|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02591 |
PLN02591 |
tryptophan synthase |
61-310 |
8.59e-163 |
|
tryptophan synthase
Pssm-ID: 178201 Cd Length: 250 Bit Score: 452.97 E-value: 8.59e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224085571 61 KVALIPYITAGDPDLSTTAEALKLLDACGCDIIELGVPYSDPLADGPVIQAAATRSLARGTNFEAITSMLKEVVPQVSCP 140
Cdd:PLN02591 1 KVAFIPYITAGDPDLDTTAEALRLLDACGADVIELGVPYSDPLADGPVIQAAATRALEKGTTLDSVISMLKEVAPQLSCP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224085571 141 IALFTYYNPILKRGIEKFMSTVNDIGVHGLVVPDVPLEETQVLRKEAVKNGLELVLLTTPTTPTERMKAIVEAADGFVYL 220
Cdd:PLN02591 81 IVLFTYYNPILKRGIDKFMATIKEAGVHGLVVPDLPLEETEALRAEAAKNGIELVLLTTPTTPTERMKAIAEASEGFVYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224085571 221 VSSVGVTGTRASVSDRVQTLLQDIKETTTKPVAVGFGISKPEHVKQVAGWGADGVIVGSAMVKLLGEAKSPEEGLKELES 300
Cdd:PLN02591 161 VSSTGVTGARASVSGRVESLLQELKEVTDKPVAVGFGISKPEHAKQIAGWGADGVIVGSAMVKALGEAKSPEEGLKRLEK 240
|
250
....*....|
gi 224085571 301 FTKSLKAALP 310
Cdd:PLN02591 241 LAKSLKAALP 250
|
|
| TrpA |
COG0159 |
Tryptophan synthase alpha chain [Amino acid transport and metabolism]; Tryptophan synthase ... |
49-309 |
1.11e-112 |
|
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: 326.64 E-value: 1.11e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224085571 49 IGETFSNLKKQGKVALIPYITAGDPDLSTTAEALKLLDACGCDIIELGVPYSDPLADGPVIQAAATRSLARGTNFEAITS 128
Cdd:COG0159 3 IDAAFAALKAEGRKALIPYLTAGDPDLETTLEIIKALVEAGADIIELGIPFSDPVADGPVIQAASERALANGVTLDDVFE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224085571 129 MLKEVVPQVSCPIALFTYYNPILKRGIEKFMSTVNDIGVHGLVVPDVPLEETQVLRKEAVKNGLELVLLTTPTTPTERMK 208
Cdd:COG0159 83 LVREFREDPDTPLVLMGYYNPVFRYGVERFAADAAEAGVDGLIVPDLPPEEAEELRAAADAHGLDLIFLVAPTTSDERIK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224085571 209 AIVEAADGFVYLVSSVGVTGTRASVSDRVQTLLQDIKETTTKPVAVGFGISKPEHVKQVAGWgADGVIVGSAMVKLLGEA 288
Cdd:COG0159 163 KIAAAASGFVYYVSVTGVTGARTAVSDDLAELVARIRAHTDLPVAVGFGISTPEQAAEVAAY-ADGVIVGSALVKLIEEG 241
|
250 260
....*....|....*....|.
