|
Name |
Accession |
Description |
Interval |
E-value |
| trpA |
PRK13111 |
tryptophan synthase subunit alpha; Provisional |
4-254 |
3.70e-125 |
|
tryptophan synthase subunit alpha; Provisional
Pssm-ID: 237285 Cd Length: 258 Bit Score: 355.95 E-value: 3.70e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459970 4 EKIKAAFENGKKAFIPYVMGGDGGLEKLKERIRFLDEAGASIVEIGIPFSDPVADGPTIQRAGKRALDSGVTLKGIFQAL 83
Cdd:PRK13111 1 ALFAALKAEGRKALIPYITAGDPDLETSLEIIKALVEAGADIIELGIPFSDPVADGPVIQAASLRALAAGVTLADVFELV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459970 84 AEVR-KEVQIPFVLMTYLNPVLAFGKERFVEKCLEAGVDGIIVPDLPYEEQNIIAPLLREANIALIPLVTVTSPIERIEK 162
Cdd:PRK13111 81 REIReKDPTIPIVLMTYYNPIFQYGVERFAADAAEAGVDGLIIPDLPPEEAEELRAAAKKHGLDLIFLVAPTTTDERLKK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459970 163 ITSESEGFVYAVTVAGVTGVRQNFKEEIHSYLEKVKSHVNLPVVAGFGISTKEHIEEMVTICDGVVVGSKVIELLEN--E 240
Cdd:PRK13111 161 IASHASGFVYYVSRAGVTGARSADAADLAELVARLKAHTDLPVAVGFGISTPEQAAAIAAVADGVIVGSALVKIIEEnpE 240
|
250
....*....|....
gi 446459970 241 KREEICELIQATKQ 254
Cdd:PRK13111 241 ALEALAAFVKELKA 254
|
|
| TrpA |
COG0159 |
Tryptophan synthase alpha chain [Amino acid transport and metabolism]; Tryptophan synthase ... |
4-251 |
3.39e-123 |
|
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: 350.90 E-value: 3.39e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459970 4 EKIKAAFE----NGKKAFIPYVMGGDGGLEKLKERIRFLDEAGASIVEIGIPFSDPVADGPTIQRAGKRALDSGVTLKGI 79
Cdd:COG0159 1 SRIDAAFAalkaEGRKALIPYLTAGDPDLETTLEIIKALVEAGADIIELGIPFSDPVADGPVIQAASERALANGVTLDDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459970 80 FQALAEVRKEVQIPFVLMTYLNPVLAFGKERFVEKCLEAGVDGIIVPDLPYEEQNIIAPLLREANIALIPLVTVTSPIER 159
Cdd:COG0159 81 FELVREFREDPDTPLVLMGYYNPVFRYGVERFAADAAEAGVDGLIVPDLPPEEAEELRAAADAHGLDLIFLVAPTTSDER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459970 160 IEKITSESEGFVYAVTVAGVTGVRQNFKEEIHSYLEKVKSHVNLPVVAGFGISTKEHIEEMVTICDGVVVGSKVIELLEN 239
Cdd:COG0159 161 IKKIAAAASGFVYYVSVTGVTGARTAVSDDLAELVARIRAHTDLPVAVGFGISTPEQAAEVAAYADGVIVGSALVKLIEE 240
|
250
....*....|..
gi 446459970 240 EKREEICELIQA 251
Cdd:COG0159 241 GGDDEALEALAA 252
|
|
| Tryptophan_synthase_alpha |
cd04724 |
Ttryptophan synthase (TRPS) alpha subunit (TSA). TPRS is a bifunctional tetrameric enzyme (2 ... |
16-253 |
1.98e-116 |
|
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: 333.29 E-value: 1.98e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459970 16 AFIPYVMGGDGGLEKLKERIRFLDEAGASIVEIGIPFSDPVADGPTIQRAGKRALDSGVTLKGIFQALAEVRKEVQIPFV 95
Cdd:cd04724 1 ALIPYITAGDPDLETTLEILKALVEAGADIIELGIPFSDPVADGPVIQAASERALANGVTLKDVLELVKEIRKKNTIPIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459970 96 LMTYLNPVLAFGKERFVEKCLEAGVDGIIVPDLPYEEQNIIAPLLREANIALIPLVTVTSPIERIEKITSESEGFVYAVT 175
Cdd:cd04724 81 LMGYYNPILQYGLERFLRDAKEAGVDGLIIPDLPPEEAEEFREAAKEYGLDLIFLVAPTTPDERIKKIAELASGFIYYVS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459970 176 VAGVTGVRQNFKEEIHSYLEKVKSHVNLPVVAGFGISTKEHIEEMVTICDGVVVGSKVIELLEN----EKREEICELIQA 251
Cdd:cd04724 161 RTGVTGARTELPDDLKELIKRIRKYTDLPIAVGFGISTPEQAAEVAKYADGVIVGSALVKIIEEggeeEALEALKELAES 240
|
..
