|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02591 |
PLN02591 |
tryptophan synthase |
75-324 |
3.96e-168 |
|
tryptophan synthase
Pssm-ID: 178201 Cd Length: 250 Bit Score: 467.22 E-value: 3.96e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002257578 75 KTAFIPYITAGDPDMGTTAEALRLLDACGADVIELGVPFSDPYNDGPVIQASAARALSAGATMDGIMSMLAEVTPELSCP 154
Cdd:PLN02591 1 KVAFIPYITAGDPDLDTTAEALRLLDACGADVIELGVPYSDPLADGPVIQAAATRALEKGTTLDSVISMLKEVAPQLSCP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002257578 155 VVLFSYLGPIVRRGPANFTAAAKEAGVQGLIVPDLPYLEACSFRSEVIKNNLELVLLTTPTTPPDRMKAITAASGGFVYL 234
Cdd:PLN02591 81 IVLFTYYNPILKRGIDKFMATIKEAGVHGLVVPDLPLEETEALRAEAAKNGIELVLLTTPTTPTERMKAIAEASEGFVYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002257578 235 VSVNGVTGSRQDVNPRVEHLLQEIKQVTDKAVCVGYGISTPDHVRQIAEWGADGVIIGSAMVRQLGEAASPKQGLKRLEK 314
Cdd:PLN02591 161 VSSTGVTGARASVSGRVESLLQELKEVTDKPVAVGFGISKPEHAKQIAGWGADGVIVGSAMVKALGEAKSPEEGLKRLEK 240
|
250
....*....|
gi 1002257578 315 YARSLKNALP 324
Cdd:PLN02591 241 LAKSLKAALP 250
|
|
| TrpA |
COG0159 |
Tryptophan synthase alpha chain [Amino acid transport and metabolism]; Tryptophan synthase ... |
61-323 |
9.17e-115 |
|
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: 332.41 E-value: 9.17e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002257578 61 SSVSRTMSRLMEKGKTAFIPYITAGDPDMGTTAEALRLLDACGADVIELGVPFSDPYNDGPVIQASAARALSAGATMDGI 140
Cdd:COG0159 1 SRIDAAFAALKAEGRKALIPYLTAGDPDLETTLEIIKALVEAGADIIELGIPFSDPVADGPVIQAASERALANGVTLDDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002257578 141 MSMLAEVTPELSCPVVLFSYLGPIVRRGPANFTAAAKEAGVQGLIVPDLPYLEACSFRSEVIKNNLELVLLTTPTTPPDR 220
Cdd:COG0159 81 FELVREFREDPDTPLVLMGYYNPVFRYGVERFAADAAEAGVDGLIVPDLPPEEAEELRAAADAHGLDLIFLVAPTTSDER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002257578 221 MKAITAASGGFVYLVSVNGVTGSRQDVNPRVEHLLQEIKQVTDKAVCVGYGISTPDHVRQIAEWgADGVIIGSAMVRQLg 300
Cdd:COG0159 161 IKKIAAAASGFVYYVSVTGVTGARTAVSDDLAELVARIRAHTDLPVAVGFGISTPEQAAEVAAY-ADGVIVGSALVKLI- 238
|
250 260
....*....|....*....|...
gi 1002257578 301 EAASPKQGLKRLEKYARSLKNAL 323
Cdd:COG0159 239 EEGGDDEALEALAAFVRELKAAL 261
|
|
| Trp_syntA |
pfam00290 |
Tryptophan synthase alpha chain; |
67-323 |
2.21e-111 |
|
Tryptophan synthase alpha chain;
Pssm-ID: 395227 Cd Length: 258 Bit Score: 323.88 E-value: 2.21e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002257578 67 MSRLMEKGKTAFIPYITAGDPDMGTTAEALRLLDACGADVIELGVPFSDPYNDGPVIQASAARALSAGATMDGIMSMLAE 146
Cdd:pfam00290 1 FANLKAENRAAFVPYVTAGDPDLEQSLEILKTLEKAGADAIELGVPFSDPLADGPTIQRANLRALASGVTLQSTLEMVRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002257578 147 VT-PELSCPVVLFSYLGPIVRRGPANFTAAAKEAGVQGLIVPDLPYLEACSFRSEVIKNNLELVLLTTPTTPPDRMKAIT 225
Cdd:pfam00290 81 VRsKGVEVPIVLMTYYNPVLNYGIERFYALAAEAGVDGLIVPDLPPEEADSLRQAAKDHGLELVFLVAPTTSDERLKTVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002257578 226 AASGGFVYLVSVNGVTGSRQDVNPRVEHLLQEIKQVTDKAVCVGYGISTPDHVRQIAeWGADGVIIGSAMVRQLGEAA-S 304
Cdd:pfam00290 161 EQAEGFVYLVSRAGVTGAENAVNAQVDELVERLKKYTAVPVAVGFGISTPEHVKQAA-AGADGVIVGSALVRIIEEAAdG 239
|
250
....*....|....*....
