signature pattern for trpA contains three conserved acidic residues. [LIVM]-E-[LIVM]-G-x(2)-[FYC]-[ST]-[DE]-[PA]-[LIVMY]-[AGLI]-[DE]-G and this is located between residues 43-58 of the model. The Sulfolobus solfataricus trpA is known to be quite divergent from other known trpA sequences. [Amino acid biosynthesis, Aromatic amino acid family]
Pssm-ID: 161792 Cd Length: 256 Bit Score: 231.08 E-value: 1.43e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225035406 8 FDALKKDGRRALIPYVTAGFPFADITPELMHGMVEAGADVIELGVPFSDPMADGPVIQKAGEAALALGIGMKQVLAIVAA 87
Cdd:TIGR00262 1 FETLKQRGEGAFIPFVTAGDPTLETSLEIIKTLIEAGADALELGVPFSDPLADGPTIQAADLRALRAGMTPEKCFELLKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225035406 88 FRQKDSTTPVVLMGYANPVERYdlvhGKKAFIRDAVAAGVDGLLVVDYPPEECEDFAAELKAAGIDLIFLLAPTSTDERM 167
Cdd:TIGR00262 81 VRQKHPNIPIGLLTYYNLIFRK----GVEEFYAKCKEVGVDGVLVADLPLEESGDLVEAAKKHGVKPIFLVAPNADDERL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225035406 168 AQVARIASGYVYYVSLKGVTGAGHLDTEAVGQMVPRIRQHLSIPVGVGFGIRDARTA-QAVGSAADAVIIGTKIIQLIED 246
Cdd:TIGR00262 157 KQIAEKSQGFVYLVSRAGVTGARNRAASALNELVKRLKAYSAKPVLVGFGISKPEQVkQAIDAGADGVIVGSAIVKIIEE 236
|
250 260
....*....|....*....|
gi 1225035406 247 --QPRERVVPAVREFLAGIR 264
Cdd:TIGR00262 237 nlNTPEKMLQALEEFVQNLK 256
|
|
| PLN02591 |
PLN02591 |
tryptophan synthase |
16-268 |
1.79e-57 |
|
tryptophan synthase
Pssm-ID: 178201 Cd Length: 250 Bit Score: 184.49 E-value: 1.79e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225035406 16 RRALIPYVTAGFPFADITPELMHGMVEAGADVIELGVPFSDPMADGPVIQKAGEAALALGIGMKQVLAIVAAFRQKDStT 95
Cdd:PLN02591 1 KVAFIPYITAGDPDLDTTAEALRLLDACGADVIELGVPYSDPLADGPVIQAAATRALEKGTTLDSVISMLKEVAPQLS-C 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225035406 96 PVVLMGYANPVERydlvHGKKAFIRDAVAAGVDGLLVVDYPPEECEDFAAELKAAGIDLIFLLAPTSTDERMAQVARIAS 175
Cdd:PLN02591 80 PIVLFTYYNPILK----RGIDKFMATIKEAGVHGLVVPDLPLEETEALRAEAAKNGIELVLLTTPTTPTERMKAIAEASE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225035406 176 GYVYYVSLKGVTGAGHLDTEAVGQMVPRIRQHLSIPVGVGFGI-RDARTAQAVGSAADAVIIGTKII-QLIEDQPRERVV 253
Cdd:PLN02591 156 GFVYLVSSTGVTGARASVSGRVESLLQELKEVTDKPVAVGFGIsKPEHAKQIAGWGADGVIVGSAMVkALGEAKSPEEGL 235
|
250
....*....|....*
gi 1225035406 254 PAVREFLAGIREALD 268
Cdd:PLN02591 236 KRLEKLAKSLKAALP 250
|
|
| trpA |
CHL00200 |
tryptophan synthase alpha subunit; Provisional |
1-267 |
7.14e-57 |
|
tryptophan synthase alpha subunit; Provisional
Pssm-ID: 214394 Cd Length: 263 Bit Score: 183.43 E-value: 7.14e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225035406 1 MSRIAATFDALKKdgRRALIPYVTAGFPFADITPELMHGMVEAGADVIELGVPFSDPMADGPVIQKAGEAALALGIGMKQ 80
Cdd:CHL00200 1 MNTISNVFEKLDK--QCALIPFITAGDPDIVITKKALKILDKKGADIIELGIPYSDPLADGPIIQEASNRALKQGINLNK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225035406 81 VLAIVAAFRQkDSTTPVVLMGYANPVerydLVHGKKAFIRDAVAAGVDGLLVVDYPPEECEDFAAELKAAGIDLIFLLAP 160
Cdd:CHL00200 79 ILSILSEVNG-EIKAPIVIFTYYNPV----LHYGINKFIKKISQAGVKGLIIPDLPYEESDYLISVCNLYNIELILLIAP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225035406 161 TSTDERMAQVARIASGYVYYVSLKGVTGaghLDTEAVGQ---MVPRIRQHLSIPVGVGFGIRDAR-TAQAVGSAADAVII 236
Cdd:CHL00200 154 TSSKSRIQKIARAAPGCIYLVSTTGVTG---LKTELDKKlkkLIETIKKMTNKPIILGFGISTSEqIKQIKGWNINGIVI 230
|
250 260 270
....*....|....*....|....*....|.