gi 446459970 252 TK 253
Cdd:cd04724 241 LK 242
|
|
| Trp_syntA |
pfam00290 |
Tryptophan synthase alpha chain; |
7-250 |
2.66e-99 |
|
Tryptophan synthase alpha chain;
Pssm-ID: 395227 Cd Length: 258 Bit Score: 290.37 E-value: 2.66e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459970 7 KAAFENGKKAFIPYVMGGDGGLEKLKERIRFLDEAGASIVEIGIPFSDPVADGPTIQRAGKRALDSGVTLKGIFQALAEV 86
Cdd:pfam00290 2 ANLKAENRAAFVPYVTAGDPDLEQSLEILKTLEKAGADAIELGVPFSDPLADGPTIQRANLRALASGVTLQSTLEMVREV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459970 87 R-KEVQIPFVLMTYLNPVLAFGKERFVEKCLEAGVDGIIVPDLPYEEQNIIAPLLREANIALIPLVTVTSPIERIEKITS 165
Cdd:pfam00290 82 RsKGVEVPIVLMTYYNPVLNYGIERFYALAAEAGVDGLIVPDLPPEEADSLRQAAKDHGLELVFLVAPTTSDERLKTVVE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459970 166 ESEGFVYAVTVAGVTGVRQNFKEEIHSYLEKVKSHVNLPVVAGFGISTKEHIEEMVTICDGVVVGSKVIELLENEKREEI 245
Cdd:pfam00290 162 QAEGFVYLVSRAGVTGAENAVNAQVDELVERLKKYTAVPVAVGFGISTPEHVKQAAAGADGVIVGSALVRIIEEAADGPE 241
|
....*
gi 446459970 246 CELIQ 250
Cdd:pfam00290 242 QGLAR 246
|
|
| trpA |
TIGR00262 |
tryptophan synthase, alpha subunit; Tryptophan synthase catalyzes the last step in the ... |
11-253 |
8.47e-83 |
|
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: 248.41 E-value: 8.47e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459970 11 ENGKKAFIPYVMGGDGGLEKLKERIRFLDEAGASIVEIGIPFSDPVADGPTIQRAGKRALDSGVTLKGIFQALAEVRKE- 89
Cdd:TIGR00262 6 QRGEGAFIPFVTAGDPTLETSLEIIKTLIEAGADALELGVPFSDPLADGPTIQAADLRALRAGMTPEKCFELLKKVRQKh 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459970 90 VQIPFVLMTYLNPVLAFGKERFVEKCLEAGVDGIIVPDLPYEEQNiiaPLLREA---NIALIPLVTVTSPIERIEKITSE 166
Cdd:TIGR00262 86 PNIPIGLLTYYNLIFRKGVEEFYAKCKEVGVDGVLVADLPLEESG---DLVEAAkkhGVKPIFLVAPNADDERLKQIAEK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459970 167 SEGFVYAVTVAGVTGVRQNFKEEIHSYLEKVKSHVNLPVVAGFGISTKEHIEEMVTI-CDGVVVGS---KVIE-LLENEK 241
Cdd:TIGR00262 163 SQGFVYLVSRAGVTGARNRAASALNELVKRLKAYSAKPVLVGFGISKPEQVKQAIDAgADGVIVGSaivKIIEeNLNTPE 242
|
250
....*....|....