gi 1002257578 305 PKQGLKRLEKYARSLKNAL 323
Cdd:pfam00290 240 PEQGLARLEELAGEMKAAA 258
|
|
| Tryptophan_synthase_alpha |
cd04724 |
Ttryptophan synthase (TRPS) alpha subunit (TSA). TPRS is a bifunctional tetrameric enzyme (2 ... |
77-320 |
4.47e-110 |
|
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: 319.81 E-value: 4.47e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002257578 77 AFIPYITAGDPDMGTTAEALRLLDACGADVIELGVPFSDPYNDGPVIQASAARALSAGATMDGIMSMLAEVTPELSCPVV 156
Cdd:cd04724 1 ALIPYITAGDPDLETTLEILKALVEAGADIIELGIPFSDPVADGPVIQAASERALANGVTLKDVLELVKEIRKKNTIPIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002257578 157 LFSYLGPIVRRGPANFTAAAKEAGVQGLIVPDLPYLEACSFRSEVIKNNLELVLLTTPTTPPDRMKAITAASGGFVYLVS 236
Cdd:cd04724 81 LMGYYNPILQYGLERFLRDAKEAGVDGLIIPDLPPEEAEEFREAAKEYGLDLIFLVAPTTPDERIKKIAELASGFIYYVS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002257578 237 VNGVTGSRQDVNPRVEHLLQEIKQVTDKAVCVGYGISTPDHVRQIAEWgADGVIIGSAMVRQLGEAAsPKQGLKRLEKYA 316
Cdd:cd04724 161 RTGVTGARTELPDDLKELIKRIRKYTDLPIAVGFGISTPEQAAEVAKY-ADGVIVGSALVKIIEEGG-EEEALEALKELA 238
|
....
gi 1002257578 317 RSLK 320
Cdd:cd04724 239 ESLK 242
|
|
| trpA |
TIGR00262 |
tryptophan synthase, alpha subunit; Tryptophan synthase catalyzes the last step in the ... |
70-320 |
1.30e-94 |
|
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: 281.16 E-value: 1.30e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002257578 70 LMEKGKTAFIPYITAGDPDMGTTAEALRLLDACGADVIELGVPFSDPYNDGPVIQASAARALSAGATMDGIMSMLAEVTP 149
Cdd:TIGR00262 4 LKQRGEGAFIPFVTAGDPTLETSLEIIKTLIEAGADALELGVPFSDPLADGPTIQAADLRALRAGMTPEKCFELLKKVRQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002257578 150 EL-SCPVVLFSYLGPIVRRGPANFTAAAKEAGVQGLIVPDLPYLEACSFRSEVIKNNLELVLLTTPTTPPDRMKAITAAS 228
Cdd:TIGR00262 84 KHpNIPIGLLTYYNLIFRKGVEEFYAKCKEVGVDGVLVADLPLEESGDLVEAAKKHGVKPIFLVAPNADDERLKQIAEKS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002257578 229 GGFVYLVSVNGVTGSRQDVNPRVEHLLQEIKQVTDKAVCVGYGISTPDHVRQIAEWGADGVIIGSAMVRQLGE-AASPKQ 307
Cdd:TIGR00262 164 QGFVYLVSRAGVTGARNRAASALNELVKRLKAYSAKPVLVGFGISKPEQVKQAIDAGADGVIVGSAIVKIIEEnLNTPEK 243
|
250
....*....|...
