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Conserved domains on  [gi|489914040|ref|WP_003817445|]
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tryptophan synthase subunit alpha [Bifidobacterium bifidum]

Protein Classification

tryptophan synthase subunit alpha( domain architecture ID 10785067)

tryptophan synthase (TRPS) alpha subunit catalyzes the cleavage of indole 3-glycerol phosphate (IGP) to indole and d-glyceraldehyde 3-phosphate (G3P).

EC:  4.2.1.20
Gene Ontology:  GO:0004834
PubMed:  2679363|11893063|18486479|32677310|12206759|11257493
SCOP:  4003071

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TrpA COG0159
Tryptophan synthase alpha chain [Amino acid transport and metabolism]; Tryptophan synthase ...
 23-286 7.46e-121

Tryptophan synthase alpha chain [Amino acid transport and metabolism]; Tryptophan synthase alpha chain is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


:

Pssm-ID: 439929  Cd Length: 262  Bit Score: 346.28  E-value: 7.46e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489914040  23 EAMFDRLKAENKPAFIGYLPYGFPNPDISLDALRTMIEHGVDAVEIGLPYSDPVMDGPVIQAASQIALNNGESINGVFKA 102
Cdd:COG0159    4 DAAFAALKAEGRKALIPYLTAGDPDLETTLEIIKALVEAGADIIELGIPFSDPVADGPVIQAASERALANGVTLDDVFEL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489914040 103 VETVANAGGVPLI-MSYWNLIYHYGVERFACDFENAGGAGLITPDLIPDEAGEWIEASDRHGLDRIFLVSPDSASERLEL 181
Cdd:COG0159   84 VREFREDPDTPLVlMGYYNPVFRYGVERFAADAAEAGVDGLIVPDLPPEEAEELRAAADAHGLDLIFLVAPTTSDERIKK 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489914040 182 VARNARGFVYAASRMGVTGERDTISASPETLVERARNAGARNVCVGIGVSTPEQGAKVGAYADGVIVGSALVHTLLDDDN 261
Cdd:COG0159  164 IAAAASGFVYYVSVTGVTGARTAVSDDLAELVARIRAHTDLPVAVGFGISTPEQAAEVAAYADGVIVGSALVKLIEEGGD 243

                        250       260
                 ....*....|....*....|....*
gi 489914040 262 vtakapKEGLRDLAAKVEALSEGIH 286
Cdd:COG0159  244 ------DEALEALAAFVRELKAALR 262
 
Name Accession Description Interval E-value
TrpA COG0159
Tryptophan synthase alpha chain [Amino acid transport and metabolism]; Tryptophan synthase ...
 23-286 7.46e-121

Tryptophan synthase alpha chain [Amino acid transport and metabolism]; Tryptophan synthase alpha chain is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


Pssm-ID: 439929  Cd Length: 262  Bit Score: 346.28  E-value: 7.46e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489914040  23 EAMFDRLKAENKPAFIGYLPYGFPNPDISLDALRTMIEHGVDAVEIGLPYSDPVMDGPVIQAASQIALNNGESINGVFKA 102
Cdd:COG0159    4 DAAFAALKAEGRKALIPYLTAGDPDLETTLEIIKALVEAGADIIELGIPFSDPVADGPVIQAASERALANGVTLDDVFEL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489914040 103 VETVANAGGVPLI-MSYWNLIYHYGVERFACDFENAGGAGLITPDLIPDEAGEWIEASDRHGLDRIFLVSPDSASERLEL 181
Cdd:COG0159   84 VREFREDPDTPLVlMGYYNPVFRYGVERFAADAAEAGVDGLIVPDLPPEEAEELRAAADAHGLDLIFLVAPTTSDERIKK 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489914040 182 VARNARGFVYAASRMGVTGERDTISASPETLVERARNAGARNVCVGIGVSTPEQGAKVGAYADGVIVGSALVHTLLDDDN 261
Cdd:COG0159  164 IAAAASGFVYYVSVTGVTGARTAVSDDLAELVARIRAHTDLPVAVGFGISTPEQAAEVAAYADGVIVGSALVKLIEEGGD 243