gi 446459970 242 R--EEICELIQATK 253
Cdd:TIGR00262 243 KmlQALEEFVQNLK 256
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| trpA |
PRK13111 |
tryptophan synthase subunit alpha; Provisional |
4-254 |
3.70e-125 |
|
tryptophan synthase subunit alpha; Provisional
Pssm-ID: 237285 Cd Length: 258 Bit Score: 355.95 E-value: 3.70e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459970 4 EKIKAAFENGKKAFIPYVMGGDGGLEKLKERIRFLDEAGASIVEIGIPFSDPVADGPTIQRAGKRALDSGVTLKGIFQAL 83
Cdd:PRK13111 1 ALFAALKAEGRKALIPYITAGDPDLETSLEIIKALVEAGADIIELGIPFSDPVADGPVIQAASLRALAAGVTLADVFELV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459970 84 AEVR-KEVQIPFVLMTYLNPVLAFGKERFVEKCLEAGVDGIIVPDLPYEEQNIIAPLLREANIALIPLVTVTSPIERIEK 162
Cdd:PRK13111 81 REIReKDPTIPIVLMTYYNPIFQYGVERFAADAAEAGVDGLIIPDLPPEEAEELRAAAKKHGLDLIFLVAPTTTDERLKK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459970 163 ITSESEGFVYAVTVAGVTGVRQNFKEEIHSYLEKVKSHVNLPVVAGFGISTKEHIEEMVTICDGVVVGSKVIELLEN--E 240
Cdd:PRK13111 161 IASHASGFVYYVSRAGVTGARSADAADLAELVARLKAHTDLPVAVGFGISTPEQAAAIAAVADGVIVGSALVKIIEEnpE 240
|
250
....*....|....
gi 446459970 241 KREEICELIQATKQ 254
Cdd:PRK13111 241 ALEALAAFVKELKA 254
|
|
| TrpA |
COG0159 |
Tryptophan synthase alpha chain [Amino acid transport and metabolism]; Tryptophan synthase ... |
4-251 |
3.39e-123 |
|
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: 350.90 E-value: 3.39e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459970 4 EKIKAAFE----NGKKAFIPYVMGGDGGLEKLKERIRFLDEAGASIVEIGIPFSDPVADGPTIQRAGKRALDSGVTLKGI 79
Cdd:COG0159 1 SRIDAAFAalkaEGRKALIPYLTAGDPDLETTLEIIKALVEAGADIIELGIPFSDPVADGPVIQAASERALANGVTLDDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459970 80 FQALAEVRKEVQIPFVLMTYLNPVLAFGKERFVEKCLEAGVDGIIVPDLPYEEQNIIAPLLREANIALIPLVTVTSPIER 159
Cdd:COG0159 81 FELVREFREDPDTPLVLMGYYNPVFRYGVERFAADAAEAGVDGLIVPDLPPEEAEELRAAADAHGLDLIFLVAPTTSDER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459970 160 IEKITSESEGFVYAVTVAGVTGVRQNFKEEIHSYLEKVKSHVNLPVVAGFGISTKEHIEEMVTICDGVVVGSKVIELLEN 239
Cdd:COG0159 161 IKKIAAAASGFVYYVSVTGVTGARTAVSDDLAELVARIRAHTDLPVAVGFGISTPEQAAEVAAYADGVIVGSALVKLIEE 240
|
250
....*....|..
gi 446459970 240 EKREEICELIQA 251
Cdd:COG0159 241 GGDDEALEALAA 252
|
|
| Tryptophan_synthase_alpha |
cd04724 |
Ttryptophan synthase (TRPS) alpha subunit (TSA). TPRS is a bifunctional tetrameric enzyme (2 ... |
16-253 |
1.98e-116 |
|
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: 333.29 E-value: 1.98e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459970 16 AFIPYVMGGDGGLEKLKERIRFLDEAGASIVEIGIPFSDPVADGPTIQRAGKRALDSGVTLKGIFQALAEVRKEVQIPFV 95
Cdd:cd04724 1 ALIPYITAGDPDLETTLEILKALVEAGADIIELGIPFSDPVADGPVIQAASERALANGVTLKDVLELVKEIRKKNTIPIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459970 96 LMTYLNPVLAFGKERFVEKCLEAGVDGIIVPDLPYEEQNIIAPLLREANIALIPLVTVTSPIERIEKITSESEGFVYAVT 175
Cdd:cd04724 81 LMGYYNPILQYGLERFLRDAKEAGVDGLIIPDLPPEEAEEFREAAKEYGLDLIFLVAPTTPDERIKKIAELASGFIYYVS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459970 176 VAGVTGVRQNFKEEIHSYLEKVKSHVNLPVVAGFGISTKEHIEEMVTICDGVVVGSKVIELLEN----EKREEICELIQA 251
Cdd:cd04724 161 RTGVTGARTELPDDLKELIKRIRKYTDLPIAVGFGISTPEQAAEVAKYADGVIVGSALVKIIEEggeeEALEALKELAES 240
|
..
