|
Name |
Accession |
Description |
Interval |
E-value |
| trpA |
PRK13111 |
tryptophan synthase subunit alpha; Provisional |
4-254 |
2.40e-123 |
|
tryptophan synthase subunit alpha; Provisional
Pssm-ID: 237285 Cd Length: 258 Bit Score: 351.33 E-value: 2.40e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459984 4 EKIKAAFENGKKVFIPYVMGGDGGLEKLKERIRFLDEAGASIVEIGIPFSDPVADGPTIQRAGKRALDSGVTLKGIFQAL 83
Cdd:PRK13111 1 ALFAALKAEGRKALIPYITAGDPDLETSLEIIKALVEAGADIIELGIPFSDPVADGPVIQAASLRALAAGVTLADVFELV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459984 84 AEVR-KEVQMPFVLMTYLNPVLAFGKERFIENCIEAGVDGIIVPDLPYEEQNIIAPLLREANIALIPLVTVTSPIERIEK 162
Cdd:PRK13111 81 REIReKDPTIPIVLMTYYNPIFQYGVERFAADAAEAGVDGLIIPDLPPEEAEELRAAAKKHGLDLIFLVAPTTTDERLKK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459984 163 ITSESEGFVYAVTVAGVTGVRQNFKEEIHSYLEKVKSHVNLPVVAGFGISTKEHVEEMVTICDGVVVGSKIIELLENEKR 242
Cdd:PRK13111 161 IASHASGFVYYVSRAGVTGARSADAADLAELVARLKAHTDLPVAVGFGISTPEQAAAIAAVADGVIVGSALVKIIEENPE 240
|
250
....*....|....
gi 446459984 243 --EEICELIYATKQ 254
Cdd:PRK13111 241 alEALAAFVKELKA 254
|
|
| TrpA |
COG0159 |
Tryptophan synthase alpha chain [Amino acid transport and metabolism]; Tryptophan synthase ... |
4-249 |
2.17e-121 |
|
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: 346.28 E-value: 2.17e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459984 4 EKIKAAFE----NGKKVFIPYVMGGDGGLEKLKERIRFLDEAGASIVEIGIPFSDPVADGPTIQRAGKRALDSGVTLKGI 79
Cdd:COG0159 1 SRIDAAFAalkaEGRKALIPYLTAGDPDLETTLEIIKALVEAGADIIELGIPFSDPVADGPVIQAASERALANGVTLDDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459984 80 FQALAEVRKEVQMPFVLMTYLNPVLAFGKERFIENCIEAGVDGIIVPDLPYEEQNIIAPLLREANIALIPLVTVTSPIER 159
Cdd:COG0159 81 FELVREFREDPDTPLVLMGYYNPVFRYGVERFAADAAEAGVDGLIVPDLPPEEAEELRAAADAHGLDLIFLVAPTTSDER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459984 160 IEKITSESEGFVYAVTVAGVTGVRQNFKEEIHSYLEKVKSHVNLPVVAGFGISTKEHVEEMVTICDGVVVGSKIIELLEN 239
Cdd:COG0159 161 IKKIAAAASGFVYYVSVTGVTGARTAVSDDLAELVARIRAHTDLPVAVGFGISTPEQAAEVAAYADGVIVGSALVKLIEE 240
|
250
....*....|
gi 446459984 240 EKREEICELI 249
Cdd:COG0159 241 GGDDEALEAL 250
|
|
| Tryptophan_synthase_alpha |
cd04724 |
Ttryptophan synthase (TRPS) alpha subunit (TSA). TPRS is a bifunctional tetrameric enzyme (2 ... |
