|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02591 |
PLN02591 |
tryptophan synthase |
35-284 |
1.46e-150 |
|
tryptophan synthase
Pssm-ID: 178201 Cd Length: 250 Bit Score: 422.15 E-value: 1.46e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303285204 35 QCAFIPFICAGDPNLDATERAIAILDDEGADVIELGVPYSDPLADGPTIAQAATRALNAGTTLDKTLALLARVSPTTKAP 114
Cdd:PLN02591 1 KVAFIPYITAGDPDLDTTAEALRLLDACGADVIELGVPYSDPLADGPVIQAAATRALEKGTTLDSVISMLKEVAPQLSCP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303285204 115 IVLFTYFNPIYQRGFEAFVEAVAAAGAKGLLVPDIPLEETPELSAICAKNGVDLVLLSTPTTPEARMTKIAEASNGFIYL 194
Cdd:PLN02591 81 IVLFTYYNPILKRGIDKFMATIKEAGVHGLVVPDLPLEETEALRAEAAKNGIELVLLTTPTTPTERMKAIAEASEGFVYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303285204 195 VSVTGVTGVRTNVESRVQELVSGLKKVTDKPVAVGFGISKKEQAAQVVGWGADGVIVGSALVRALGEAPTPEEGLERLTA 274
Cdd:PLN02591 161 VSSTGVTGARASVSGRVESLLQELKEVTDKPVAVGFGISKPEHAKQIAGWGADGVIVGSAMVKALGEAKSPEEGLKRLEK 240
|
250
....*....|
gi 303285204 275 LAKELREGSN 284
Cdd:PLN02591 241 LAKSLKAALP 250
|
|
| TrpA |
COG0159 |
Tryptophan synthase alpha chain [Amino acid transport and metabolism]; Tryptophan synthase ... |
23-282 |
1.92e-122 |
|
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: 351.29 E-value: 1.92e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303285204 23 IGATFAALKKRGQCAFIPFICAGDPNLDATERAIAILDDEGADVIELGVPYSDPLADGPTIAQAATRALNAGTTLDKTLA 102
Cdd:COG0159 3 IDAAFAALKAEGRKALIPYLTAGDPDLETTLEIIKALVEAGADIIELGIPFSDPVADGPVIQAASERALANGVTLDDVFE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303285204 103 LLARVSPTTKAPIVLFTYFNPIYQRGFEAFVEAVAAAGAKGLLVPDIPLEETPELSAICAKNGVDLVLLSTPTTPEARMT 182
Cdd:COG0159 83 LVREFREDPDTPLVLMGYYNPVFRYGVERFAADAAEAGVDGLIVPDLPPEEAEELRAAADAHGLDLIFLVAPTTSDERIK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303285204 183 KIAEASNGFIYLVSVTGVTGVRTNVESRVQELVSGLKKVTDKPVAVGFGISKKEQAAQVVGWgADGVIVGSALVRALGEA 262
Cdd:COG0159 163 KIAAAASGFVYYVSVTGVTGARTAVSDDLAELVARIRAHTDLPVAVGFGISTPEQAAEVAAY-ADGVIVGSALVKLIEEG 241
|
250 260
....*....|....*....|
gi 303285204 263 PtPEEGLERLTALAKELREG 282
Cdd:COG0159 242 G-DDEALEALAAFVRELKAA 260
|
|
| Tryptophan_synthase_alpha |
cd04724 |
Ttryptophan synthase (TRPS) alpha subunit (TSA). TPRS is a bifunctional tetrameric enzyme (2 ... |
37-280 |
1.25e-112 |
|
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: 325.59 E-value: 1.25e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303285204 37 AFIPFICAGDPNLDATERAIAILDDEGADVIELGVPYSDPLADGPTIAQAATRALNAGTTLDKTLALLARVSPTTKAPIV 116
Cdd:cd04724 1 ALIPYITAGDPDLETTLEILKALVEAGADIIELGIPFSDPVADGPVIQAASERALANGVTLKDVLELVKEIRKKNTIPIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303285204 117 LFTYFNPIYQRGFEAFVEAVAAAGAKGLLVPDIPLEETPELSAICAKNGVDLVLLSTPTTPEARMTKIAEASNGFIYLVS 196
Cdd:cd04724 81 LMGYYNPILQYGLERFLRDAKEAGVDGLIIPDLPPEEAEEFREAAKEYGLDLIFLVAPTTPDERIKKIAELASGFIYYVS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303285204 197 VTGVTGVRTNVESRVQELVSGLKKVTDKPVAVGFGISKKEQAAQVVGWgADGVIVGSALVRALGEAPtPEEGLERLTALA 276
Cdd:cd04724 161 RTGVTGARTELPDDLKELIKRIRKYTDLPIAVGFGISTPEQAAEVAKY-ADGVIVGSALVKIIEEGG-EEEALEALKELA 238
|
....