gi 1002257578 308 GLKRLEKYARSLK 320
Cdd:TIGR00262 244 MLQALEEFVQNLK 256
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02591 |
PLN02591 |
tryptophan synthase |
75-324 |
3.96e-168 |
|
tryptophan synthase
Pssm-ID: 178201 Cd Length: 250 Bit Score: 467.22 E-value: 3.96e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002257578 75 KTAFIPYITAGDPDMGTTAEALRLLDACGADVIELGVPFSDPYNDGPVIQASAARALSAGATMDGIMSMLAEVTPELSCP 154
Cdd:PLN02591 1 KVAFIPYITAGDPDLDTTAEALRLLDACGADVIELGVPYSDPLADGPVIQAAATRALEKGTTLDSVISMLKEVAPQLSCP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002257578 155 VVLFSYLGPIVRRGPANFTAAAKEAGVQGLIVPDLPYLEACSFRSEVIKNNLELVLLTTPTTPPDRMKAITAASGGFVYL 234
Cdd:PLN02591 81 IVLFTYYNPILKRGIDKFMATIKEAGVHGLVVPDLPLEETEALRAEAAKNGIELVLLTTPTTPTERMKAIAEASEGFVYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002257578 235 VSVNGVTGSRQDVNPRVEHLLQEIKQVTDKAVCVGYGISTPDHVRQIAEWGADGVIIGSAMVRQLGEAASPKQGLKRLEK 314
Cdd:PLN02591 161 VSSTGVTGARASVSGRVESLLQELKEVTDKPVAVGFGISKPEHAKQIAGWGADGVIVGSAMVKALGEAKSPEEGLKRLEK 240
|
250
....*....|
gi 1002257578 315 YARSLKNALP 324
Cdd:PLN02591 241 LAKSLKAALP 250
|
|
| TrpA |
COG0159 |
Tryptophan synthase alpha chain [Amino acid transport and metabolism]; Tryptophan synthase ... |
61-323 |
9.17e-115 |
|
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: 332.41 E-value: 9.17e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002257578 61 SSVSRTMSRLMEKGKTAFIPYITAGDPDMGTTAEALRLLDACGADVIELGVPFSDPYNDGPVIQASAARALSAGATMDGI 140
Cdd:COG0159 1 SRIDAAFAALKAEGRKALIPYLTAGDPDLETTLEIIKALVEAGADIIELGIPFSDPVADGPVIQAASERALANGVTLDDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002257578 141 MSMLAEVTPELSCPVVLFSYLGPIVRRGPANFTAAAKEAGVQGLIVPDLPYLEACSFRSEVIKNNLELVLLTTPTTPPDR 220
Cdd:COG0159 81 FELVREFREDPDTPLVLMGYYNPVFRYGVERFAADAAEAGVDGLIVPDLPPEEAEELRAAADAHGLDLIFLVAPTTSDER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002257578 221 MKAITAASGGFVYLVSVNGVTGSRQDVNPRVEHLLQEIKQVTDKAVCVGYGISTPDHVRQIAEWgADGVIIGSAMVRQLg 300
Cdd:COG0159 161 IKKIAAAASGFVYYVSVTGVTGARTAVSDDLAELVARIRAHTDLPVAVGFGISTPEQAAEVAAY-ADGVIVGSALVKLI- 238
|
250 260
....*....|....*....|...