gi 446459970 252 TK 253
Cdd:cd04724 241 LK 242
|
|
| Trp_syntA |
pfam00290 |
Tryptophan synthase alpha chain; |
7-250 |
2.66e-99 |
|
Tryptophan synthase alpha chain;
Pssm-ID: 395227 Cd Length: 258 Bit Score: 290.37 E-value: 2.66e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459970 7 KAAFENGKKAFIPYVMGGDGGLEKLKERIRFLDEAGASIVEIGIPFSDPVADGPTIQRAGKRALDSGVTLKGIFQALAEV 86
Cdd:pfam00290 2 ANLKAENRAAFVPYVTAGDPDLEQSLEILKTLEKAGADAIELGVPFSDPLADGPTIQRANLRALASGVTLQSTLEMVREV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459970 87 R-KEVQIPFVLMTYLNPVLAFGKERFVEKCLEAGVDGIIVPDLPYEEQNIIAPLLREANIALIPLVTVTSPIERIEKITS 165
Cdd:pfam00290 82 RsKGVEVPIVLMTYYNPVLNYGIERFYALAAEAGVDGLIVPDLPPEEADSLRQAAKDHGLELVFLVAPTTSDERLKTVVE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459970 166 ESEGFVYAVTVAGVTGVRQNFKEEIHSYLEKVKSHVNLPVVAGFGISTKEHIEEMVTICDGVVVGSKVIELLENEKREEI 245
Cdd:pfam00290 162 QAEGFVYLVSRAGVTGAENAVNAQVDELVERLKKYTAVPVAVGFGISTPEHVKQAAAGADGVIVGSALVRIIEEAADGPE 241
|
....*
gi 446459970 246 CELIQ 250
Cdd:pfam00290 242 QGLAR 246
|
|
| trpA |
TIGR00262 |
tryptophan synthase, alpha subunit; Tryptophan synthase catalyzes the last step in the ... |
11-253 |
8.47e-83 |
|
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: 248.41 E-value: 8.47e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459970 11 ENGKKAFIPYVMGGDGGLEKLKERIRFLDEAGASIVEIGIPFSDPVADGPTIQRAGKRALDSGVTLKGIFQALAEVRKE- 89
Cdd:TIGR00262 6 QRGEGAFIPFVTAGDPTLETSLEIIKTLIEAGADALELGVPFSDPLADGPTIQAADLRALRAGMTPEKCFELLKKVRQKh 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459970 90 VQIPFVLMTYLNPVLAFGKERFVEKCLEAGVDGIIVPDLPYEEQNiiaPLLREA---NIALIPLVTVTSPIERIEKITSE 166
Cdd:TIGR00262 86 PNIPIGLLTYYNLIFRKGVEEFYAKCKEVGVDGVLVADLPLEESG---DLVEAAkkhGVKPIFLVAPNADDERLKQIAEK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459970 167 SEGFVYAVTVAGVTGVRQNFKEEIHSYLEKVKSHVNLPVVAGFGISTKEHIEEMVTI-CDGVVVGS---KVIE-LLENEK 241
Cdd:TIGR00262 163 SQGFVYLVSRAGVTGARNRAASALNELVKRLKAYSAKPVLVGFGISKPEQVKQAIDAgADGVIVGSaivKIIEeNLNTPE 242
|
250
....*....|....