gi 303285204 277 KELR 280
Cdd:cd04724 239 ESLK 242
|
|
| trpA |
TIGR00262 |
tryptophan synthase, alpha subunit; Tryptophan synthase catalyzes the last step in the ... |
27-280 |
8.99e-104 |
|
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: 303.50 E-value: 8.99e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303285204 27 FAALKKRGQCAFIPFICAGDPNLDATERAIAILDDEGADVIELGVPYSDPLADGPTIAQAATRALNAGTTLDKTLALLAR 106
Cdd:TIGR00262 1 FETLKQRGEGAFIPFVTAGDPTLETSLEIIKTLIEAGADALELGVPFSDPLADGPTIQAADLRALRAGMTPEKCFELLKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303285204 107 VSP-TTKAPIVLFTYFNPIYQRGFEAFVEAVAAAGAKGLLVPDIPLEETPELSAICAKNGVDLVLLSTPTTPEARMTKIA 185
Cdd:TIGR00262 81 VRQkHPNIPIGLLTYYNLIFRKGVEEFYAKCKEVGVDGVLVADLPLEESGDLVEAAKKHGVKPIFLVAPNADDERLKQIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303285204 186 EASNGFIYLVSVTGVTGVRTNVESRVQELVSGLKKVTDKPVAVGFGISKKEQAAQVVGWGADGVIVGSALVRALGE-APT 264
Cdd:TIGR00262 161 EKSQGFVYLVSRAGVTGARNRAASALNELVKRLKAYSAKPVLVGFGISKPEQVKQAIDAGADGVIVGSAIVKIIEEnLNT 240
|
250
....*....|....*.
gi 303285204 265 PEEGLERLTALAKELR 280
Cdd:TIGR00262 241 PEKMLQALEEFVQNLK 256
|
|
| Trp_syntA |
pfam00290 |
Tryptophan synthase alpha chain; |
27-283 |
1.48e-102 |
|
Tryptophan synthase alpha chain;
Pssm-ID: 395227 Cd Length: 258 Bit Score: 300.77 E-value: 1.48e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303285204 27 FAALKKRGQCAFIPFICAGDPNLDATERAIAILDDEGADVIELGVPYSDPLADGPTIAQAATRALNAGTTLDKTLALLAR 106
Cdd:pfam00290 1 FANLKAENRAAFVPYVTAGDPDLEQSLEILKTLEKAGADAIELGVPFSDPLADGPTIQRANLRALASGVTLQSTLEMVRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303285204 107 V-SPTTKAPIVLFTYFNPIYQRGFEAFVEAVAAAGAKGLLVPDIPLEETPELSAICAKNGVDLVLLSTPTTPEARMTKIA 185
Cdd:pfam00290 81 VrSKGVEVPIVLMTYYNPVLNYGIERFYALAAEAGVDGLIVPDLPPEEADSLRQAAKDHGLELVFLVAPTTSDERLKTVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303285204 186 EASNGFIYLVSVTGVTGVRTNVESRVQELVSGLKKVTDKPVAVGFGISKKEQAAQvVGWGADGVIVGSALVRALGEAP-T 264
Cdd:pfam00290 161 EQAEGFVYLVSRAGVTGAENAVNAQVDELVERLKKYTAVPVAVGFGISTPEHVKQ-AAAGADGVIVGSALVRIIEEAAdG 239
|
250
....*....|....*....
