|
Name |
Accession |
Description |
Interval |
E-value |
| trpA |
PRK13111 |
tryptophan synthase subunit alpha; Provisional |
7-252 |
1.04e-102 |
|
tryptophan synthase subunit alpha; Provisional
Pssm-ID: 237285 Cd Length: 258 Bit Score: 298.95 E-value: 1.04e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518148865 7 KHLQAIKAEGKGLFIPYIMAGDHDkgLDGLFDTISFLEAQGVSAIEIGIPWSDPVADGPVIELAGQRSLVKGTSLVSI-- 84
Cdd:PRK13111 1 ALFAALKAEGRKALIPYITAGDPD--LETSLEIIKALVEAGADIIELGIPFSDPVADGPVIQAASLRALAAGVTLADVfe 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518148865 85 -IARLQEKKTQVPLVIMTYFNPVFQYGVETFVADLQNTSVKGLIIPDLPHEQESFIKPYLENLDLALVPLVSLTTGLERQ 163
Cdd:PRK13111 79 lVREIREKDPTIPIVLMTYYNPIFQYGVERFAADAAEAGVDGLIIPDLPPEEAEELRAAAKKHGLDLIFLVAPTTTDERL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518148865 164 KELIEGAQGFVYAVAINGVTGKTGNYRDDLDKHLKHLTEIAQIPVLTGFGVSTLADIKRFNQVSDGVIVGSKIVKGLHE- 242
Cdd:PRK13111 159 KKIASHASGFVYYVSRAGVTGARSADAADLAELVARLKAHTDLPVAVGFGISTPEQAAAIAAVADGVIVGSALVKIIEEn 238
|
250
....*....|.
gi 518148865 243 -GMQEEIKDFI 252
Cdd:PRK13111 239 pEALEALAAFV 249
|
|
| TrpA |
COG0159 |
Tryptophan synthase alpha chain [Amino acid transport and metabolism]; Tryptophan synthase ... |
5-252 |
2.05e-97 |
|
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: 285.81 E-value: 2.05e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518148865 5 LTKHLQAIKAEGKGLFIPYIMAGDHDkgLDGLFDTISFLEAQGVSAIEIGIPWSDPVADGPVIELAGQRSLVKGTSLVSI 84
Cdd:COG0159 3 IDAAFAALKAEGRKALIPYLTAGDPD--LETTLEIIKALVEAGADIIELGIPFSDPVADGPVIQAASERALANGVTLDDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518148865 85 IARLQE--KKTQVPLVIMTYFNPVFQYGVETFVADLQNTSVKGLIIPDLPHEQESFIKPYLENLDLALVPLVSLTTGLER 162
Cdd:COG0159 81 FELVREfrEDPDTPLVLMGYYNPVFRYGVERFAADAAEAGVDGLIVPDLPPEEAEELRAAADAHGLDLIFLVAPTTSDER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518148865 163 QKELIEGAQGFVYAVAINGVTGKTGNYRDDLDKHLKHLTEIAQIPVLTGFGVSTLADIKRFNQVSDGVIVGSKIVKGLHE 242
Cdd:COG0159 161 IKKIAAAASGFVYYVSVTGVTGARTAVSDDLAELVARIRAHTDLPVAVGFGISTPEQAAEVAAYADGVIVGSALVKLIEE 240
|
250
....*....|....