gi 224085571 289 KSpEEGLKELESFTKSLKAAL 309
Cdd:COG0159 242 GD-DEALEALAAFVRELKAAL 261
|
|
| Tryptophan_synthase_alpha |
cd04724 |
Ttryptophan synthase (TRPS) alpha subunit (TSA). TPRS is a bifunctional tetrameric enzyme (2 ... |
63-306 |
5.18e-103 |
|
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: 301.32 E-value: 5.18e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224085571 63 ALIPYITAGDPDLSTTAEALKLLDACGCDIIELGVPYSDPLADGPVIQAAATRSLARGTNFEAITSMLKEVVPQVSCPIA 142
Cdd:cd04724 1 ALIPYITAGDPDLETTLEILKALVEAGADIIELGIPFSDPVADGPVIQAASERALANGVTLKDVLELVKEIRKKNTIPIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224085571 143 LFTYYNPILKRGIEKFMSTVNDIGVHGLVVPDVPLEETQVLRKEAVKNGLELVLLTTPTTPTERMKAIVEAADGFVYLVS 222
Cdd:cd04724 81 LMGYYNPILQYGLERFLRDAKEAGVDGLIIPDLPPEEAEEFREAAKEYGLDLIFLVAPTTPDERIKKIAELASGFIYYVS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224085571 223 SVGVTGTRASVSDRVQTLLQDIKETTTKPVAVGFGISKPEHVKQVAGWgADGVIVGSAMVKLLGEAKsPEEGLKELESFT 302
Cdd:cd04724 161 RTGVTGARTELPDDLKELIKRIRKYTDLPIAVGFGISTPEQAAEVAKY-ADGVIVGSALVKIIEEGG-EEEALEALKELA 238
|
....
gi 224085571 303 KSLK 306
Cdd:cd04724 239 ESLK 242
|
|
| Trp_syntA |
pfam00290 |
Tryptophan synthase alpha chain; |
53-309 |
7.43e-102 |
|
Tryptophan synthase alpha chain;
Pssm-ID: 395227 Cd Length: 258 Bit Score: 298.84 E-value: 7.43e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224085571 53 FSNLKKQGKVALIPYITAGDPDLSTTAEALKLLDACGCDIIELGVPYSDPLADGPVIQAAATRSLARGTNFEAITSMLKE 132
Cdd:pfam00290 1 FANLKAENRAAFVPYVTAGDPDLEQSLEILKTLEKAGADAIELGVPFSDPLADGPTIQRANLRALASGVTLQSTLEMVRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224085571 133 V-VPQVSCPIALFTYYNPILKRGIEKFMSTVNDIGVHGLVVPDVPLEETQVLRKEAVKNGLELVLLTTPTTPTERMKAIV 211
Cdd:pfam00290 81 VrSKGVEVPIVLMTYYNPVLNYGIERFYALAAEAGVDGLIVPDLPPEEADSLRQAAKDHGLELVFLVAPTTSDERLKTVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224085571 212 EAADGFVYLVSSVGVTGTRASVSDRVQTLLQDIKETTTKPVAVGFGISKPEHVKQVAgWGADGVIVGSAMVKLLGE-AKS 290
Cdd:pfam00290 161 EQAEGFVYLVSRAGVTGAENAVNAQVDELVERLKKYTAVPVAVGFGISTPEHVKQAA-AGADGVIVGSALVRIIEEaADG 239
|
250
....*....|....*....
gi 224085571 291 PEEGLKELESFTKSLKAAL 309
Cdd:pfam00290 240 PEQGLARLEELAGEMKAAA 258
|
|
| trpA |
TIGR00262 |
tryptophan synthase, alpha subunit; Tryptophan synthase catalyzes the last step in the ... |
53-306 |
2.30e-93 |
|
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: 277.30 E-value: 2.30e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224085571 53 FSNLKKQGKVALIPYITAGDPDLSTTAEALKLLDACGCDIIELGVPYSDPLADGPVIQAAATRSLARGTNFEAITSMLKE 132
Cdd:TIGR00262 1 FETLKQRGEGAFIPFVTAGDPTLETSLEIIKTLIEAGADALELGVPFSDPLADGPTIQAADLRALRAGMTPEKCFELLKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224085571 133 VVPQ-VSCPIALFTYYNPILKRGIEKFMSTVNDIGVHGLVVPDVPLEETQVLRKEAVKNGLELVLLTTPTTPTERMKAIV 211
Cdd:TIGR00262 81 VRQKhPNIPIGLLTYYNLIFRKGVEEFYAKCKEVGVDGVLVADLPLEESGDLVEAAKKHGVKPIFLVAPNADDERLKQIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224085571 212 EAADGFVYLVSSVGVTGTRASVSDRVQTLLQDIKETTTKPVAVGFGISKPEHVKQVAGWGADGVIVGSAMVKLLGE-AKS 290
Cdd:TIGR00262 161 EKSQGFVYLVSRAGVTGARNRAASALNELVKRLKAYSAKPVLVGFGISKPEQVKQAIDAGADGVIVGSAIVKIIEEnLNT 240
|
250
....*....|....*.