gi 1002257578 301 EAASPKQGLKRLEKYARSLKNAL 323
Cdd:COG0159 239 EEGGDDEALEALAAFVRELKAAL 261
|
|
| trpA |
PRK13111 |
tryptophan synthase subunit alpha; Provisional |
65-323 |
9.99e-114 |
|
tryptophan synthase subunit alpha; Provisional
Pssm-ID: 237285 Cd Length: 258 Bit Score: 329.76 E-value: 9.99e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002257578 65 RTMSRLMEKGKTAFIPYITAGDPDMGTTAEALRLLDACGADVIELGVPFSDPYNDGPVIQASAARALSAGATMDGIMSML 144
Cdd:PRK13111 1 ALFAALKAEGRKALIPYITAGDPDLETSLEIIKALVEAGADIIELGIPFSDPVADGPVIQAASLRALAAGVTLADVFELV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002257578 145 AEV-TPELSCPVVLFSYLGPIVRRGPANFTAAAKEAGVQGLIVPDLPYLEACSFRSEVIKNNLELVLLTTPTTPPDRMKA 223
Cdd:PRK13111 81 REIrEKDPTIPIVLMTYYNPIFQYGVERFAADAAEAGVDGLIIPDLPPEEAEELRAAAKKHGLDLIFLVAPTTTDERLKK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002257578 224 ITAASGGFVYLVSVNGVTGSRQDVNPRVEHLLQEIKQVTDKAVCVGYGISTPDHVRQIAEwGADGVIIGSAMVRQLGEAa 303
Cdd:PRK13111 161 IASHASGFVYYVSRAGVTGARSADAADLAELVARLKAHTDLPVAVGFGISTPEQAAAIAA-VADGVIVGSALVKIIEEN- 238
|
250 260
....*....|....*....|
gi 1002257578 304 spKQGLKRLEKYARSLKNAL 323
Cdd:PRK13111 239 --PEALEALAAFVKELKAAL 256
|
|
| Trp_syntA |
pfam00290 |
Tryptophan synthase alpha chain; |
67-323 |
2.21e-111 |
|
Tryptophan synthase alpha chain;
Pssm-ID: 395227 Cd Length: 258 Bit Score: 323.88 E-value: 2.21e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002257578 67 MSRLMEKGKTAFIPYITAGDPDMGTTAEALRLLDACGADVIELGVPFSDPYNDGPVIQASAARALSAGATMDGIMSMLAE 146
Cdd:pfam00290 1 FANLKAENRAAFVPYVTAGDPDLEQSLEILKTLEKAGADAIELGVPFSDPLADGPTIQRANLRALASGVTLQSTLEMVRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002257578 147 VT-PELSCPVVLFSYLGPIVRRGPANFTAAAKEAGVQGLIVPDLPYLEACSFRSEVIKNNLELVLLTTPTTPPDRMKAIT 225
Cdd:pfam00290 81 VRsKGVEVPIVLMTYYNPVLNYGIERFYALAAEAGVDGLIVPDLPPEEADSLRQAAKDHGLELVFLVAPTTSDERLKTVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002257578 226 AASGGFVYLVSVNGVTGSRQDVNPRVEHLLQEIKQVTDKAVCVGYGISTPDHVRQIAeWGADGVIIGSAMVRQLGEAA-S 304
Cdd:pfam00290 161 EQAEGFVYLVSRAGVTGAENAVNAQVDELVERLKKYTAVPVAVGFGISTPEHVKQAA-AGADGVIVGSALVRIIEEAAdG 239
|
250
....*....|....*....
gi 1002257578 305 PKQGLKRLEKYARSLKNAL 323
Cdd:pfam00290 240 PEQGLARLEELAGEMKAAA 258
|
|
| Tryptophan_synthase_alpha |
cd04724 |
Ttryptophan synthase (TRPS) alpha subunit (TSA). TPRS is a bifunctional tetrameric enzyme (2 ... |
77-320 |
4.47e-110 |
|
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: 319.81 E-value: 4.47e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002257578 77 AFIPYITAGDPDMGTTAEALRLLDACGADVIELGVPFSDPYNDGPVIQASAARALSAGATMDGIMSMLAEVTPELSCPVV 156
Cdd:cd04724 1 ALIPYITAGDPDLETTLEILKALVEAGADIIELGIPFSDPVADGPVIQAASERALANGVTLKDVLELVKEIRKKNTIPIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002257578 157 LFSYLGPIVRRGPANFTAAAKEAGVQGLIVPDLPYLEACSFRSEVIKNNLELVLLTTPTTPPDRMKAITAASGGFVYLVS 236
Cdd:cd04724 81 LMGYYNPILQYGLERFLRDAKEAGVDGLIIPDLPPEEAEEFREAAKEYGLDLIFLVAPTTPDERIKKIAELASGFIYYVS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002257578 237 VNGVTGSRQDVNPRVEHLLQEIKQVTDKAVCVGYGISTPDHVRQIAEWgADGVIIGSAMVRQLGEAAsPKQGLKRLEKYA 316
Cdd:cd04724 161 RTGVTGARTELPDDLKELIKRIRKYTDLPIAVGFGISTPEQAAEVAKY-ADGVIVGSALVKIIEEGG-EEEALEALKELA 238
|
....