gi 446459970 242 R--EEICELIQATK 253
Cdd:TIGR00262 243 KmlQALEEFVQNLK 256
|
|
| PLN02591 |
PLN02591 |
tryptophan synthase |
14-237 |
4.50e-74 |
|
tryptophan synthase
Pssm-ID: 178201 Cd Length: 250 Bit Score: 226.09 E-value: 4.50e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459970 14 KKAFIPYVMGGDGGLEKLKERIRFLDEAGASIVEIGIPFSDPVADGPTIQRAGKRALDSGVTLKGIFQALAEVRKEVQIP 93
Cdd:PLN02591 1 KVAFIPYITAGDPDLDTTAEALRLLDACGADVIELGVPYSDPLADGPVIQAAATRALEKGTTLDSVISMLKEVAPQLSCP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459970 94 FVLMTYLNPVLAFGKERFVEKCLEAGVDGIIVPDLPYEEQNIIAPLLREANIALIPLVTVTSPIERIEKITSESEGFVYA 173
Cdd:PLN02591 81 IVLFTYYNPILKRGIDKFMATIKEAGVHGLVVPDLPLEETEALRAEAAKNGIELVLLTTPTTPTERMKAIAEASEGFVYL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446459970 174 VTVAGVTGVRQNFKEEIHSYLEKVKSHVNLPVVAGFGISTKEHIEEMVTI-CDGVVVGSKVIELL 237
Cdd:PLN02591 161 VSSTGVTGARASVSGRVESLLQELKEVTDKPVAVGFGISKPEHAKQIAGWgADGVIVGSAMVKAL 225
|
|
| trpA |
CHL00200 |
tryptophan synthase alpha subunit; Provisional |
6-253 |
7.45e-71 |
|
tryptophan synthase alpha subunit; Provisional
Pssm-ID: 214394 Cd Length: 263 Bit Score: 218.10 E-value: 7.45e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459970 6 IKAAFENGKK--AFIPYVMGGDGGLEKLKERIRFLDEAGASIVEIGIPFSDPVADGPTIQRAGKRALDSGVTLKGIFQAL 83
Cdd:CHL00200 4 ISNVFEKLDKqcALIPFITAGDPDIVITKKALKILDKKGADIIELGIPYSDPLADGPIIQEASNRALKQGINLNKILSIL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459970 84 AEVRKEVQIPFVLMTYLNPVLAFGKERFVEKCLEAGVDGIIVPDLPYEEQNIIAPLLREANIALIPLVTVTSPIERIEKI 163
Cdd:CHL00200 84 SEVNGEIKAPIVIFTYYNPVLHYGINKFIKKISQAGVKGLIIPDLPYEESDYLISVCNLYNIELILLIAPTSSKSRIQKI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459970 164 TSESEGFVYAVTVAGVTGVRQNFKEEIHSYLEKVKSHVNLPVVAGFGISTKEHIEEMVTI-CDGVVVGSKVIELLENEKR 242
Cdd:CHL00200 164 ARAAPGCIYLVSTTGVTGLKTELDKKLKKLIETIKKMTNKPIILGFGISTSEQIKQIKGWnINGIVIGSACVQILLGSSP 243
|
250
....*....|....*
gi 446459970 243 EE----ICELIQATK 253
Cdd:CHL00200 244 EKgldqLSEFCKVAK 258
|
|
| trpA |
PRK13125 |
tryptophan synthase subunit alpha; Provisional |
14-254 |
1.21e-21 |
|
tryptophan synthase subunit alpha; Provisional
Pssm-ID: 237286 Cd Length: 244 Bit Score: 90.10 E-value: 1.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459970 14 KKAFIPYVMGGDGGLEKLKERIRFLDEAgASIVEIGIPFSDPVADGPTIQRAGKraldsGVTLKGIFQALAEVRKEVQIP 93
Cdd:PRK13125 3 RPGLVVYLTAGYPNVESFKEFIIGLVEL-VDILELGIPPKYPKYDGPVIRKSHR-----KVKGLDIWPLLEEVRKDVSVP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459970 94 FVLMTYLNPVLAfGKERFVEKCLEAGVDGIIVPDLPY---EEQNIIAPLLREANIALIPLVTVTSPIERIEKITSESEGF 170
Cdd:PRK13125 77 IILMTYLEDYVD-SLDNFLNMARDVGADGVLFPDLLIdypDDLEKYVEIIKNKGLKPVFFTSPKFPDLLIHRLSKLSPLF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459970 171 VYaVTVAGVTGVrqnfkeEIHSYLEKVKSHV-----NLPVVAGFGISTKEHIEEMVTI-CDGVVVGSKVIELLENEKREE 244