gi 518148865 243 G----MQEEIKDFI 252
Cdd:COG0159 241 GgddeALEALAAFV 254
|
|
| Trp_syntA |
pfam00290 |
Tryptophan synthase alpha chain; |
9-250 |
3.09e-93 |
|
Tryptophan synthase alpha chain;
Pssm-ID: 395227 Cd Length: 258 Bit Score: 274.96 E-value: 3.09e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518148865 9 LQAIKAEGKGLFIPYIMAGDHDkgLDGLFDTISFLEAQGVSAIEIGIPWSDPVADGPVIELAGQRSLVKGTSLVSI---I 85
Cdd:pfam00290 1 FANLKAENRAAFVPYVTAGDPD--LEQSLEILKTLEKAGADAIELGVPFSDPLADGPTIQRANLRALASGVTLQSTlemV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518148865 86 ARLQEKKTQVPLVIMTYFNPVFQYGVETFVADLQNTSVKGLIIPDLPHEQESFIKPYLENLDLALVPLVSLTTGLERQKE 165
Cdd:pfam00290 79 REVRSKGVEVPIVLMTYYNPVLNYGIERFYALAAEAGVDGLIVPDLPPEEADSLRQAAKDHGLELVFLVAPTTSDERLKT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518148865 166 LIEGAQGFVYAVAINGVTGKTGNYRDDLDKHLKHLTEIAQIPVLTGFGVSTLADIKRFNQVSDGVIVGSKIVKGLHEGMQ 245
Cdd:pfam00290 159 VVEQAEGFVYLVSRAGVTGAENAVNAQVDELVERLKKYTAVPVAVGFGISTPEHVKQAAAGADGVIVGSALVRIIEEAAD 238
|
....*
gi 518148865 246 EEIKD 250
Cdd:pfam00290 239 GPEQG 243
|
|
| Tryptophan_synthase_alpha |
cd04724 |
Ttryptophan synthase (TRPS) alpha subunit (TSA). TPRS is a bifunctional tetrameric enzyme (2 ... |
19-252 |
1.95e-87 |
|
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: 259.72 E-value: 1.95e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518148865 19 LFIPYIMAGDHDkgLDGLFDTISFLEAQGVSAIEIGIPWSDPVADGPVIELAGQRSLVKGTSLVSIIARLQE--KKTQVP 96
Cdd:cd04724 1 ALIPYITAGDPD--LETTLEILKALVEAGADIIELGIPFSDPVADGPVIQAASERALANGVTLKDVLELVKEirKKNTIP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518148865 97 LVIMTYFNPVFQYGVETFVADLQNTSVKGLIIPDLPHEQESFIKPYLENLDLALVPLVSLTTGLERQKELIEGAQGFVYA 176
Cdd:cd04724 79 IVLMGYYNPILQYGLERFLRDAKEAGVDGLIIPDLPPEEAEEFREAAKEYGLDLIFLVAPTTPDERIKKIAELASGFIYY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518148865 177 VAINGVTGKTGNYRDDLDKHLKHLTEIAQIPVLTGFGVSTLADIKRFNQVSDGVIVGSKIVK----GLHEGMQEEIKDFI 252
Cdd:cd04724 159 VSRTGVTGARTELPDDLKELIKRIRKYTDLPIAVGFGISTPEQAAEVAKYADGVIVGSALVKiieeGGEEEALEALKELA 238
|
|
| trpA |
TIGR00262 |
tryptophan synthase, alpha subunit; Tryptophan synthase catalyzes the last step in the ... |
11-252 |
2.75e-60 |
|
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: 191.02 E-value: 2.75e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518148865 11 AIKAEGKGLFIPYIMAGDHDkgLDGLFDTISFLEAQGVSAIEIGIPWSDPVADGPVIELAGQRSLVKGTSLV---SIIAR 87
Cdd:TIGR00262 3 TLKQRGEGAFIPFVTAGDPT--LETSLEIIKTLIEAGADALELGVPFSDPLADGPTIQAADLRALRAGMTPEkcfELLKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518148865 88 LQEKKTQVPLVIMTYFNPVFQYGVETFVADLQNTSVKGLIIPDLPHEQESFIKPYLENLDLALVPLVSLTTGLERQKELI 167
Cdd:TIGR00262 81 VRQKHPNIPIGLLTYYNLIFRKGVEEFYAKCKEVGVDGVLVADLPLEESGDLVEAAKKHGVKPIFLVAPNADDERLKQIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518148865 168 EGAQGFVYAVAINGVTGKTGNYRDDLDKHLKHLTEIAQIPVLTGFGVSTLADIKRFNQV-SDGVIVGSKIVK------GL 240
Cdd:TIGR00262 161 EKSQGFVYLVSRAGVTGARNRAASALNELVKRLKAYSAKPVLVGFGISKPEQVKQAIDAgADGVIVGSAIVKiieenlNT 240
|
250
....*....|..
gi 518148865 241 HEGMQEEIKDFI 252
Cdd:TIGR00262 241 PEKMLQALEEFV 252
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| trpA |
PRK13111 |
tryptophan synthase subunit alpha; Provisional |
7-252 |
1.04e-102 |
|
tryptophan synthase subunit alpha; Provisional
Pssm-ID: 237285 Cd Length: 258 Bit Score: 298.95 E-value: 1.04e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518148865 7 KHLQAIKAEGKGLFIPYIMAGDHDkgLDGLFDTISFLEAQGVSAIEIGIPWSDPVADGPVIELAGQRSLVKGTSLVSI-- 84
Cdd:PRK13111 1 ALFAALKAEGRKALIPYITAGDPD--LETSLEIIKALVEAGADIIELGIPFSDPVADGPVIQAASLRALAAGVTLADVfe 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518148865 85 -IARLQEKKTQVPLVIMTYFNPVFQYGVETFVADLQNTSVKGLIIPDLPHEQESFIKPYLENLDLALVPLVSLTTGLERQ 163
Cdd:PRK13111 79 lVREIREKDPTIPIVLMTYYNPIFQYGVERFAADAAEAGVDGLIIPDLPPEEAEELRAAAKKHGLDLIFLVAPTTTDERL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518148865 164 KELIEGAQGFVYAVAINGVTGKTGNYRDDLDKHLKHLTEIAQIPVLTGFGVSTLADIKRFNQVSDGVIVGSKIVKGLHE- 242
Cdd:PRK13111 159 KKIASHASGFVYYVSRAGVTGARSADAADLAELVARLKAHTDLPVAVGFGISTPEQAAAIAAVADGVIVGSALVKIIEEn 238
|
250
....*....|.