gi 303285204 265 PEEGLERLTALAKELREGS 283
Cdd:pfam00290 240 PEQGLARLEELAGEMKAAA 258
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02591 |
PLN02591 |
tryptophan synthase |
35-284 |
1.46e-150 |
|
tryptophan synthase
Pssm-ID: 178201 Cd Length: 250 Bit Score: 422.15 E-value: 1.46e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303285204 35 QCAFIPFICAGDPNLDATERAIAILDDEGADVIELGVPYSDPLADGPTIAQAATRALNAGTTLDKTLALLARVSPTTKAP 114
Cdd:PLN02591 1 KVAFIPYITAGDPDLDTTAEALRLLDACGADVIELGVPYSDPLADGPVIQAAATRALEKGTTLDSVISMLKEVAPQLSCP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303285204 115 IVLFTYFNPIYQRGFEAFVEAVAAAGAKGLLVPDIPLEETPELSAICAKNGVDLVLLSTPTTPEARMTKIAEASNGFIYL 194
Cdd:PLN02591 81 IVLFTYYNPILKRGIDKFMATIKEAGVHGLVVPDLPLEETEALRAEAAKNGIELVLLTTPTTPTERMKAIAEASEGFVYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303285204 195 VSVTGVTGVRTNVESRVQELVSGLKKVTDKPVAVGFGISKKEQAAQVVGWGADGVIVGSALVRALGEAPTPEEGLERLTA 274
Cdd:PLN02591 161 VSSTGVTGARASVSGRVESLLQELKEVTDKPVAVGFGISKPEHAKQIAGWGADGVIVGSAMVKALGEAKSPEEGLKRLEK 240
|
250
....*....|
gi 303285204 275 LAKELREGSN 284
Cdd:PLN02591 241 LAKSLKAALP 250
|
|
| TrpA |
COG0159 |
Tryptophan synthase alpha chain [Amino acid transport and metabolism]; Tryptophan synthase ... |
23-282 |
1.92e-122 |
|
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: 351.29 E-value: 1.92e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303285204 23 IGATFAALKKRGQCAFIPFICAGDPNLDATERAIAILDDEGADVIELGVPYSDPLADGPTIAQAATRALNAGTTLDKTLA 102
Cdd:COG0159 3 IDAAFAALKAEGRKALIPYLTAGDPDLETTLEIIKALVEAGADIIELGIPFSDPVADGPVIQAASERALANGVTLDDVFE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303285204 103 LLARVSPTTKAPIVLFTYFNPIYQRGFEAFVEAVAAAGAKGLLVPDIPLEETPELSAICAKNGVDLVLLSTPTTPEARMT 182
Cdd:COG0159 83 LVREFREDPDTPLVLMGYYNPVFRYGVERFAADAAEAGVDGLIVPDLPPEEAEELRAAADAHGLDLIFLVAPTTSDERIK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303285204 183 KIAEASNGFIYLVSVTGVTGVRTNVESRVQELVSGLKKVTDKPVAVGFGISKKEQAAQVVGWgADGVIVGSALVRALGEA 262
Cdd:COG0159 163 KIAAAASGFVYYVSVTGVTGARTAVSDDLAELVARIRAHTDLPVAVGFGISTPEQAAEVAAY-ADGVIVGSALVKLIEEG 241
|
250 260
....*....|....*....|
gi 303285204 263 PtPEEGLERLTALAKELREG 282
Cdd:COG0159 242 G-DDEALEALAAFVRELKAA 260
|
|
| trpA |
PRK13111 |
tryptophan synthase subunit alpha; Provisional |
25-282 |
1.00e-120 |
|
tryptophan synthase subunit alpha; Provisional
Pssm-ID: 237285 Cd Length: 258 Bit Score: 346.71 E-value: 1.00e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303285204 25 ATFAALKKRGQCAFIPFICAGDPNLDATERAIAILDDEGADVIELGVPYSDPLADGPTIAQAATRALNAGTTLDKTLALL 104
Cdd:PRK13111 1 ALFAALKAEGRKALIPYITAGDPDLETSLEIIKALVEAGADIIELGIPFSDPVADGPVIQAASLRALAAGVTLADVFELV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303285204 105 ARVSPT-TKAPIVLFTYFNPIYQRGFEAFVEAVAAAGAKGLLVPDIPLEETPELSAICAKNGVDLVLLSTPTTPEARMTK 183
Cdd:PRK13111 81 REIREKdPTIPIVLMTYYNPIFQYGVERFAADAAEAGVDGLIIPDLPPEEAEELRAAAKKHGLDLIFLVAPTTTDERLKK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303285204 184 IAEASNGFIYLVSVTGVTGVRTNVESRVQELVSGLKKVTDKPVAVGFGISKKEQAAQVVGwGADGVIVGSALVRALGEAP 263
Cdd:PRK13111 161 IASHASGFVYYVSRAGVTGARSADAADLAELVARLKAHTDLPVAVGFGISTPEQAAAIAA-VADGVIVGSALVKIIEENP 239
|
250
....*....|....*....