gi 224085571 291 PEEGLKELESFTKSLK 306
Cdd:TIGR00262 241 PEKMLQALEEFVQNLK 256
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02591 |
PLN02591 |
tryptophan synthase |
61-310 |
8.59e-163 |
|
tryptophan synthase
Pssm-ID: 178201 Cd Length: 250 Bit Score: 452.97 E-value: 8.59e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224085571 61 KVALIPYITAGDPDLSTTAEALKLLDACGCDIIELGVPYSDPLADGPVIQAAATRSLARGTNFEAITSMLKEVVPQVSCP 140
Cdd:PLN02591 1 KVAFIPYITAGDPDLDTTAEALRLLDACGADVIELGVPYSDPLADGPVIQAAATRALEKGTTLDSVISMLKEVAPQLSCP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224085571 141 IALFTYYNPILKRGIEKFMSTVNDIGVHGLVVPDVPLEETQVLRKEAVKNGLELVLLTTPTTPTERMKAIVEAADGFVYL 220
Cdd:PLN02591 81 IVLFTYYNPILKRGIDKFMATIKEAGVHGLVVPDLPLEETEALRAEAAKNGIELVLLTTPTTPTERMKAIAEASEGFVYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224085571 221 VSSVGVTGTRASVSDRVQTLLQDIKETTTKPVAVGFGISKPEHVKQVAGWGADGVIVGSAMVKLLGEAKSPEEGLKELES 300
Cdd:PLN02591 161 VSSTGVTGARASVSGRVESLLQELKEVTDKPVAVGFGISKPEHAKQIAGWGADGVIVGSAMVKALGEAKSPEEGLKRLEK 240
|
250
....*....|
gi 224085571 301 FTKSLKAALP 310
Cdd:PLN02591 241 LAKSLKAALP 250
|
|
| trpA |
PRK13111 |
tryptophan synthase subunit alpha; Provisional |
51-309 |
3.78e-113 |
|
tryptophan synthase subunit alpha; Provisional
Pssm-ID: 237285 Cd Length: 258 Bit Score: 327.45 E-value: 3.78e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224085571 51 ETFSNLKKQGKVALIPYITAGDPDLSTTAEALKLLDACGCDIIELGVPYSDPLADGPVIQAAATRSLARGTNFEAITSML 130
Cdd:PRK13111 1 ALFAALKAEGRKALIPYITAGDPDLETSLEIIKALVEAGADIIELGIPFSDPVADGPVIQAASLRALAAGVTLADVFELV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224085571 131 KEV-VPQVSCPIALFTYYNPILKRGIEKFMSTVNDIGVHGLVVPDVPLEETQVLRKEAVKNGLELVLLTTPTTPTERMKA 209
Cdd:PRK13111 81 REIrEKDPTIPIVLMTYYNPIFQYGVERFAADAAEAGVDGLIIPDLPPEEAEELRAAAKKHGLDLIFLVAPTTTDERLKK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224085571 210 IVEAADGFVYLVSSVGVTGTRASVSDRVQTLLQDIKETTTKPVAVGFGISKPEHVKQVAGwGADGVIVGSAMVKLLGEAk 289
Cdd:PRK13111 161 IASHASGFVYYVSRAGVTGARSADAADLAELVARLKAHTDLPVAVGFGISTPEQAAAIAA-VADGVIVGSALVKIIEEN- 238
|
250 260
....*....|....*....|
gi 224085571 290 spEEGLKELESFTKSLKAAL 309