gi 518148865 243 -GMQEEIKDFI 252
Cdd:PRK13111 239 pEALEALAAFV 249
|
|
| TrpA |
COG0159 |
Tryptophan synthase alpha chain [Amino acid transport and metabolism]; Tryptophan synthase ... |
5-252 |
2.05e-97 |
|
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: 285.81 E-value: 2.05e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518148865 5 LTKHLQAIKAEGKGLFIPYIMAGDHDkgLDGLFDTISFLEAQGVSAIEIGIPWSDPVADGPVIELAGQRSLVKGTSLVSI 84
Cdd:COG0159 3 IDAAFAALKAEGRKALIPYLTAGDPD--LETTLEIIKALVEAGADIIELGIPFSDPVADGPVIQAASERALANGVTLDDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518148865 85 IARLQE--KKTQVPLVIMTYFNPVFQYGVETFVADLQNTSVKGLIIPDLPHEQESFIKPYLENLDLALVPLVSLTTGLER 162
Cdd:COG0159 81 FELVREfrEDPDTPLVLMGYYNPVFRYGVERFAADAAEAGVDGLIVPDLPPEEAEELRAAADAHGLDLIFLVAPTTSDER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518148865 163 QKELIEGAQGFVYAVAINGVTGKTGNYRDDLDKHLKHLTEIAQIPVLTGFGVSTLADIKRFNQVSDGVIVGSKIVKGLHE 242
Cdd:COG0159 161 IKKIAAAASGFVYYVSVTGVTGARTAVSDDLAELVARIRAHTDLPVAVGFGISTPEQAAEVAAYADGVIVGSALVKLIEE 240
|
250
....*....|....
gi 518148865 243 G----MQEEIKDFI 252
Cdd:COG0159 241 GgddeALEALAAFV 254
|
|
| Trp_syntA |
pfam00290 |
Tryptophan synthase alpha chain; |
9-250 |
3.09e-93 |
|
Tryptophan synthase alpha chain;
Pssm-ID: 395227 Cd Length: 258 Bit Score: 274.96 E-value: 3.09e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518148865 9 LQAIKAEGKGLFIPYIMAGDHDkgLDGLFDTISFLEAQGVSAIEIGIPWSDPVADGPVIELAGQRSLVKGTSLVSI---I 85
Cdd:pfam00290 1 FANLKAENRAAFVPYVTAGDPD--LEQSLEILKTLEKAGADAIELGVPFSDPLADGPTIQRANLRALASGVTLQSTlemV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518148865 86 ARLQEKKTQVPLVIMTYFNPVFQYGVETFVADLQNTSVKGLIIPDLPHEQESFIKPYLENLDLALVPLVSLTTGLERQKE 165
Cdd:pfam00290 79 REVRSKGVEVPIVLMTYYNPVLNYGIERFYALAAEAGVDGLIVPDLPPEEADSLRQAAKDHGLELVFLVAPTTSDERLKT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518148865 166 LIEGAQGFVYAVAINGVTGKTGNYRDDLDKHLKHLTEIAQIPVLTGFGVSTLADIKRFNQVSDGVIVGSKIVKGLHEGMQ 245
Cdd:pfam00290 159 VVEQAEGFVYLVSRAGVTGAENAVNAQVDELVERLKKYTAVPVAVGFGISTPEHVKQAAAGADGVIVGSALVRIIEEAAD 238
|
....*
gi 518148865 246 EEIKD 250
Cdd:pfam00290 239 GPEQG 243
|
|
| Tryptophan_synthase_alpha |
cd04724 |
Ttryptophan synthase (TRPS) alpha subunit (TSA). TPRS is a bifunctional tetrameric enzyme (2 ... |
19-252 |
1.95e-87 |
|
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: 259.72 E-value: 1.95e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518148865 19 LFIPYIMAGDHDkgLDGLFDTISFLEAQGVSAIEIGIPWSDPVADGPVIELAGQRSLVKGTSLVSIIARLQE--KKTQVP 96
Cdd:cd04724 1 ALIPYITAGDPD--LETTLEILKALVEAGADIIELGIPFSDPVADGPVIQAASERALANGVTLKDVLELVKEirKKNTIP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518148865 97 LVIMTYFNPVFQYGVETFVADLQNTSVKGLIIPDLPHEQESFIKPYLENLDLALVPLVSLTTGLERQKELIEGAQGFVYA 176