gi 303285204 264 tpeEGLERLTALAKELREG 282
Cdd:PRK13111 240 ---EALEALAAFVKELKAA 255
|
|
| Tryptophan_synthase_alpha |
cd04724 |
Ttryptophan synthase (TRPS) alpha subunit (TSA). TPRS is a bifunctional tetrameric enzyme (2 ... |
37-280 |
1.25e-112 |
|
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: 325.59 E-value: 1.25e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303285204 37 AFIPFICAGDPNLDATERAIAILDDEGADVIELGVPYSDPLADGPTIAQAATRALNAGTTLDKTLALLARVSPTTKAPIV 116
Cdd:cd04724 1 ALIPYITAGDPDLETTLEILKALVEAGADIIELGIPFSDPVADGPVIQAASERALANGVTLKDVLELVKEIRKKNTIPIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303285204 117 LFTYFNPIYQRGFEAFVEAVAAAGAKGLLVPDIPLEETPELSAICAKNGVDLVLLSTPTTPEARMTKIAEASNGFIYLVS 196
Cdd:cd04724 81 LMGYYNPILQYGLERFLRDAKEAGVDGLIIPDLPPEEAEEFREAAKEYGLDLIFLVAPTTPDERIKKIAELASGFIYYVS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303285204 197 VTGVTGVRTNVESRVQELVSGLKKVTDKPVAVGFGISKKEQAAQVVGWgADGVIVGSALVRALGEAPtPEEGLERLTALA 276
Cdd:cd04724 161 RTGVTGARTELPDDLKELIKRIRKYTDLPIAVGFGISTPEQAAEVAKY-ADGVIVGSALVKIIEEGG-EEEALEALKELA 238
|
....
gi 303285204 277 KELR 280
Cdd:cd04724 239 ESLK 242
|
|
| trpA |
TIGR00262 |
tryptophan synthase, alpha subunit; Tryptophan synthase catalyzes the last step in the ... |
27-280 |
8.99e-104 |
|
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: 303.50 E-value: 8.99e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303285204 27 FAALKKRGQCAFIPFICAGDPNLDATERAIAILDDEGADVIELGVPYSDPLADGPTIAQAATRALNAGTTLDKTLALLAR 106
Cdd:TIGR00262 1 FETLKQRGEGAFIPFVTAGDPTLETSLEIIKTLIEAGADALELGVPFSDPLADGPTIQAADLRALRAGMTPEKCFELLKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303285204 107 VSP-TTKAPIVLFTYFNPIYQRGFEAFVEAVAAAGAKGLLVPDIPLEETPELSAICAKNGVDLVLLSTPTTPEARMTKIA 185
Cdd:TIGR00262 81 VRQkHPNIPIGLLTYYNLIFRKGVEEFYAKCKEVGVDGVLVADLPLEESGDLVEAAKKHGVKPIFLVAPNADDERLKQIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303285204 186 EASNGFIYLVSVTGVTGVRTNVESRVQELVSGLKKVTDKPVAVGFGISKKEQAAQVVGWGADGVIVGSALVRALGE-APT 264
Cdd:TIGR00262 161 EKSQGFVYLVSRAGVTGARNRAASALNELVKRLKAYSAKPVLVGFGISKPEQVKQAIDAGADGVIVGSAIVKIIEEnLNT 240
|
250
....*....|....*.