17-249 |
1.80e-114 |
|
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: 328.28 E-value: 1.80e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459984 17 FIPYVMGGDGGLEKLKERIRFLDEAGASIVEIGIPFSDPVADGPTIQRAGKRALDSGVTLKGIFQALAEVRKEVQMPFVL 96
Cdd:cd04724 2 LIPYITAGDPDLETTLEILKALVEAGADIIELGIPFSDPVADGPVIQAASERALANGVTLKDVLELVKEIRKKNTIPIVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459984 97 MTYLNPVLAFGKERFIENCIEAGVDGIIVPDLPYEEQNIIAPLLREANIALIPLVTVTSPIERIEKITSESEGFVYAVTV 176
Cdd:cd04724 82 MGYYNPILQYGLERFLRDAKEAGVDGLIIPDLPPEEAEEFREAAKEYGLDLIFLVAPTTPDERIKKIAELASGFIYYVSR 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446459984 177 AGVTGVRQNFKEEIHSYLEKVKSHVNLPVVAGFGISTKEHVEEMVTICDGVVVGSKIIELLENEKREEICELI 249
Cdd:cd04724 162 TGVTGARTELPDDLKELIKRIRKYTDLPIAVGFGISTPEQAAEVAKYADGVIVGSALVKIIEEGGEEEALEAL 234
|
|
| Trp_syntA |
pfam00290 |
Tryptophan synthase alpha chain; |
7-249 |
4.36e-98 |
|
Tryptophan synthase alpha chain;
Pssm-ID: 395227 Cd Length: 258 Bit Score: 287.28 E-value: 4.36e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459984 7 KAAFENGKKVFIPYVMGGDGGLEKLKERIRFLDEAGASIVEIGIPFSDPVADGPTIQRAGKRALDSGVTLKGIFQALAEV 86
Cdd:pfam00290 2 ANLKAENRAAFVPYVTAGDPDLEQSLEILKTLEKAGADAIELGVPFSDPLADGPTIQRANLRALASGVTLQSTLEMVREV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459984 87 R-KEVQMPFVLMTYLNPVLAFGKERFIENCIEAGVDGIIVPDLPYEEQNIIAPLLREANIALIPLVTVTSPIERIEKITS 165
Cdd:pfam00290 82 RsKGVEVPIVLMTYYNPVLNYGIERFYALAAEAGVDGLIVPDLPPEEADSLRQAAKDHGLELVFLVAPTTSDERLKTVVE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459984 166 ESEGFVYAVTVAGVTGVRQNFKEEIHSYLEKVKSHVNLPVVAGFGISTKEHVEEMVTICDGVVVGSKIIELLENEKREEI 245
Cdd:pfam00290 162 QAEGFVYLVSRAGVTGAENAVNAQVDELVERLKKYTAVPVAVGFGISTPEHVKQAAAGADGVIVGSALVRIIEEAADGPE 241
|
....
gi 446459984 246 CELI 249
Cdd:pfam00290 242 QGLA 245
|
|
| trpA |
TIGR00262 |
tryptophan synthase, alpha subunit; Tryptophan synthase catalyzes the last step in the ... |
13-244 |
3.87e-80 |
|
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: 241.48 E-value: 3.87e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459984 13 GKKVFIPYVMGGDGGLEKLKERIRFLDEAGASIVEIGIPFSDPVADGPTIQRAGKRALDSGVTLKGIFQALAEVRKE-VQ 91