gi 1002257578 317 RSLK 320
Cdd:cd04724 239 ESLK 242
|
|
| trpA |
TIGR00262 |
tryptophan synthase, alpha subunit; Tryptophan synthase catalyzes the last step in the ... |
70-320 |
1.30e-94 |
|
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: 281.16 E-value: 1.30e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002257578 70 LMEKGKTAFIPYITAGDPDMGTTAEALRLLDACGADVIELGVPFSDPYNDGPVIQASAARALSAGATMDGIMSMLAEVTP 149
Cdd:TIGR00262 4 LKQRGEGAFIPFVTAGDPTLETSLEIIKTLIEAGADALELGVPFSDPLADGPTIQAADLRALRAGMTPEKCFELLKKVRQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002257578 150 EL-SCPVVLFSYLGPIVRRGPANFTAAAKEAGVQGLIVPDLPYLEACSFRSEVIKNNLELVLLTTPTTPPDRMKAITAAS 228
Cdd:TIGR00262 84 KHpNIPIGLLTYYNLIFRKGVEEFYAKCKEVGVDGVLVADLPLEESGDLVEAAKKHGVKPIFLVAPNADDERLKQIAEKS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002257578 229 GGFVYLVSVNGVTGSRQDVNPRVEHLLQEIKQVTDKAVCVGYGISTPDHVRQIAEWGADGVIIGSAMVRQLGE-AASPKQ 307
Cdd:TIGR00262 164 QGFVYLVSRAGVTGARNRAASALNELVKRLKAYSAKPVLVGFGISKPEQVKQAIDAGADGVIVGSAIVKIIEEnLNTPEK 243
|
250
....*....|...
gi 1002257578 308 GLKRLEKYARSLK 320
Cdd:TIGR00262 244 MLQALEEFVQNLK 256
|
|
| trpA |
CHL00200 |
tryptophan synthase alpha subunit; Provisional |
66-323 |
3.57e-84 |
|
tryptophan synthase alpha subunit; Provisional
Pssm-ID: 214394 Cd Length: 263 Bit Score: 254.69 E-value: 3.57e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002257578 66 TMSRLMEKG--KTAFIPYITAGDPDMGTTAEALRLLDACGADVIELGVPFSDPYNDGPVIQASAARALSAGATMDGIMSM 143
Cdd:CHL00200 3 TISNVFEKLdkQCALIPFITAGDPDIVITKKALKILDKKGADIIELGIPYSDPLADGPIIQEASNRALKQGINLNKILSI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002257578 144 LAEVTPELSCPVVLFSYLGPIVRRGPANFTAAAKEAGVQGLIVPDLPYLEACSFRSEVIKNNLELVLLTTPTTPPDRMKA 223
Cdd:CHL00200 83 LSEVNGEIKAPIVIFTYYNPVLHYGINKFIKKISQAGVKGLIIPDLPYEESDYLISVCNLYNIELILLIAPTSSKSRIQK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002257578 224 ITAASGGFVYLVSVNGVTGSRQDVNPRVEHLLQEIKQVTDKAVCVGYGISTPDHVRQIAEWGADGVIIGSAMVRQLgEAA 303
Cdd:CHL00200 163 IARAAPGCIYLVSTTGVTGLKTELDKKLKKLIETIKKMTNKPIILGFGISTSEQIKQIKGWNINGIVIGSACVQIL-LGS 241
|
250 260
....*....|....*....|
gi 1002257578 304 SPKQGLKRLEKYARSLKNAL 323
Cdd:CHL00200 242 SPEKGLDQLSEFCKVAKKSI 261
|
|
| trpA |
PRK13125 |
tryptophan synthase subunit alpha; Provisional |
75-324 |
1.85e-28 |
|
tryptophan synthase subunit alpha; Provisional
Pssm-ID: 237286 Cd Length: 244 Bit Score: 110.13 E-value: 1.85e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002257578 75 KTAFIPYITAGDPDMGTTAEALRLLDACgADVIELGVPFSDPYNDGPVIqasaaRALSAGATMDGIMSMLAEVTPELSCP 154
Cdd:PRK13125 3 RPGLVVYLTAGYPNVESFKEFIIGLVEL-VDILELGIPPKYPKYDGPVI-----RKSHRKVKGLDIWPLLEEVRKDVSVP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002257578 155 VVLFSYLGPIVRRgPANFTAAAKEAGVQGLIVPDLP--YLEACSFRSEVIKNN-LELVLLTTPTTPPDRMKAITAASGGF 231
Cdd:PRK13125 77 IILMTYLEDYVDS-LDNFLNMARDVGADGVLFPDLLidYPDDLEKYVEIIKNKgLKPVFFTSPKFPDLLIHRLSKLSPLF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002257578 232 VYLvSVNGVTGSRQDVNprVEHLLQEIKQ-VTDKAVCVGYGISTPDHVRQIAEWGADGVIIGSAMVRQLgeaasPKQGLK 310
Cdd:PRK13125 156 IYY-GLRPATGVPLPVS--VERNIKRVRNlVGNKYLVVGFGLDSPEDARDALSAGADGVVVGTAFIEEL-----EKNGVE 227
|
250
....*....|....