gi 303285204 265 PEEGLERLTALAKELR 280
Cdd:TIGR00262 241 PEKMLQALEEFVQNLK 256
|
|
| Trp_syntA |
pfam00290 |
Tryptophan synthase alpha chain; |
27-283 |
1.48e-102 |
|
Tryptophan synthase alpha chain;
Pssm-ID: 395227 Cd Length: 258 Bit Score: 300.77 E-value: 1.48e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303285204 27 FAALKKRGQCAFIPFICAGDPNLDATERAIAILDDEGADVIELGVPYSDPLADGPTIAQAATRALNAGTTLDKTLALLAR 106
Cdd:pfam00290 1 FANLKAENRAAFVPYVTAGDPDLEQSLEILKTLEKAGADAIELGVPFSDPLADGPTIQRANLRALASGVTLQSTLEMVRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303285204 107 V-SPTTKAPIVLFTYFNPIYQRGFEAFVEAVAAAGAKGLLVPDIPLEETPELSAICAKNGVDLVLLSTPTTPEARMTKIA 185
Cdd:pfam00290 81 VrSKGVEVPIVLMTYYNPVLNYGIERFYALAAEAGVDGLIVPDLPPEEADSLRQAAKDHGLELVFLVAPTTSDERLKTVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303285204 186 EASNGFIYLVSVTGVTGVRTNVESRVQELVSGLKKVTDKPVAVGFGISKKEQAAQvVGWGADGVIVGSALVRALGEAP-T 264
Cdd:pfam00290 161 EQAEGFVYLVSRAGVTGAENAVNAQVDELVERLKKYTAVPVAVGFGISTPEHVKQ-AAAGADGVIVGSALVRIIEEAAdG 239
|
250
....*....|....*....
gi 303285204 265 PEEGLERLTALAKELREGS 283
Cdd:pfam00290 240 PEQGLARLEELAGEMKAAA 258
|
|
| trpA |
CHL00200 |
tryptophan synthase alpha subunit; Provisional |
22-281 |
1.21e-99 |
|
tryptophan synthase alpha subunit; Provisional
Pssm-ID: 214394 Cd Length: 263 Bit Score: 293.59 E-value: 1.21e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303285204 22 SIGATFAALKKrgQCAFIPFICAGDPNLDATERAIAILDDEGADVIELGVPYSDPLADGPTIAQAATRALNAGTTLDKTL 101
Cdd:CHL00200 3 TISNVFEKLDK--QCALIPFITAGDPDIVITKKALKILDKKGADIIELGIPYSDPLADGPIIQEASNRALKQGINLNKIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303285204 102 ALLARVSPTTKAPIVLFTYFNPIYQRGFEAFVEAVAAAGAKGLLVPDIPLEETPELSAICAKNGVDLVLLSTPTTPEARM 181
Cdd:CHL00200 81 SILSEVNGEIKAPIVIFTYYNPVLHYGINKFIKKISQAGVKGLIIPDLPYEESDYLISVCNLYNIELILLIAPTSSKSRI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303285204 182 TKIAEASNGFIYLVSVTGVTGVRTNVESRVQELVSGLKKVTDKPVAVGFGISKKEQAAQVVGWGADGVIVGSALVRALgE 261
Cdd:CHL00200 161 QKIARAAPGCIYLVSTTGVTGLKTELDKKLKKLIETIKKMTNKPIILGFGISTSEQIKQIKGWNINGIVIGSACVQIL-L 239
|
250 260
....*....|....*....|
gi 303285204 262 APTPEEGLERLTALAKELRE 281
Cdd:CHL00200 240 GSSPEKGLDQLSEFCKVAKK 259
|
|
| trpA |
PRK13125 |
tryptophan synthase subunit alpha; Provisional |
37-282 |
1.92e-25 |
|
tryptophan synthase subunit alpha; Provisional
Pssm-ID: 237286 Cd Length: 244 Bit Score: 101.66 E-value: 1.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303285204 37 AFIPFICAGDPNLDATERAIAILDdEGADVIELGVPYSDPLADGPTIAQAATRALNAGTtldktLALLARVSPTTKAPIV 116
Cdd:PRK13125 5 GLVVYLTAGYPNVESFKEFIIGLV-ELVDILELGIPPKYPKYDGPVIRKSHRKVKGLDI-----WPLLEEVRKDVSVPII 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303285204 117 LFTYFNPiYQRGFEAFVEAVAAAGAKGLLVPDIPL---EETPELSAICAKNGVDLVLLSTPTTPEARMTKIAEASNGFIY 193
Cdd:PRK13125 79 LMTYLED-YVDSLDNFLNMARDVGADGVLFPDLLIdypDDLEKYVEIIKNKGLKPVFFTSPKFPDLLIHRLSKLSPLFIY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303285204 194 LvSVTGVTGVRTNVEsrVQELVSGLKK-VTDKPVAVGFGISKKEQAAQVVGWGADGVIVGSALVRALgeaptPEEGLERL 272
Cdd:PRK13125 158 Y-GLRPATGVPLPVS--VERNIKRVRNlVGNKYLVVGFGLDSPEDARDALSAGADGVVVGTAFIEEL-----EKNGVESA 229
|
250
....*....|
gi 303285204 273 TALAKELREG 282