Cdd:cd04724 79 IVLMGYYNPILQYGLERFLRDAKEAGVDGLIIPDLPPEEAEEFREAAKEYGLDLIFLVAPTTPDERIKKIAELASGFIYY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518148865 177 VAINGVTGKTGNYRDDLDKHLKHLTEIAQIPVLTGFGVSTLADIKRFNQVSDGVIVGSKIVK----GLHEGMQEEIKDFI 252
Cdd:cd04724 159 VSRTGVTGARTELPDDLKELIKRIRKYTDLPIAVGFGISTPEQAAEVAKYADGVIVGSALVKiieeGGEEEALEALKELA 238
|
|
| trpA |
TIGR00262 |
tryptophan synthase, alpha subunit; Tryptophan synthase catalyzes the last step in the ... |
11-252 |
2.75e-60 |
|
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: 191.02 E-value: 2.75e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518148865 11 AIKAEGKGLFIPYIMAGDHDkgLDGLFDTISFLEAQGVSAIEIGIPWSDPVADGPVIELAGQRSLVKGTSLV---SIIAR 87
Cdd:TIGR00262 3 TLKQRGEGAFIPFVTAGDPT--LETSLEIIKTLIEAGADALELGVPFSDPLADGPTIQAADLRALRAGMTPEkcfELLKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518148865 88 LQEKKTQVPLVIMTYFNPVFQYGVETFVADLQNTSVKGLIIPDLPHEQESFIKPYLENLDLALVPLVSLTTGLERQKELI 167
Cdd:TIGR00262 81 VRQKHPNIPIGLLTYYNLIFRKGVEEFYAKCKEVGVDGVLVADLPLEESGDLVEAAKKHGVKPIFLVAPNADDERLKQIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518148865 168 EGAQGFVYAVAINGVTGKTGNYRDDLDKHLKHLTEIAQIPVLTGFGVSTLADIKRFNQV-SDGVIVGSKIVK------GL 240
Cdd:TIGR00262 161 EKSQGFVYLVSRAGVTGARNRAASALNELVKRLKAYSAKPVLVGFGISKPEQVKQAIDAgADGVIVGSAIVKiieenlNT 240
|
250
....*....|..
gi 518148865 241 HEGMQEEIKDFI 252
Cdd:TIGR00262 241 PEKMLQALEEFV 252
|
|
| PLN02591 |
PLN02591 |
tryptophan synthase |
20-242 |
3.82e-60 |
|
tryptophan synthase
Pssm-ID: 178201 Cd Length: 250 Bit Score: 190.65 E-value: 3.82e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518148865 20 FIPYIMAGDHDkgLDGLFDTISFLEAQGVSAIEIGIPWSDPVADGPVIELAGQRSLVKGTSLVSIIARLQEKKTQV--PL 97
Cdd:PLN02591 4 FIPYITAGDPD--LDTTAEALRLLDACGADVIELGVPYSDPLADGPVIQAAATRALEKGTTLDSVISMLKEVAPQLscPI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518148865 98 VIMTYFNPVFQYGVETFVADLQNTSVKGLIIPDLPHEQESFIKPYLENLDLALVPLVSLTTGLERQKELIEGAQGFVYAV 177
Cdd:PLN02591 82 VLFTYYNPILKRGIDKFMATIKEAGVHGLVVPDLPLEETEALRAEAAKNGIELVLLTTPTTPTERMKAIAEASEGFVYLV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518148865 178 AINGVTGKTGNYRDDLDKHLKHLTEIAQIPVLTGFGVSTLADIKrfnQV----SDGVIVGSKIVKGLHE 242
Cdd:PLN02591 162 SSTGVTGARASVSGRVESLLQELKEVTDKPVAVGFGISKPEHAK---QIagwgADGVIVGSAMVKALGE 227
|
|
| trpA |
CHL00200 |
tryptophan synthase alpha subunit; Provisional |
19-252 |
5.54e-55 |
|
tryptophan synthase alpha subunit; Provisional
Pssm-ID: 214394 Cd Length: 263 Bit Score: 177.65 E-value: 5.54e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518148865 19 LFIPYIMAGDHDkgLDGLFDTISFLEAQGVSAIEIGIPWSDPVADGPVIELAGQRSLVKGTSLVSIIARLQE--KKTQVP 96
Cdd:CHL00200 16 ALIPFITAGDPD--IVITKKALKILDKKGADIIELGIPYSDPLADGPIIQEASNRALKQGINLNKILSILSEvnGEIKAP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518148865 97 LVIMTYFNPVFQYGVETFVADLQNTSVKGLIIPDLPHEQESFIKPYLENLDLALVPLVSLTTGLERQKELIEGAQGFVYA 176