gi 1002257578 311 RLEKYARSLKNALP 324
Cdd:PRK13125 228 SALNLLKKIRGALD 241
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
78-293 |
2.33e-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: 2.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002257578 78 FIPYITAGDPDmGTTAEALRLLDACGADVIELGVPFSDPYNDGPVIQASAARALSAGATMDGIMSMLAEVTPELSCPVvl 157
Cdd:cd04722 1 VILALLAGGPS-GDPVELAKAAAEAGADAIIVGTRSSDPEEAETDDKEVLKEVAAETDLPLGVQLAINDAAAAVDIAA-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002257578 158 fsylgpivrrgpanftAAAKEAGVQGLIVPDLPYLEACSFRS--EVIK---NNLELVLLTTPTTPPDRMKAITAAsGGFV 232
Cdd:cd04722 78 ----------------AAARAAGADGVEIHGAVGYLAREDLEliRELReavPDVKVVVKLSPTGELAAAAAEEAG-VDEV 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002257578 233 YLVSVNGVTGSRqDVNPRVEHLLQEIKQVTDKAVCVGYGISTPDHVRQIAEWGADGVIIGS 293
Cdd:cd04722 141 GLGNGGGGGGGR-DAVPIADLLLILAKRGSKVPVIAGGGINDPEDAAEALALGADGVIVGS 200
|
|
| HisA_HisF |
cd04723 |
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase (HisA) ... |
254-295 |
1.79e-05 |
|
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: 45.34 E-value: 1.79e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1002257578 254 LLQEIKQVTDKAVCVGYGISTPDHVRQIAEWGADGVIIGSAM 295
Cdd:cd04723 180 LLERLAARADIPVIAAGGVRSVEDLELLKKLGASGALVASAL 221
|
|
| His_biosynth |
pfam00977 |
Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine ... |
249-298 |
1.52e-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: 42.47 E-value: 1.52e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1002257578 249 PRVEHLLQEIKQVTDKAVCVGYGISTPDHVRQIAEWGADGVIIGSAMVRQ 298
Cdd:pfam00977 59 PVNLDVVEEIAEEVFIPVQVGGGIRSLEDVERLLSAGADRVIIGTAAVKN 108
|
|
| IGPS |
cd00331 |
Indole-3-glycerol phosphate synthase (IGPS); an enzyme in the tryptophan biosynthetic pathway, ... |
271-312 |
1.72e-04 |
|
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: 42.07 E-value: 1.72e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1002257578 271 GISTPDHVRQIAEWGADGVIIGSAMVRqlgeAASPKQGLKRL 312
Cdd:cd00331 180 GISTPEDVKRLAEAGADAVLIGESLMR----APDPGAALREL 217
|
|
| trpC |
PRK00278 |
indole-3-glycerol phosphate synthase TrpC; |
271-312 |
2.36e-04 |
|
indole-3-glycerol phosphate synthase TrpC;
Pssm-ID: 234710 Cd Length: 260 Bit Score: 42.07 E-value: 2.36e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1002257578 271 GISTPDHVRQIAEWGADGVIIGSAMVRQlgeaASPKQGLKRL 312
Cdd:PRK00278 219 GIFTPEDLKRLAKAGADAVLVGESLMRA----DDPGAALREL 256
|
|
| HisA |
COG0106 |
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase [Amino ... |
254-294 |
7.29e-04 |
|
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: 40.41 E-value: 7.29e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1002257578 254 LLQEIKQVTDKAVCVGYGISTPDHVRQIAEWGADGVIIGSA 294
Cdd:COG0106 180 LYRELAAATGIPVIASGGVSSLDDLRALKELGVEGAIVGKA 220
|
|
| HisA |
cd04732 |
HisA. Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase ... |
254-294 |
2.33e-03 |
|
HisA. Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase catalyzes the fourth step in histidine biosynthesis, an isomerisation of the aminoaldose moiety of ProFAR to the aminoketose of PRFAR (N-(5'-phospho-D-1'-ribulosylformimino)-5-amino-1-(5''-phospho-ribosyl)-4-imidazolecarboxamide). In bacteria and archaea, ProFAR isomerase is encoded by the HisA gene.