Cdd:PRK13111 239 --PEALEALAAFVKELKAAL 256
|
|
| TrpA |
COG0159 |
Tryptophan synthase alpha chain [Amino acid transport and metabolism]; Tryptophan synthase ... |
49-309 |
1.11e-112 |
|
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: 326.64 E-value: 1.11e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224085571 49 IGETFSNLKKQGKVALIPYITAGDPDLSTTAEALKLLDACGCDIIELGVPYSDPLADGPVIQAAATRSLARGTNFEAITS 128
Cdd:COG0159 3 IDAAFAALKAEGRKALIPYLTAGDPDLETTLEIIKALVEAGADIIELGIPFSDPVADGPVIQAASERALANGVTLDDVFE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224085571 129 MLKEVVPQVSCPIALFTYYNPILKRGIEKFMSTVNDIGVHGLVVPDVPLEETQVLRKEAVKNGLELVLLTTPTTPTERMK 208
Cdd:COG0159 83 LVREFREDPDTPLVLMGYYNPVFRYGVERFAADAAEAGVDGLIVPDLPPEEAEELRAAADAHGLDLIFLVAPTTSDERIK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224085571 209 AIVEAADGFVYLVSSVGVTGTRASVSDRVQTLLQDIKETTTKPVAVGFGISKPEHVKQVAGWgADGVIVGSAMVKLLGEA 288
Cdd:COG0159 163 KIAAAASGFVYYVSVTGVTGARTAVSDDLAELVARIRAHTDLPVAVGFGISTPEQAAEVAAY-ADGVIVGSALVKLIEEG 241
|
250 260
....*....|....*....|.
gi 224085571 289 KSpEEGLKELESFTKSLKAAL 309
Cdd:COG0159 242 GD-DEALEALAAFVRELKAAL 261
|
|
| Tryptophan_synthase_alpha |
cd04724 |
Ttryptophan synthase (TRPS) alpha subunit (TSA). TPRS is a bifunctional tetrameric enzyme (2 ... |
63-306 |
5.18e-103 |
|
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: 301.32 E-value: 5.18e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224085571 63 ALIPYITAGDPDLSTTAEALKLLDACGCDIIELGVPYSDPLADGPVIQAAATRSLARGTNFEAITSMLKEVVPQVSCPIA 142
Cdd:cd04724 1 ALIPYITAGDPDLETTLEILKALVEAGADIIELGIPFSDPVADGPVIQAASERALANGVTLKDVLELVKEIRKKNTIPIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224085571 143 LFTYYNPILKRGIEKFMSTVNDIGVHGLVVPDVPLEETQVLRKEAVKNGLELVLLTTPTTPTERMKAIVEAADGFVYLVS 222
Cdd:cd04724 81 LMGYYNPILQYGLERFLRDAKEAGVDGLIIPDLPPEEAEEFREAAKEYGLDLIFLVAPTTPDERIKKIAELASGFIYYVS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224085571 223 SVGVTGTRASVSDRVQTLLQDIKETTTKPVAVGFGISKPEHVKQVAGWgADGVIVGSAMVKLLGEAKsPEEGLKELESFT 302
Cdd:cd04724 161 RTGVTGARTELPDDLKELIKRIRKYTDLPIAVGFGISTPEQAAEVAKY-ADGVIVGSALVKIIEEGG-EEEALEALKELA 238
|
....