Cdd:TIGR00262 8 GEGAFIPFVTAGDPTLETSLEIIKTLIEAGADALELGVPFSDPLADGPTIQAADLRALRAGMTPEKCFELLKKVRQKhPN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459984 92 MPFVLMTYLNPVLAFGKERFIENCIEAGVDGIIVPDLPYEEQNiiaPLLREA---NIALIPLVTVTSPIERIEKITSESE 168
Cdd:TIGR00262 88 IPIGLLTYYNLIFRKGVEEFYAKCKEVGVDGVLVADLPLEESG---DLVEAAkkhGVKPIFLVAPNADDERLKQIAEKSQ 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446459984 169 GFVYAVTVAGVTGVRQNFKEEIHSYLEKVKSHVNLPVVAGFGISTKEHVEEMVTI-CDGVVVGSKIIELLENEKREE 244
Cdd:TIGR00262 165 GFVYLVSRAGVTGARNRAASALNELVKRLKAYSAKPVLVGFGISKPEQVKQAIDAgADGVIVGSAIVKIIEENLNTP 241
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| trpA |
PRK13111 |
tryptophan synthase subunit alpha; Provisional |
4-254 |
2.40e-123 |
|
tryptophan synthase subunit alpha; Provisional
Pssm-ID: 237285 Cd Length: 258 Bit Score: 351.33 E-value: 2.40e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459984 4 EKIKAAFENGKKVFIPYVMGGDGGLEKLKERIRFLDEAGASIVEIGIPFSDPVADGPTIQRAGKRALDSGVTLKGIFQAL 83
Cdd:PRK13111 1 ALFAALKAEGRKALIPYITAGDPDLETSLEIIKALVEAGADIIELGIPFSDPVADGPVIQAASLRALAAGVTLADVFELV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459984 84 AEVR-KEVQMPFVLMTYLNPVLAFGKERFIENCIEAGVDGIIVPDLPYEEQNIIAPLLREANIALIPLVTVTSPIERIEK 162
Cdd:PRK13111 81 REIReKDPTIPIVLMTYYNPIFQYGVERFAADAAEAGVDGLIIPDLPPEEAEELRAAAKKHGLDLIFLVAPTTTDERLKK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459984 163 ITSESEGFVYAVTVAGVTGVRQNFKEEIHSYLEKVKSHVNLPVVAGFGISTKEHVEEMVTICDGVVVGSKIIELLENEKR 242
Cdd:PRK13111 161 IASHASGFVYYVSRAGVTGARSADAADLAELVARLKAHTDLPVAVGFGISTPEQAAAIAAVADGVIVGSALVKIIEENPE 240
|
250
....*....|....
gi 446459984 243 --EEICELIYATKQ 254
Cdd:PRK13111 241 alEALAAFVKELKA 254
|
|
| TrpA |
COG0159 |
Tryptophan synthase alpha chain [Amino acid transport and metabolism]; Tryptophan synthase ... |
4-249 |
2.17e-121 |
|
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: 346.28 E-value: 2.17e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459984 4 EKIKAAFE----NGKKVFIPYVMGGDGGLEKLKERIRFLDEAGASIVEIGIPFSDPVADGPTIQRAGKRALDSGVTLKGI 79
Cdd:COG0159 1 SRIDAAFAalkaEGRKALIPYLTAGDPDLETTLEIIKALVEAGADIIELGIPFSDPVADGPVIQAASERALANGVTLDDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459984 80 FQALAEVRKEVQMPFVLMTYLNPVLAFGKERFIENCIEAGVDGIIVPDLPYEEQNIIAPLLREANIALIPLVTVTSPIER 159