Cdd:CHL00200 94 IVIFTYYNPVLHYGINKFIKKISQAGVKGLIIPDLPYEESDYLISVCNLYNIELILLIAPTSSKSRIQKIARAAPGCIYL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518148865 177 VAINGVTGKTGNyrddLDKHLKHLTE----IAQIPVLTGFGVSTLADIKRF-NQVSDGVIVGSKIVKGL----HEGMQEE 247
Cdd:CHL00200 174 VSTTGVTGLKTE----LDKKLKKLIEtikkMTNKPIILGFGISTSEQIKQIkGWNINGIVIGSACVQILlgssPEKGLDQ 249
|
....*
gi 518148865 248 IKDFI 252
Cdd:CHL00200 250 LSEFC 254
|
|
| trpA |
PRK13125 |
tryptophan synthase subunit alpha; Provisional |
16-252 |
1.85e-08 |
|
tryptophan synthase subunit alpha; Provisional
Pssm-ID: 237286 Cd Length: 244 Bit Score: 53.51 E-value: 1.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518148865 16 GKGLFIpYIMAG-----DHDKGLDGLFDTISFLEaqgvsaieIGIPWSDPVADGPVIELAGQRslVKGTSLVSIIARLQe 90
Cdd:PRK13125 3 RPGLVV-YLTAGypnveSFKEFIIGLVELVDILE--------LGIPPKYPKYDGPVIRKSHRK--VKGLDIWPLLEEVR- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518148865 91 KKTQVPLVIMTYFnpvfqygvETFVADLQNT-------SVKGLIIPDL----PHEQESFIKpYLENLDLALVPLVS---- 155
Cdd:PRK13125 71 KDVSVPIILMTYL--------EDYVDSLDNFlnmardvGADGVLFPDLlidyPDDLEKYVE-IIKNKGLKPVFFTSpkfp 141
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170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518148865 156 --LTTGLERQKELiegaqgFVYAvainGVTGKTG----NYRDDLDKHLKHLTEiaQIPVLTGFGVSTLADIKRFNQV-SD 228
Cdd:PRK13125 142 dlLIHRLSKLSPL------FIYY----GLRPATGvplpVSVERNIKRVRNLVG--NKYLVVGFGLDSPEDARDALSAgAD 209
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250 260
....*....|....*....|....
gi 518148865 229 GVIVGSKIVKGLHEGMQEEIKDFI 252
Cdd:PRK13125 210 GVVVGTAFIEELEKNGVESALNLL 233
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|
| BtpA |
pfam03437 |
BtpA family; The BtpA protein is tightly associated with the thylakoid membranes, where it ... |
182-239 |
3.07e-04 |
|
BtpA family; The BtpA protein is tightly associated with the thylakoid membranes, where it stabilizes the reaction centre proteins of photosystem I.
Pssm-ID: 281436 Cd Length: 254 Bit Score: 41.30 E-value: 3.07e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 518148865 182 VTGKTGNYRDDLDKhLKHLTEIAQIPVLTGFGVStLADIKRFNQVSDGVIVGSKIVKG 239
Cdd:pfam03437 178 LSGKTTGGEPDLEE-LKLAKETVKTPVLAGSGVN-LENLEELLSIADGFIIGTSIKKD 233
|
|
| HisA_HisF |
cd04723 |
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase (HisA) ... |
192-243 |
5.05e-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: 40.33 E-value: 5.05e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 518148865 192 DLDKhLKHLTEIAQIPVLTGFGVSTLADIKRFNQVS-DGVIVGSkivkGLHEG 243
Cdd:cd04723 177 DLEL-LERLAARADIPVIAAGGVRSVEDLELLKKLGaSGALVAS----ALHDG 224
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