                        250       260
                 ....*....|....*....|....*
gi 489914040 262 vtakapKEGLRDLAAKVEALSEGIH 286
Cdd:COG0159  244 ------DEALEALAAFVRELKAALR 262
trpA PRK13111
tryptophan synthase subunit alpha; Provisional
 24-287 8.46e-121

tryptophan synthase subunit alpha; Provisional


Pssm-ID: 237285  Cd Length: 258  Bit Score: 346.32  E-value: 8.46e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489914040  24 AMFDRLKAENKPAFIGYLPYGFPNPDISLDALRTMIEHGVDAVEIGLPYSDPVMDGPVIQAASQIALNNGESINGVFKAV 103
Cdd:PRK13111   1 ALFAALKAEGRKALIPYITAGDPDLETSLEIIKALVEAGADIIELGIPFSDPVADGPVIQAASLRALAAGVTLADVFELV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489914040 104 ETV-ANAGGVPLI-MSYWNLIYHYGVERFACDFENAGGAGLITPDLIPDEAGEWIEASDRHGLDRIFLVSPDSASERLEL 181
Cdd:PRK13111  81 REIrEKDPTIPIVlMTYYNPIFQYGVERFAADAAEAGVDGLIIPDLPPEEAEELRAAAKKHGLDLIFLVAPTTTDERLKK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489914040 182 VARNARGFVYAASRMGVTGERDTISASPETLVERARNAGARNVCVGIGVSTPEQGAKVGAYADGVIVGSALVHTLLDDdn 261
Cdd:PRK13111 161 IASHASGFVYYVSRAGVTGARSADAADLAELVARLKAHTDLPVAVGFGISTPEQAAAIAAVADGVIVGSALVKIIEEN-- 238

                        250       260
                 ....*....|....*....|....*.
gi 489914040 262 vtakapKEGLRDLAAKVEALSEGIHN 287
Cdd:PRK13111 239 ------PEALEALAAFVKELKAALRS 258
Tryptophan_synthase_alpha cd04724
Ttryptophan synthase (TRPS) alpha subunit (TSA). TPRS is a bifunctional tetrameric enzyme (2 ...
 36-281 7.99e-105

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: 305.17  E-value: 7.99e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489914040  36 AFIGYLPYGFPNPDISLDALRTMIEHGVDAVEIGLPYSDPVMDGPVIQAASQIALNNGESINGVFKAVETVANAGGVPLI 115
Cdd:cd04724    1 ALIPYITAGDPDLETTLEILKALVEAGADIIELGIPFSDPVADGPVIQAASERALANGVTLKDVLELVKEIRKKNTIPIV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489914040 116 -MSYWNLIYHYGVERFACDFENAGGAGLITPDLIPDEAGEWIEASDRHGLDRIFLVSPDSASERLELVARNARGFVYAAS 194
Cdd:cd04724   81 lMGYYNPILQYGLERFLRDAKEAGVDGLIIPDLPPEEAEEFREAAKEYGLDLIFLVAPTTPDERIKKIAELASGFIYYVS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489914040 195 RMGVTGERDTISASPETLVERARNAGARNVCVGIGVSTPEQGAKVGAYADGVIVGSALVHTLLDDdnvtakAPKEGLRDL 274
Cdd:cd04724  161 RTGVTGARTELPDDLKELIKRIRKYTDLPIAVGFGISTPEQAAEVAKYADGVIVGSALVKIIEEG------GEEEALEAL 234


                 ....*..
gi 489914040 275 AAKVEAL 281
Cdd:cd04724  235 KELAESL 241
Trp_syntA pfam00290
Tryptophan synthase alpha chain;
26-285 1.24e-84

Tryptophan synthase alpha chain;