gi 224085571 303 KSLK 306
Cdd:cd04724 239 ESLK 242
|
|
| Trp_syntA |
pfam00290 |
Tryptophan synthase alpha chain; |
53-309 |
7.43e-102 |
|
Tryptophan synthase alpha chain;
Pssm-ID: 395227 Cd Length: 258 Bit Score: 298.84 E-value: 7.43e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224085571 53 FSNLKKQGKVALIPYITAGDPDLSTTAEALKLLDACGCDIIELGVPYSDPLADGPVIQAAATRSLARGTNFEAITSMLKE 132
Cdd:pfam00290 1 FANLKAENRAAFVPYVTAGDPDLEQSLEILKTLEKAGADAIELGVPFSDPLADGPTIQRANLRALASGVTLQSTLEMVRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224085571 133 V-VPQVSCPIALFTYYNPILKRGIEKFMSTVNDIGVHGLVVPDVPLEETQVLRKEAVKNGLELVLLTTPTTPTERMKAIV 211
Cdd:pfam00290 81 VrSKGVEVPIVLMTYYNPVLNYGIERFYALAAEAGVDGLIVPDLPPEEADSLRQAAKDHGLELVFLVAPTTSDERLKTVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224085571 212 EAADGFVYLVSSVGVTGTRASVSDRVQTLLQDIKETTTKPVAVGFGISKPEHVKQVAgWGADGVIVGSAMVKLLGE-AKS 290
Cdd:pfam00290 161 EQAEGFVYLVSRAGVTGAENAVNAQVDELVERLKKYTAVPVAVGFGISTPEHVKQAA-AGADGVIVGSALVRIIEEaADG 239
|
250
....*....|....*....
gi 224085571 291 PEEGLKELESFTKSLKAAL 309
Cdd:pfam00290 240 PEQGLARLEELAGEMKAAA 258
|
|
| trpA |
CHL00200 |
tryptophan synthase alpha subunit; Provisional |
49-309 |
1.22e-95 |
|
tryptophan synthase alpha subunit; Provisional
Pssm-ID: 214394 Cd Length: 263 Bit Score: 283.58 E-value: 1.22e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224085571 49 IGETFSNLKKQgkVALIPYITAGDPDLSTTAEALKLLDACGCDIIELGVPYSDPLADGPVIQAAATRSLARGTNFEAITS 128
Cdd:CHL00200 4 ISNVFEKLDKQ--CALIPFITAGDPDIVITKKALKILDKKGADIIELGIPYSDPLADGPIIQEASNRALKQGINLNKILS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224085571 129 MLKEVVPQVSCPIALFTYYNPILKRGIEKFMSTVNDIGVHGLVVPDVPLEETQVLRKEAVKNGLELVLLTTPTTPTERMK 208
Cdd:CHL00200 82 ILSEVNGEIKAPIVIFTYYNPVLHYGINKFIKKISQAGVKGLIIPDLPYEESDYLISVCNLYNIELILLIAPTSSKSRIQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224085571 209 AIVEAADGFVYLVSSVGVTGTRASVSDRVQTLLQDIKETTTKPVAVGFGISKPEHVKQVAGWGADGVIVGSAMVK-LLGE 287
Cdd:CHL00200 162 KIARAAPGCIYLVSTTGVTGLKTELDKKLKKLIETIKKMTNKPIILGFGISTSEQIKQIKGWNINGIVIGSACVQiLLGS 241
|
250 260
....*....|....*....|..
gi 224085571 288 akSPEEGLKELESFTKSLKAAL 309
Cdd:CHL00200 242 --SPEKGLDQLSEFCKVAKKSI 261
|
|
| trpA |
TIGR00262 |
tryptophan synthase, alpha subunit; Tryptophan synthase catalyzes the last step in the ... |
53-306 |
2.30e-93 |
|
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: 277.30 E-value: 2.30e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224085571 53 FSNLKKQGKVALIPYITAGDPDLSTTAEALKLLDACGCDIIELGVPYSDPLADGPVIQAAATRSLARGTNFEAITSMLKE 132
Cdd:TIGR00262 1 FETLKQRGEGAFIPFVTAGDPTLETSLEIIKTLIEAGADALELGVPFSDPLADGPTIQAADLRALRAGMTPEKCFELLKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224085571 133 VVPQ-VSCPIALFTYYNPILKRGIEKFMSTVNDIGVHGLVVPDVPLEETQVLRKEAVKNGLELVLLTTPTTPTERMKAIV 211
Cdd:TIGR00262 81 VRQKhPNIPIGLLTYYNLIFRKGVEEFYAKCKEVGVDGVLVADLPLEESGDLVEAAKKHGVKPIFLVAPNADDERLKQIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224085571 212 EAADGFVYLVSSVGVTGTRASVSDRVQTLLQDIKETTTKPVAVGFGISKPEHVKQVAGWGADGVIVGSAMVKLLGE-AKS 290
Cdd:TIGR00262 161 EKSQGFVYLVSRAGVTGARNRAASALNELVKRLKAYSAKPVLVGFGISKPEQVKQAIDAGADGVIVGSAIVKIIEEnLNT 240
|
250
....*....|....*.