Pssm-ID: 240083 Cd Length: 234 Bit Score: 38.62 E-value: 2.33e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1002257578 254 LLQEIKQVTDKAVCVGYGISTPDHVRQIAEWGADGVIIGSA 294
Cdd:cd04732 181 LYKELAAATGIPVIASGGVSSLDDIKALKELGVAGVIVGKA 221
|
|
| TMP_TenI |
cd00564 |
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step ... |
241-312 |
4.92e-03 |
|
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step in the thiamine biosynthesis pathway, the substitution of the pyrophosphate of 2-methyl-4-amino-5- hydroxymethylpyrimidine pyrophosphate by 4-methyl-5- (beta-hydroxyethyl) thiazole phosphate to yield thiamine phosphate. TenI is a enzymatically inactive regulatory protein involved in the regulation of several extracellular enzymes. This superfamily also contains other enzymatically inactive proteins with unknown functions.
Pssm-ID: 238317 [Multi-domain] Cd Length: 196 Bit Score: 37.50 E-value: 4.92e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002257578 241 TGSRQDVNPRVE-HLLQEIKQVTDKAVcVGYGISTPDHVRQIAEWGADGViigsAMVRQLGEAASPKQGLKRL 312
Cdd:cd00564 127 TPTKPGAGPPLGlELLREIAELVEIPV-VAIGGITPENAAEVLAAGADGV----AVISAITGADDPAAAAREL 194
|
|
| IGPS |
pfam00218 |
Indole-3-glycerol phosphate synthase; |
271-298 |
5.02e-03 |
|
Indole-3-glycerol phosphate synthase;
Pssm-ID: 395163 Cd Length: 252 Bit Score: 38.05 E-value: 5.02e-03
10 20
....*....|....*....|....*...
gi 1002257578 271 GISTPDHVRQIAEWGADGVIIGSAMVRQ 298
Cdd:pfam00218 216 GIYTPADVRELKEHGANAFLVGESLMRQ 243
|
|
| His_biosynth |
pfam00977 |
Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine ... |
254-295 |
5.19e-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: 5.19e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1002257578 254 LLQEIKQVTDKAVCVGYGISTPDHVRQIAEWGADGVIIGSAM 295
Cdd:pfam00977 181 LTRELAEAVNIPVIASGGVGSLEDLKELFTEGVDGVIAGSAL 222
|
|
| NanE |
cd04729 |
N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to ... |
223-297 |
5.60e-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: 37.55 E-value: 5.60e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002257578 223 AITAASGGFVYLVS-VNGVTGSRQDVNPRVEHLLQEIKQVTDKAVCVGYGISTPDHVRQIAEWGADGVIIGSAMVR 297
Cdd:cd04729 136 ALNAAKLGFDIIGTtLSGYTEETAKTEDPDFELLKELRKALGIPVIAEGRINSPEQAAKALELGADAVVVGSAITR 211
|
|
| PRK07695 |
PRK07695 |
thiazole tautomerase TenI; |
241-320 |
6.56e-03 |
|
thiazole tautomerase TenI;
Pssm-ID: 181086 [Multi-domain] Cd Length: 201 Bit Score: 37.31 E-value: 6.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002257578 241 TGSRQDVNPRVEHLLQEIKQ-VTDKAVCVGyGIsTPDHVRQIAEWGADGVIIGSAMVrqlgEAASPKQGLKRlekYARSL 319
Cdd:PRK07695 127 TDCKKGVPARGLEELSDIARaLSIPVIAIG-GI-TPENTRDVLAAGVSGIAVMSGIF----SSANPYSKAKR---YAESI 197
|
.
gi 1002257578 320 K 320
Cdd:PRK07695 198 K 198
|
|
| |