Cdd:COG0159 81 FELVREFREDPDTPLVLMGYYNPVFRYGVERFAADAAEAGVDGLIVPDLPPEEAEELRAAADAHGLDLIFLVAPTTSDER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459984 160 IEKITSESEGFVYAVTVAGVTGVRQNFKEEIHSYLEKVKSHVNLPVVAGFGISTKEHVEEMVTICDGVVVGSKIIELLEN 239
Cdd:COG0159 161 IKKIAAAASGFVYYVSVTGVTGARTAVSDDLAELVARIRAHTDLPVAVGFGISTPEQAAEVAAYADGVIVGSALVKLIEE 240
|
250
....*....|
gi 446459984 240 EKREEICELI 249
Cdd:COG0159 241 GGDDEALEAL 250
|
|
| Tryptophan_synthase_alpha |
cd04724 |
Ttryptophan synthase (TRPS) alpha subunit (TSA). TPRS is a bifunctional tetrameric enzyme (2 ... |
17-249 |
1.80e-114 |
|
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: 328.28 E-value: 1.80e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459984 17 FIPYVMGGDGGLEKLKERIRFLDEAGASIVEIGIPFSDPVADGPTIQRAGKRALDSGVTLKGIFQALAEVRKEVQMPFVL 96
Cdd:cd04724 2 LIPYITAGDPDLETTLEILKALVEAGADIIELGIPFSDPVADGPVIQAASERALANGVTLKDVLELVKEIRKKNTIPIVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459984 97 MTYLNPVLAFGKERFIENCIEAGVDGIIVPDLPYEEQNIIAPLLREANIALIPLVTVTSPIERIEKITSESEGFVYAVTV 176
Cdd:cd04724 82 MGYYNPILQYGLERFLRDAKEAGVDGLIIPDLPPEEAEEFREAAKEYGLDLIFLVAPTTPDERIKKIAELASGFIYYVSR 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446459984 177 AGVTGVRQNFKEEIHSYLEKVKSHVNLPVVAGFGISTKEHVEEMVTICDGVVVGSKIIELLENEKREEICELI 249
Cdd:cd04724 162 TGVTGARTELPDDLKELIKRIRKYTDLPIAVGFGISTPEQAAEVAKYADGVIVGSALVKIIEEGGEEEALEAL 234
|
|
| Trp_syntA |
pfam00290 |
Tryptophan synthase alpha chain; |
7-249 |
4.36e-98 |
|
Tryptophan synthase alpha chain;
Pssm-ID: 395227 Cd Length: 258 Bit Score: 287.28 E-value: 4.36e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459984 7 KAAFENGKKVFIPYVMGGDGGLEKLKERIRFLDEAGASIVEIGIPFSDPVADGPTIQRAGKRALDSGVTLKGIFQALAEV 86
Cdd:pfam00290 2 ANLKAENRAAFVPYVTAGDPDLEQSLEILKTLEKAGADAIELGVPFSDPLADGPTIQRANLRALASGVTLQSTLEMVREV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459984 87 R-KEVQMPFVLMTYLNPVLAFGKERFIENCIEAGVDGIIVPDLPYEEQNIIAPLLREANIALIPLVTVTSPIERIEKITS 165
Cdd:pfam00290 82 RsKGVEVPIVLMTYYNPVLNYGIERFYALAAEAGVDGLIVPDLPPEEADSLRQAAKDHGLELVFLVAPTTSDERLKTVVE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459984 166 ESEGFVYAVTVAGVTGVRQNFKEEIHSYLEKVKSHVNLPVVAGFGISTKEHVEEMVTICDGVVVGSKIIELLENEKREEI 245
Cdd:pfam00290 162 QAEGFVYLVSRAGVTGAENAVNAQVDELVERLKKYTAVPVAVGFGISTPEHVKQAAAGADGVIVGSALVRIIEEAADGPE 241
|
....