Cdd:PRK13125 230 LNLLKKIRGA 239
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
42-253 |
1.83e-05 |
|
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: 44.88 E-value: 1.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303285204 42 ICAGDPNLDATERAIA-ILDDEGADVIELGVPYSDPLADGPTIAqaatralnagttldktlALLARVSPTTKAPIVLFTY 120
Cdd:cd04722 3 LALLAGGPSGDPVELAkAAAEAGADAIIVGTRSSDPEEAETDDK-----------------EVLKEVAAETDLPLGVQLA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303285204 121 FNPIYQRgFEAFVEAVAAAGAKGLLVPDIPLEETPELSAICAK-----NGVDLVLLSTPTTPEARMTKIAEASnGFIYLV 195
Cdd:cd04722 66 INDAAAA-VDIAAAAARAAGADGVEIHGAVGYLAREDLELIRElreavPDVKVVVKLSPTGELAAAAAEEAGV-DEVGLG 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 303285204 196 SVTGVTGVRTnVESRVQELVSGLKKVTDKPVAVGFGISKKEQAAQVVGWGADGVIVGS 253
Cdd:cd04722 144 NGGGGGGGRD-AVPIADLLLILAKRGSKVPVIAGGGINDPEDAAEALALGADGVIVGS 200
|
|
| GGGP-family |
TIGR01768 |
geranylgeranylglyceryl phosphate synthase family protein; This model represents a family of ... |
213-253 |
9.68e-04 |
|
geranylgeranylglyceryl phosphate synthase family protein; This model represents a family of sequences including geranylgeranylglyceryl phosphate synthase which catalyzes the first committed step in the synthesis of ether-linked membrane lipids in archaea. The clade of bacterial sequences may have the same function or a closely related function. This model supercedes TIGR00265, which has been retired.
Pssm-ID: 273794 Cd Length: 223 Bit Score: 39.77 E-value: 9.68e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 303285204 213 ELVSGLKKVTDK-PVAVGFGISKKEQAAQVVGWGADGVIVGS 253
Cdd:TIGR01768 168 ELVAEVKKVLDKaRLFVGGGIRSVEKAREMAEAGADTVVTGN 209
|
|
| NanE |
cd04729 |
N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to ... |
194-257 |
1.83e-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: 39.10 E-value: 1.83e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 303285204 194 LVSVT--GVTGVRTNVESRVQELVSGLKKVTDKPVAVGFGISKKEQAAQVVGWGADGVIVGSALVR 257
Cdd:cd04729 146 IIGTTlsGYTEETAKTEDPDFELLKELRKALGIPVIAEGRINSPEQAAKALELGADAVVVGSAITR 211
|
|
| IGPS |
cd00331 |
Indole-3-glycerol phosphate synthase (IGPS); an enzyme in the tryptophan biosynthetic pathway, ... |
231-272 |
2.33e-03 |
|
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: 38.60 E-value: 2.33e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 303285204 231 GISKKEQAAQVVGWGADGVIVGSALVRalgeAPTPEEGLERL 272
Cdd:cd00331 180 GISTPEDVKRLAEAGADAVLIGESLMR----APDPGAALREL 217
|
|
| PcrB_like |
cd02812 |
PcrB_like proteins. One member of this family, a protein from Archaeoglobus fulgidus, has been ... |
213-262 |
2.33e-03 |
|
PcrB_like proteins. One member of this family, a protein from Archaeoglobus fulgidus, has been characterized as a (S)-3-O-geranylgeranylglyceryl phosphate synthase (AfGGGPS). AfGGGPS catalyzes the formation of an ether linkage between sn-glycerol-1-phosphate (G1P) and geranylgeranyl diphosphate (GGPP), the committed step in archaeal lipid biosynthesis. Therefore, it has been proposed that PcrB-like proteins are either prenyltransferases or are involved in lipoteichoic acid biosynthesis although the exact function is still unknown.