Pssm-ID: 395227  Cd Length: 258  Bit Score: 254.54  E-value: 1.24e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489914040   26 FDRLKAENKPAFIGYLPYGFPNPDISLDALRTMIEHGVDAVEIGLPYSDPVMDGPVIQAASQIALNNGESINGVFKAVET 105
Cdd:pfam00290   1 FANLKAENRAAFVPYVTAGDPDLEQSLEILKTLEKAGADAIELGVPFSDPLADGPTIQRANLRALASGVTLQSTLEMVRE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489914040  106 VANAG-GVPLI-MSYWNLIYHYGVERFACDFENAGGAGLITPDLIPDEAGEWIEASDRHGLDRIFLVSPDSASERLELVA 183
Cdd:pfam00290  81 VRSKGvEVPIVlMTYYNPVLNYGIERFYALAAEAGVDGLIVPDLPPEEADSLRQAAKDHGLELVFLVAPTTSDERLKTVV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489914040  184 RNARGFVYAASRMGVTGERDTISASPETLVERARNAGARNVCVGIGVSTPEQGAKVGAYADGVIVGSALVHTLLDDdnvt 263
Cdd:pfam00290 161 EQAEGFVYLVSRAGVTGAENAVNAQVDELVERLKKYTAVPVAVGFGISTPEHVKQAAAGADGVIVGSALVRIIEEA---- 236

                         250       260
                  ....*....|....*....|..
gi 489914040  264 AKAPKEGLRDLAAKVEALSEGI 285
Cdd:pfam00290 237 ADGPEQGLARLEELAGEMKAAA 258
trpA TIGR00262
tryptophan synthase, alpha subunit; Tryptophan synthase catalyzes the last step in the ...
 26-282 6.93e-76

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: 232.24  E-value: 6.93e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489914040   26 FDRLKAENKPAFIGYLPYGFPNPDISLDALRTMIEHGVDAVEIGLPYSDPVMDGPVIQAASQIALNNGESINGVFKAVET 105
Cdd:TIGR00262   1 FETLKQRGEGAFIPFVTAGDPTLETSLEIIKTLIEAGADALELGVPFSDPLADGPTIQAADLRALRAGMTPEKCFELLKK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489914040  106 V-ANAGGVPLI-MSYWNLIYHYGVERFACDFENAGGAGLITPDLIPDEAGEWIEASDRHGLDRIFLVSPDSASERLELVA 183
Cdd:TIGR00262  81 VrQKHPNIPIGlLTYYNLIFRKGVEEFYAKCKEVGVDGVLVADLPLEESGDLVEAAKKHGVKPIFLVAPNADDERLKQIA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489914040  184 RNARGFVYAASRMGVTGERDTISASPETLVERARNAGARNVCVGIGVSTPEQGAKV-GAYADGVIVGSALVHTLldddNV 262
Cdd:TIGR00262 161 EKSQGFVYLVSRAGVTGARNRAASALNELVKRLKAYSAKPVLVGFGISKPEQVKQAiDAGADGVIVGSAIVKII----EE 236

                         250       260
                  ....*....|....*....|
gi 489914040  263 TAKAPKEGLRDLAAKVEALS 282
Cdd:TIGR00262 237 NLNTPEKMLQALEEFVQNLK 256
 
Name Accession Description Interval E-value
TrpA COG0159
Tryptophan synthase alpha chain [Amino acid transport and metabolism]; Tryptophan synthase ...
 23-286 7.46e-121

Tryptophan synthase alpha chain [Amino acid transport and metabolism]; Tryptophan synthase alpha chain is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


Pssm-ID: 439929  Cd Length: 262  Bit Score: 346.28  E-value: 7.46e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489914040  23 EAMFDRLKAENKPAFIGYLPYGFPNPDISLDALRTMIEHGVDAVEIGLPYSDPVMDGPVIQAASQIALNNGESINGVFKA 102
Cdd:COG0159    4 DAAFAALKAEGRKALIPYLTAGDPDLETTLEIIKALVEAGADIIELGIPFSDPVADGPVIQAASERALANGVTLDDVFEL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489914040 103 VETVANAGGVPLI-MSYWNLIYHYGVERFACDFENAGGAGLITPDLIPDEAGEWIEASDRHGLDRIFLVSPDSASERLEL 181
Cdd:COG0159   84 VREFREDPDTPLVlMGYYNPVFRYGVERFAADAAEAGVDGLIVPDLPPEEAEELRAAADAHGLDLIFLVAPTTSDERIKK 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489914040 182 VARNARGFVYAASRMGVTGERDTISASPETLVERARNAGARNVCVGIGVSTPEQGAKVGAYADGVIVGSALVHTLLDDDN 261
Cdd:COG0159  164 IAAAASGFVYYVSVTGVTGARTAVSDDLAELVARIRAHTDLPVAVGFGISTPEQAAEVAAYADGVIVGSALVKLIEEGGD 243