gi 224085571 291 PEEGLKELESFTKSLK 306
Cdd:TIGR00262 241 PEKMLQALEEFVQNLK 256
|
|
| trpA |
PRK13125 |
tryptophan synthase subunit alpha; Provisional |
63-310 |
1.04e-21 |
|
tryptophan synthase subunit alpha; Provisional
Pssm-ID: 237286 Cd Length: 244 Bit Score: 91.64 E-value: 1.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224085571 63 ALIPYITAGDPDLSTTAEALKLLDACgCDIIELGVPYSDPLADGPVIQAAAtrslaRGTNFEAITSMLKEVVPQVSCPIA 142
Cdd:PRK13125 5 GLVVYLTAGYPNVESFKEFIIGLVEL-VDILELGIPPKYPKYDGPVIRKSH-----RKVKGLDIWPLLEEVRKDVSVPII 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224085571 143 LFTYYNPILKRgIEKFMSTVNDIGVHGLVVPDVPL---EETQVLRKEAVKNGLELVLLTTPTTPTERMKAIVEAADGFVY 219
Cdd:PRK13125 79 LMTYLEDYVDS-LDNFLNMARDVGADGVLFPDLLIdypDDLEKYVEIIKNKGLKPVFFTSPKFPDLLIHRLSKLSPLFIY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224085571 220 LvssvGV---TGTRASVS-----DRVQTLLQDiketttKPVAVGFGISKPEHVKQVAGWGADGVIVGSAMVKLLgEAKSP 291
Cdd:PRK13125 158 Y----GLrpaTGVPLPVSverniKRVRNLVGN------KYLVVGFGLDSPEDARDALSAGADGVVVGTAFIEEL-EKNGV 226
|
250
....*....|....*....
gi 224085571 292 EEGLkeleSFTKSLKAALP 310
Cdd:PRK13125 227 ESAL----NLLKKIRGALD 241
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
64-279 |
2.02e-06 |
|
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: 47.58 E-value: 2.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224085571 64 LIPYITAGDPDlSTTAEALKLLDACGCDIIELGVPYSDPLADGPVIQAAAtrslargtnfeaitsmlKEVVPQVSCPIAL 143
Cdd:cd04722 1 VILALLAGGPS-GDPVELAKAAAEAGADAIIVGTRSSDPEEAETDDKEVL-----------------KEVAAETDLPLGV 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224085571 144 FTYYNPILK-RGIEKFMSTVN-----DIGVHGLVVPDVPLEETQVLRKEAvkNGLELVLLTTPTTPTERMKAIVEAADgF 217
Cdd:cd04722 63 QLAINDAAAaVDIAAAAARAAgadgvEIHGAVGYLAREDLELIRELREAV--PDVKVVVKLSPTGELAAAAAEEAGVD-E 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 224085571 218 VYLVSSVGVTGTRaSVSDRVQTLLQDIKETTTKPVAVGFGISKPEHVKQVAGWGADGVIVGS 279
Cdd:cd04722 140 VGLGNGGGGGGGR-DAVPIADLLLILAKRGSKVPVIAGGGINDPEDAAEALALGADGVIVGS 200
|
|
| IGPS |
cd00331 |
Indole-3-glycerol phosphate synthase (IGPS); an enzyme in the tryptophan biosynthetic pathway, ... |
257-298 |
8.57e-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: 42.84 E-value: 8.57e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 224085571 257 GISKPEHVKQVAGWGADGVIVGSAMVKllgeAKSPEEGLKEL 298
Cdd:cd00331 180 GISTPEDVKRLAEAGADAVLIGESLMR----APDPGAALREL 217
|
|
| HisA_HisF |
cd04723 |
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase (HisA) ... |
240-281 |
1.45e-04 |
|
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: 42.26 E-value: 1.45e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 224085571 240 LLQDIKETTTKPVAVGFGISKPEHVKQVAGWGADGVIVGSAM 281