gi 446459984 246 CELI 249
Cdd:pfam00290 242 QGLA 245
|
|
| trpA |
TIGR00262 |
tryptophan synthase, alpha subunit; Tryptophan synthase catalyzes the last step in the ... |
13-244 |
3.87e-80 |
|
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: 241.48 E-value: 3.87e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459984 13 GKKVFIPYVMGGDGGLEKLKERIRFLDEAGASIVEIGIPFSDPVADGPTIQRAGKRALDSGVTLKGIFQALAEVRKE-VQ 91
Cdd:TIGR00262 8 GEGAFIPFVTAGDPTLETSLEIIKTLIEAGADALELGVPFSDPLADGPTIQAADLRALRAGMTPEKCFELLKKVRQKhPN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459984 92 MPFVLMTYLNPVLAFGKERFIENCIEAGVDGIIVPDLPYEEQNiiaPLLREA---NIALIPLVTVTSPIERIEKITSESE 168
Cdd:TIGR00262 88 IPIGLLTYYNLIFRKGVEEFYAKCKEVGVDGVLVADLPLEESG---DLVEAAkkhGVKPIFLVAPNADDERLKQIAEKSQ 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446459984 169 GFVYAVTVAGVTGVRQNFKEEIHSYLEKVKSHVNLPVVAGFGISTKEHVEEMVTI-CDGVVVGSKIIELLENEKREE 244
Cdd:TIGR00262 165 GFVYLVSRAGVTGARNRAASALNELVKRLKAYSAKPVLVGFGISKPEQVKQAIDAgADGVIVGSAIVKIIEENLNTP 241
|
|
| PLN02591 |
PLN02591 |
tryptophan synthase |
14-237 |
1.09e-73 |
|
tryptophan synthase
Pssm-ID: 178201 Cd Length: 250 Bit Score: 224.93 E-value: 1.09e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459984 14 KKVFIPYVMGGDGGLEKLKERIRFLDEAGASIVEIGIPFSDPVADGPTIQRAGKRALDSGVTLKGIFQALAEVRKEVQMP 93
Cdd:PLN02591 1 KVAFIPYITAGDPDLDTTAEALRLLDACGADVIELGVPYSDPLADGPVIQAAATRALEKGTTLDSVISMLKEVAPQLSCP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459984 94 FVLMTYLNPVLAFGKERFIENCIEAGVDGIIVPDLPYEEQNIIAPLLREANIALIPLVTVTSPIERIEKITSESEGFVYA 173
Cdd:PLN02591 81 IVLFTYYNPILKRGIDKFMATIKEAGVHGLVVPDLPLEETEALRAEAAKNGIELVLLTTPTTPTERMKAIAEASEGFVYL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446459984 174 VTVAGVTGVRQNFKEEIHSYLEKVKSHVNLPVVAGFGISTKEHVEEMVTI-CDGVVVGSKIIELL 237
Cdd:PLN02591 161 VSSTGVTGARASVSGRVESLLQELKEVTDKPVAVGFGISKPEHAKQIAGWgADGVIVGSAMVKAL 225
|
|
| trpA |
CHL00200 |
tryptophan synthase alpha subunit; Provisional |
6-244 |
8.59e-70 |
|
tryptophan synthase alpha subunit; Provisional
Pssm-ID: 214394 Cd Length: 263 Bit Score: 215.40 E-value: 8.59e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459984 6 IKAAFENGKK--VFIPYVMGGDGGLEKLKERIRFLDEAGASIVEIGIPFSDPVADGPTIQRAGKRALDSGVTLKGIFQAL 83
Cdd:CHL00200 4 ISNVFEKLDKqcALIPFITAGDPDIVITKKALKILDKKGADIIELGIPYSDPLADGPIIQEASNRALKQGINLNKILSIL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459984 84 AEVRKEVQMPFVLMTYLNPVLAFGKERFIENCIEAGVDGIIVPDLPYEEQNIIAPLLREANIALIPLVTVTSPIERIEKI 163
Cdd:CHL00200 84 SEVNGEIKAPIVIFTYYNPVLHYGINKFIKKISQAGVKGLIIPDLPYEESDYLISVCNLYNIELILLIAPTSSKSRIQKI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459984 164 TSESEGFVYAVTVAGVTGVRQNFKEEIHSYLEKVKSHVNLPVVAGFGISTKEHVEEMVTI-CDGVVVGSKIIELLENEKR 242
Cdd:CHL00200 164 ARAAPGCIYLVSTTGVTGLKTELDKKLKKLIETIKKMTNKPIILGFGISTSEQIKQIKGWnINGIVIGSACVQILLGSSP 243
|
..