                        250       260
                 ....*....|....*....|....*
gi 489914040 262 vtakapKEGLRDLAAKVEALSEGIH 286
Cdd:COG0159  244 ------DEALEALAAFVRELKAALR 262
trpA PRK13111
tryptophan synthase subunit alpha; Provisional
 24-287 8.46e-121

tryptophan synthase subunit alpha; Provisional


Pssm-ID: 237285  Cd Length: 258  Bit Score: 346.32  E-value: 8.46e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489914040  24 AMFDRLKAENKPAFIGYLPYGFPNPDISLDALRTMIEHGVDAVEIGLPYSDPVMDGPVIQAASQIALNNGESINGVFKAV 103
Cdd:PRK13111   1 ALFAALKAEGRKALIPYITAGDPDLETSLEIIKALVEAGADIIELGIPFSDPVADGPVIQAASLRALAAGVTLADVFELV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489914040 104 ETV-ANAGGVPLI-MSYWNLIYHYGVERFACDFENAGGAGLITPDLIPDEAGEWIEASDRHGLDRIFLVSPDSASERLEL 181
Cdd:PRK13111  81 REIrEKDPTIPIVlMTYYNPIFQYGVERFAADAAEAGVDGLIIPDLPPEEAEELRAAAKKHGLDLIFLVAPTTTDERLKK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489914040 182 VARNARGFVYAASRMGVTGERDTISASPETLVERARNAGARNVCVGIGVSTPEQGAKVGAYADGVIVGSALVHTLLDDdn 261
Cdd:PRK13111 161 IASHASGFVYYVSRAGVTGARSADAADLAELVARLKAHTDLPVAVGFGISTPEQAAAIAAVADGVIVGSALVKIIEEN-- 238

                        250       260
                 ....*....|....*....|....*.
gi 489914040 262 vtakapKEGLRDLAAKVEALSEGIHN 287
Cdd:PRK13111 239 ------PEALEALAAFVKELKAALRS 258
Tryptophan_synthase_alpha cd04724
Ttryptophan synthase (TRPS) alpha subunit (TSA). TPRS is a bifunctional tetrameric enzyme (2 ...
 36-281 7.99e-105

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: 305.17  E-value: 7.99e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489914040  36 AFIGYLPYGFPNPDISLDALRTMIEHGVDAVEIGLPYSDPVMDGPVIQAASQIALNNGESINGVFKAVETVANAGGVPLI 115
Cdd:cd04724    1 ALIPYITAGDPDLETTLEILKALVEAGADIIELGIPFSDPVADGPVIQAASERALANGVTLKDVLELVKEIRKKNTIPIV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489914040 116 -MSYWNLIYHYGVERFACDFENAGGAGLITPDLIPDEAGEWIEASDRHGLDRIFLVSPDSASERLELVARNARGFVYAAS 194
Cdd:cd04724   81 lMGYYNPILQYGLERFLRDAKEAGVDGLIIPDLPPEEAEEFREAAKEYGLDLIFLVAPTTPDERIKKIAELASGFIYYVS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489914040 195 RMGVTGERDTISASPETLVERARNAGARNVCVGIGVSTPEQGAKVGAYADGVIVGSALVHTLLDDdnvtakAPKEGLRDL 274
Cdd:cd04724  161 RTGVTGARTELPDDLKELIKRIRKYTDLPIAVGFGISTPEQAAEVAKYADGVIVGSALVKIIEEG------GEEEALEAL 234


                 ....*..
gi 489914040 275 AAKVEAL 281
Cdd:cd04724  235 KELAESL 241
Trp_syntA pfam00290
Tryptophan synthase alpha chain;
26-285 1.24e-84

Tryptophan synthase alpha chain;