Cdd:PRK13125 156 IY-YGLRPATGV------PLPVSVERNIKRVrnlvgNKYLVVGFGLDSPEDARDALSAgADGVVVGTAFIEELEKNGVES 228
|
250
....*....|
gi 446459970 245 ICELIQATKQ 254
Cdd:PRK13125 229 ALNLLKKIRG 238
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
17-231 |
1.69e-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: 1.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459970 17 FIPYVMGGdGGLEKLKERIRFLDEAGASIVEIGIPFSDPVADGPTIQRAgkraldsgvtlkgifqaLAEVRKEVQIPFVL 96
Cdd:cd04722 1 VILALLAG-GPSGDPVELAKAAAEAGADAIIVGTRSSDPEEAETDDKEV-----------------LKEVAAETDLPLGV 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459970 97 MTYLNPVLAFGKERfVEKCLEAGVDGIIVPDLPYEEQNIIAPLLREANIAL--IPLVTVTSPIERIEKITSESEG--FVY 172
Cdd:cd04722 63 QLAINDAAAAVDIA-AAAARAAGADGVEIHGAVGYLAREDLELIRELREAVpdVKVVVKLSPTGELAAAAAEEAGvdEVG 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459970 173 AVTVAGVTGvRQNFKEEIHSYLEKVKSHVNLPVVAGFGISTKEHIEEMV-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 |
5.95e-04 |
|
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: 40.16 E-value: 5.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459970 75 TLKGIFQALAEVRKEVQIPF-VLMTYLNPVLAFgkERFVEKCLEAGVDGIIV---PDLPYEEQniiaplLREANIALIPl 150
Cdd:cd04730 37 TPEALRAEIRKIRALTDKPFgVNLLVPSSNPDF--EALLEVALEEGVPVVSFsfgPPAEVVER------LKAAGIKVIP- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459970 151 vTVTSPIErieKITSESEGfVYAVTVAGVT--GVRQNFKEEIHSYLEKVKSHVNLPVVAGFGISTKEHIEEMVTI-CDGV 227
Cdd:cd04730 108 -TVTSVEE---ARKAEAAG-ADALVAQGAEagGHRGTFDIGTFALVPEVRDAVDIPVIAAGGIADGRGIAAALALgADGV 182
|
....
gi 446459970 228 VVGS 231
Cdd:cd04730 183 QMGT 186
|
|
| BtpA |
COG0434 |
Membrane biogenesis protein, BtpA/SgcQ family [Cell wall/membrane/envelope biogenesis]; |
194-231 |
1.46e-03 |
|
Membrane biogenesis protein, BtpA/SgcQ family [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440203 Cd Length: 268 Bit Score: 39.00 E-value: 1.46e-03
10 20 30
....*....|....*....|....*....|....*....
gi 446459970 194 LEKVKSHV-NLPVVAGFGIsTKEHIEEMVTICDGVVVGS 231
Cdd:COG0434 203 LKRVKEAApDVPVLVGSGV-TPENVAELLSVADGAIVGS 240
|
|
| DRE_TIM_metallolyase |
cd03174 |
DRE-TIM metallolyase superfamily; The DRE-TIM metallolyase superfamily includes ... |
35-127 |
6.18e-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: 37.05 E-value: 6.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459970 35 IRFLDEAGASIVEIGipfsdpvadgptiqragkraldSGVTLKGIFQ------ALAEVRKEVQ-IPFVlmtylnpVLAFG 107
Cdd:cd03174 25 AEALDEAGVDSIEVG----------------------SGASPKAVPQmeddweVLRAIRKLVPnVKLQ-------ALVRN 75
|
90 100
....*....|....*....|
gi 446459970 108 KERFVEKCLEAGVDGIIVPD 127
Cdd:cd03174 76 REKGIERALEAGVDEVRIFD 95
|
|
| |