Pssm-ID: 239206 Cd Length: 219 Bit Score: 38.76 E-value: 2.33e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 303285204 213 ELVSGLKKVTDK-PVAVGFGISKKEQAAQVVGWGADGVIVGSALVRALGEA 262
Cdd:cd02812 164 EVVRAVKKVLGDtPLIVGGGIRSGEQAKEMAEAGADTIVVGNIVEEDPNAA 214
|
|
| TIGR00007 |
TIGR00007 |
phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; This protein family ... |
177-257 |
3.17e-03 |
|
phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; This protein family consists of HisA, phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase, the enzyme catalyzing the fourth step in histidine biosynthesis. It is closely related to the enzyme HisF for the sixth step. Examples of this enzyme in Actinobacteria have been found to be bifunctional, also possessing phosphoribosylanthranilate isomerase activity; the trusted cutoff here has now been raised to 275.0 to exclude the bifunctional group, now represented by model TIGR01919. HisA from Lactococcus lactis was reported to be inactive (MEDLINE:93322317). [Amino acid biosynthesis, Histidine family]
Pssm-ID: 272850 [Multi-domain] Cd Length: 230 Bit Score: 38.33 E-value: 3.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303285204 177 PEARMTKIAEASNGFIYLVSVTGVTGVRTNVESRVQELVsglkKVTDKPVAVGFGISKKEQAAQVVGWGADGVIVGSALV 256
Cdd:TIGR00007 30 PVEAAKKWEEEGAERIHVVDLDGAKEGGPVNLPVIKKIV----RETGVPVQVGGGIRSLEDVEKLLDLGVDRVIIGTAAV 105
|
.
gi 303285204 257 R 257
Cdd:TIGR00007 106 E 106
|
|
| BtpA |
COG0434 |
Membrane biogenesis protein, BtpA/SgcQ family [Cell wall/membrane/envelope biogenesis]; |
200-280 |
3.87e-03 |
|
Membrane biogenesis protein, BtpA/SgcQ family [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440203 Cd Length: 268 Bit Score: 38.23 E-value: 3.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303285204 200 VTGVRTNVESRVQELVSGLKKVTDKPVAVGFGIsKKEQAAQVVGWgADGVIVGSALVRAlG--EAPTPEEGLERLTALAK 277
Cdd:COG0434 189 VSGARTGEATDLEDLKRVKEAAPDVPVLVGSGV-TPENVAELLSV-ADGAIVGSSLKRD-GktWNPVDPERVRRFMEAVR 265
|
...
gi 303285204 278 ELR 280
Cdd:COG0434 266 RLR 268
|
|
| PRK04169 |
PRK04169 |
heptaprenylglyceryl phosphate synthase; |
213-255 |
4.41e-03 |
|
heptaprenylglyceryl phosphate synthase;
Pssm-ID: 235237 Cd Length: 232 Bit Score: 37.87 E-value: 4.41e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 303285204 213 ELVSGLKKVTDK-PVAVGFGISKKEQAAQVVGWGADGVIVGSAL 255
Cdd:PRK04169 173 EMVKAVKKALDItPLIYGGGIRSPEQARELMAAGADTIVVGNII 216
|
|
| |