gi 1225035406 237 GTKIIQLIEDQPRERVVPAVREFLAGIREAL 267
Cdd:CHL00200 231 GSACVQILLGSSPEKGLDQLSEFCKVAKKSI 261
|
|
| trpA |
PRK13125 |
tryptophan synthase subunit alpha; Provisional |
16-268 |
1.17e-23 |
|
tryptophan synthase subunit alpha; Provisional
Pssm-ID: 237286 Cd Length: 244 Bit Score: 96.26 E-value: 1.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225035406 16 RRALIPYVTAGFPFADITPELMHGMVEAgADVIELGVPFSDPMADGPVIQKAGEAALALGIgmkqvLAIVAAFRQKDStT 95
Cdd:PRK13125 3 RPGLVVYLTAGYPNVESFKEFIIGLVEL-VDILELGIPPKYPKYDGPVIRKSHRKVKGLDI-----WPLLEEVRKDVS-V 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225035406 96 PVVLMGYANpveryDLVHGKKAFIRDAVAAGVDGLLVVDYP---PEECEDFAAELKAAGIDLIFLLAPTSTDERMAQVAR 172
Cdd:PRK13125 76 PIILMTYLE-----DYVDSLDNFLNMARDVGADGVLFPDLLidyPDDLEKYVEIIKNKGLKPVFFTSPKFPDLLIHRLSK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225035406 173 IASGYVYYvSLKGVTGaghldTE---AVGQMVPRIRQHL-SIPVGVGFGIRDARTAQAVGSA-ADAVIIGTKIIQLIEdq 247
Cdd:PRK13125 151 LSPLFIYY-GLRPATG-----VPlpvSVERNIKRVRNLVgNKYLVVGFGLDSPEDARDALSAgADGVVVGTAFIEELE-- 222
|
250 260
....*....|....*....|.
gi 1225035406 248 pRERVVPAvREFLAGIREALD 268
Cdd:PRK13125 223 -KNGVESA-LNLLKKIRGALD 241
|
|
| His_biosynth |
pfam00977 |
Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine ... |
200-256 |
7.67e-04 |
|
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: 39.77 E-value: 7.67e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1225035406 200 MVPRIRQHLSIPVGVGFGIRDARTAQAVGSA-ADAVIIGTK-------IIQLIEDQPRERVVPAV 256
Cdd:pfam00977 64 VVEEIAEEVFIPVQVGGGIRSLEDVERLLSAgADRVIIGTAavknpelIKEAAEKFGSQCIVVAI 128
|
|
| FadH |
COG1902 |
2,4-dienoyl-CoA reductase or related NADH-dependent reductase, Old Yellow Enzyme (OYE) family ... |
134-237 |
1.31e-03 |
|
2,4-dienoyl-CoA reductase or related NADH-dependent reductase, Old Yellow Enzyme (OYE) family [Energy production and conversion];
Pssm-ID: 441506 [Multi-domain] Cd Length: 365 Bit Score: 39.77 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225035406 134 DYPPEECEDFAAELKAAGIDLIFLLAPtSTDERMAQVARIASGYvyyvslkgvtgagHLDteavgqMVPRIRQHLSIPVG 213
Cdd:COG1902 232 GLTLEESVELAKALEEAGVDYLHVSSG-GYEPDAMIPTIVPEGY-------------QLP------FAARIRKAVGIPVI 291
|
90 100
....*....|....*....|....*..
gi 1225035406 214 VGFGIRDARTAQAV---GsAADAVIIG 237
Cdd:COG1902 292 AVGGITTPEQAEAAlasG-DADLVALG 317
|
|
| HisA |
cd04732 |
HisA. Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase ... |
203-256 |
1.41e-03 |
|
HisA. Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (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.
Pssm-ID: 240083 Cd Length: 234 Bit Score: 39.00 E-value: 1.41e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1225035406 203 RIRQHLSIPVGVGFGIRDARTAQAVGSA-ADAVIIGTKII-------QLIEDQPRERVVPAV 256
Cdd:cd04732 67 EIVKAVGIPVQVGGGIRSLEDIERLLDLgVSRVIIGTAAVknpelvkELLKEYGGERIVVGL 128
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
28-238 |
1.46e-03 |
|
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: 38.72 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225035406 28 PFADITPELMHGMVEAGADVIELGVPFSDPMADGPVIQKAgeaalalgigMKQVLAIVAAfrqkdsttPVVLMGYANpvE 107
Cdd:cd04722 9 GPSGDPVELAKAAAEAGADAIIVGTRSSDPEEAETDDKEV----------LKEVAAETDL--------PLGVQLAIN--D 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225035406 108 RYDLVHGKKAFIRDAVAAGVDGLLVVDYPPEECEDFAAELKAAGIDLIFLLAPTSTDER-MAQVARIASGYVYYVSlKGV 186
Cdd:cd04722 69 AAAAVDIAAAAARAAGADGVEIHGAVGYLAREDLELIRELREAVPDVKVVVKLSPTGELaAAAAEEAGVDEVGLGN-GGG 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1225035406 187 TGAGHLDTEAVGQMVPRIRQHLSIPVGVGFGIRDARTA-QAVGSAADAVIIGT 238
Cdd:cd04722 148 GGGGRDAVPIADLLLILAKRGSKVPVIAGGGINDPEDAaEALALGADGVIVGS 200
|
|
| PRK04169 |
PRK04169 |
heptaprenylglyceryl phosphate synthase; |
200-264 |
2.58e-03 |
|
heptaprenylglyceryl phosphate synthase;
Pssm-ID: 235237 Cd Length: 232 Bit Score: 38.25 E-value: 2.58e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1225035406 200 MVPRIRQHLSI-PVGVGFGIRDARTA-QAVGSAADAVIIGTkiiqLIEDQPRErvvpAVREFLAGIR 264
Cdd:PRK04169 174 MVKAVKKALDItPLIYGGGIRSPEQArELMAAGADTIVVGN----IIEEDPKK----TVKAIKKAIK 232
|
|
| |