gi 446459984 243 EE 244
Cdd:CHL00200 244 EK 245
|
|
| trpA |
PRK13125 |
tryptophan synthase subunit alpha; Provisional |
14-249 |
2.50e-20 |
|
tryptophan synthase subunit alpha; Provisional
Pssm-ID: 237286 Cd Length: 244 Bit Score: 86.63 E-value: 2.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459984 14 KKVFIPYVMGGDGGLEKLKERIRFLDEAgASIVEIGIPFSDPVADGPTIQRAGKraldsGVTLKGIFQALAEVRKEVQMP 93
Cdd:PRK13125 3 RPGLVVYLTAGYPNVESFKEFIIGLVEL-VDILELGIPPKYPKYDGPVIRKSHR-----KVKGLDIWPLLEEVRKDVSVP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459984 94 FVLMTYLNPVLAfGKERFIENCIEAGVDGIIVPDLPY---EEQNIIAPLLREANIALIPLVTVTSPIERIEKITSESEGF 170
Cdd:PRK13125 77 IILMTYLEDYVD-SLDNFLNMARDVGADGVLFPDLLIdypDDLEKYVEIIKNKGLKPVFFTSPKFPDLLIHRLSKLSPLF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459984 171 VYaVTVAGVTGVrqnfkeEIHSYLEKVKSHV-----NLPVVAGFGISTKEHVEEMVTI-CDGVVVGSKIIELLENEKREE 244
Cdd:PRK13125 156 IY-YGLRPATGV------PLPVSVERNIKRVrnlvgNKYLVVGFGLDSPEDARDALSAgADGVVVGTAFIEELEKNGVES 228
|
....*
gi 446459984 245 ICELI 249
Cdd:PRK13125 229 ALNLL 233
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
17-231 |
1.62e-08 |
|
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: 53.36 E-value: 1.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459984 17 FIPYVMGGdGGLEKLKERIRFLDEAGASIVEIGIPFSDPVADGPTIQRAgkraldsgvtlkgifqaLAEVRKEVQMPFVL 96
Cdd:cd04722 1 VILALLAG-GPSGDPVELAKAAAEAGADAIIVGTRSSDPEEAETDDKEV-----------------LKEVAAETDLPLGV 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459984 97 MTYLNPVLAFGKERFiENCIEAGVDGIIVPDLPYEEQNIIAPLLREANIAL--IPLVTVTSPIERIEKITSESEG--FVY 172
Cdd:cd04722 63 QLAINDAAAAVDIAA-AAARAAGADGVEIHGAVGYLAREDLELIRELREAVpdVKVVVKLSPTGELAAAAAEEAGvdEVG 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459984 173 AVTVAGVTGvRQNFKEEIHSYLEKVKSHVNLPVVAGFGISTKEHVEEMV-TICDGVVVGS 231
Cdd:cd04722 142 LGNGGGGGG-GRDAVPIADLLLILAKRGSKVPVIAGGGINDPEDAAEALaLGADGVIVGS 200
|
|
| NPD_like |
cd04730 |
2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes ... |
75-231 |
1.18e-03 |
|
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: 39.39 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459984 75 TLKGIFQALAEVRKEVQMPF-VLMTYLNPVLAFgkERFIENCIEAGVDGIIV---PDLPYEEQniiaplLREANIALIPl 150
Cdd:cd04730 37 TPEALRAEIRKIRALTDKPFgVNLLVPSSNPDF--EALLEVALEEGVPVVSFsfgPPAEVVER------LKAAGIKVIP- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459984 151 vTVTSPIErieKITSESEGfVYAVTVAGVT--GVRQNFKEEIHSYLEKVKSHVNLPVVAGFGISTKEHVEEMVTI-CDGV 227
Cdd:cd04730 108 -TVTSVEE---ARKAEAAG-ADALVAQGAEagGHRGTFDIGTFALVPEVRDAVDIPVIAAGGIADGRGIAAALALgADGV 182
|
....
gi 446459984 228 VVGS 231
Cdd:cd04730 183 QMGT 186
|
|
| BtpA |
COG0434 |
Membrane biogenesis protein, BtpA/SgcQ family [Cell wall/membrane/envelope biogenesis]; |
194-231 |
1.27e-03 |
|
Membrane biogenesis protein, BtpA/SgcQ family [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440203 Cd Length: 268 Bit Score: 39.39 E-value: 1.27e-03
10 20 30
....*....|....*....|....*....|....*....