Cdd:cd04723 180 LLERLAARADIPVIAAGGVRSVEDLELLKKLGASGALVASAL 221
|
|
| NanE |
cd04729 |
N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to ... |
209-280 |
2.06e-04 |
|
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: 41.79 E-value: 2.06e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 224085571 209 AIVEAADGFVYLVSS-VGVTGTRASVSDRVQTLLQDIKETTTKPVAVGFGISKPEHVKQVAGWGADGVIVGSA 280
Cdd:cd04729 136 ALNAAKLGFDIIGTTlSGYTEETAKTEDPDFELLKELRKALGIPVIAEGRINSPEQAAKALELGADAVVVGSA 208
|
|
| His_biosynth |
pfam00977 |
Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine ... |
240-281 |
4.33e-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: 40.92 E-value: 4.33e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 224085571 240 LLQDIKETTTKPVAVGFGISKPEHVKQVAGWGADGVIVGSAM 281
Cdd:pfam00977 181 LTRELAEAVNIPVIASGGVGSLEDLKELFTEGVDGVIAGSAL 222
|
|
| trpC |
PRK00278 |
indole-3-glycerol phosphate synthase TrpC; |
257-298 |
5.68e-04 |
|
indole-3-glycerol phosphate synthase TrpC;
Pssm-ID: 234710 Cd Length: 260 Bit Score: 40.91 E-value: 5.68e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 224085571 257 GISKPEHVKQVAGWGADGVIVGSAMVKllgeAKSPEEGLKEL 298
Cdd:PRK00278 219 GIFTPEDLKRLAKAGADAVLVGESLMR----ADDPGAALREL 256
|
|
| PRK04302 |
PRK04302 |
triosephosphate isomerase; Provisional |
228-298 |
2.17e-03 |
|
triosephosphate isomerase; Provisional
Pssm-ID: 235274 Cd Length: 223 Bit Score: 38.70 E-value: 2.17e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 224085571 228 GTRASVS----DRVQTLLQDIKETTTK-PVAVGFGISKPEHVKQVAGWGADGVIVGSAMVKllgeAKSPEEGLKEL 298
Cdd:PRK04302 147 GTGIPVSkakpEVVEDAVEAVKKVNPDvKVLCGAGISTGEDVKAALELGADGVLLASGVVK----AKDPEAALRDL 218
|
|
| HisA |
COG0106 |
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase [Amino ... |
240-280 |
4.13e-03 |
|
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase [Amino acid transport and metabolism]; Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase is part of the Pathway/BioSystem: Histidine biosynthesis
Pssm-ID: 439876 Cd Length: 236 Bit Score: 38.10 E-value: 4.13e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 224085571 240 LLQDIKETTTKPVAVGFGISKPEHVKQVAGWGADGVIVGSA 280
Cdd:COG0106 180 LYRELAAATGIPVIASGGVSSLDDLRALKELGVEGAIVGKA 220
|
|
| His_biosynth |
pfam00977 |
Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine ... |
240-283 |
4.35e-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: 37.84 E-value: 4.35e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 224085571 240 LLQDIKETTTKPVAVGFGISKPEHVKQVAGWGADGVIVGSAMVK 283
Cdd:pfam00977 64 VVEEIAEEVFIPVQVGGGIRSLEDVERLLSAGADRVIIGTAAVK 107
|
|
| |