gi 446459984 194 LEKVKSHV-NLPVVAGFGIsTKEHVEEMVTICDGVVVGS 231
Cdd:COG0434 203 LKRVKEAApDVPVLVGSGV-TPENVAELLSVADGAIVGS 240
|
|
| PBP1_ABC_sugar_binding-like |
cd01536 |
periplasmic sugar-binding domain of active transport systems that are members of the type 1 ... |
112-165 |
1.64e-03 |
|
periplasmic sugar-binding domain of active transport systems that are members of the type 1 periplasmic binding protein (PBP1) superfamily; Periplasmic sugar-binding domain of active transport systems that are members of the type 1 periplasmic binding protein (PBP1) superfamily. The members of this family function as the primary receptors for chemotaxis and transport of many sugar based solutes in bacteria and archaea. The sugar binding domain is also homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR. Moreover, this periplasmic binding domain, also known as Venus flytrap domain, undergoes transition from an open to a closed conformational state upon the binding of ligands such as lactose, ribose, fructose, xylose, arabinose, galactose/glucose, and other sugars. This family also includes the periplasmic binding domain of autoinducer-2 (AI-2) receptors such as LsrB and LuxP which are highly homologous to periplasmic pentose/hexose sugar-binding proteins.
Pssm-ID: 380478 [Multi-domain] Cd Length: 268 Bit Score: 39.09 E-value: 1.64e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 446459984 112 IENCIEAGVDGIIVpdLPYEEQNIIaPLLREANIALIPLVTVTSPIERIEKITS 165
Cdd:cd01536 48 IEDLIAQGVDAIII--APVDSEALV-PAVKKANAAGIPVVAVDTDIDGGGDVVA 98
|
|
| DRE_TIM_metallolyase |
cd03174 |
DRE-TIM metallolyase superfamily; The DRE-TIM metallolyase superfamily includes ... |
35-127 |
4.92e-03 |
|
DRE-TIM metallolyase superfamily; The DRE-TIM metallolyase superfamily includes 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM".
Pssm-ID: 163674 [Multi-domain] Cd Length: 265 Bit Score: 37.44 E-value: 4.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459984 35 IRFLDEAGASIVEIGipfsdpvadgptiqragkraldSGVTLKGIFQ------ALAEVRKEvqMPFVLMTylnpVLAFGK 108
Cdd:cd03174 25 AEALDEAGVDSIEVG----------------------SGASPKAVPQmeddweVLRAIRKL--VPNVKLQ----ALVRNR 76
|
90
....*....|....*....
gi 446459984 109 ERFIENCIEAGVDGIIVPD 127
Cdd:cd03174 77 EKGIERALEAGVDEVRIFD 95
|
|
| PBP1_ABC_sugar_binding-like |
cd06317 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
111-157 |
5.51e-03 |
|
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380540 [Multi-domain] Cd Length: 281 Bit Score: 37.36 E-value: 5.51e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 446459984 111 FIENCIEAGVDGIIVPDLpyeEQNIIAPLLREANIALIPLVTVTSPI 157
Cdd:cd06317 47 AVDNYIARGVDAIILDAI---DVNGSIPAIKRASEAGIPVIAYDAVI 90
|
|
| NanE |
cd04729 |
N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to ... |
175-233 |
8.35e-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: 36.40 E-value: 8.35e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459984 175 TVAGVTGVRQNFKEEIHSYLEKVKSHVNLPVVAGFGISTKEHVEEMVTI-CDGVVVGSKI 233
Cdd:cd04729 150 TLSGYTEETAKTEDPDFELLKELRKALGIPVIAEGRINSPEQAAKALELgADAVVVGSAI 209
|
|
| |