Pssm-ID: 395227  Cd Length: 258  Bit Score: 254.54  E-value: 1.24e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489914040   26 FDRLKAENKPAFIGYLPYGFPNPDISLDALRTMIEHGVDAVEIGLPYSDPVMDGPVIQAASQIALNNGESINGVFKAVET 105
Cdd:pfam00290   1 FANLKAENRAAFVPYVTAGDPDLEQSLEILKTLEKAGADAIELGVPFSDPLADGPTIQRANLRALASGVTLQSTLEMVRE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489914040  106 VANAG-GVPLI-MSYWNLIYHYGVERFACDFENAGGAGLITPDLIPDEAGEWIEASDRHGLDRIFLVSPDSASERLELVA 183
Cdd:pfam00290  81 VRSKGvEVPIVlMTYYNPVLNYGIERFYALAAEAGVDGLIVPDLPPEEADSLRQAAKDHGLELVFLVAPTTSDERLKTVV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489914040  184 RNARGFVYAASRMGVTGERDTISASPETLVERARNAGARNVCVGIGVSTPEQGAKVGAYADGVIVGSALVHTLLDDdnvt 263
Cdd:pfam00290 161 EQAEGFVYLVSRAGVTGAENAVNAQVDELVERLKKYTAVPVAVGFGISTPEHVKQAAAGADGVIVGSALVRIIEEA---- 236

                         250       260
                  ....*....|....*....|..
gi 489914040  264 AKAPKEGLRDLAAKVEALSEGI 285
Cdd:pfam00290 237 ADGPEQGLARLEELAGEMKAAA 258
trpA TIGR00262
tryptophan synthase, alpha subunit; Tryptophan synthase catalyzes the last step in the ...
 26-282 6.93e-76

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: 232.24  E-value: 6.93e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489914040   26 FDRLKAENKPAFIGYLPYGFPNPDISLDALRTMIEHGVDAVEIGLPYSDPVMDGPVIQAASQIALNNGESINGVFKAVET 105
Cdd:TIGR00262   1 FETLKQRGEGAFIPFVTAGDPTLETSLEIIKTLIEAGADALELGVPFSDPLADGPTIQAADLRALRAGMTPEKCFELLKK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489914040  106 V-ANAGGVPLI-MSYWNLIYHYGVERFACDFENAGGAGLITPDLIPDEAGEWIEASDRHGLDRIFLVSPDSASERLELVA 183
Cdd:TIGR00262  81 VrQKHPNIPIGlLTYYNLIFRKGVEEFYAKCKEVGVDGVLVADLPLEESGDLVEAAKKHGVKPIFLVAPNADDERLKQIA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489914040  184 RNARGFVYAASRMGVTGERDTISASPETLVERARNAGARNVCVGIGVSTPEQGAKV-GAYADGVIVGSALVHTLldddNV 262
Cdd:TIGR00262 161 EKSQGFVYLVSRAGVTGARNRAASALNELVKRLKAYSAKPVLVGFGISKPEQVKQAiDAGADGVIVGSAIVKII----EE 236

                         250       260
                  ....*....|....*....|
gi 489914040  263 TAKAPKEGLRDLAAKVEALS 282
Cdd:TIGR00262 237 NLNTPEKMLQALEEFVQNLK 256
PLN02591 PLN02591
tryptophan synthase
 34-285 1.88e-65

tryptophan synthase


Pssm-ID: 178201  Cd Length: 250  Bit Score: 205.29  E-value: 1.88e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489914040  34 KPAFIGYLPYGFPNPDISLDALRTMIEHGVDAVEIGLPYSDPVMDGPVIQAASQIALNNGESINGVFKAVETVANAGGVP 113
Cdd:PLN02591   1 KVAFIPYITAGDPDLDTTAEALRLLDACGADVIELGVPYSDPLADGPVIQAAATRALEKGTTLDSVISMLKEVAPQLSCP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489914040 114 LIM-SYWNLIYHYGVERFACDFENAGGAGLITPDLIPDEAGEWIEASDRHGLDRIFLVSPDSASERLELVARNARGFVYA 192
Cdd:PLN02591  81 IVLfTYYNPILKRGIDKFMATIKEAGVHGLVVPDLPLEETEALRAEAAKNGIELVLLTTPTTPTERMKAIAEASEGFVYL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489914040 193 ASRMGVTGERDTISASPETLVERARNAGARNVCVGIGVSTPEQGAKVGAY-ADGVIVGSALVHTLLDddnvtAKAPKEGL 271
Cdd:PLN02591 161 VSSTGVTGARASVSGRVESLLQELKEVTDKPVAVGFGISKPEHAKQIAGWgADGVIVGSAMVKALGE-----AKSPEEGL 235

                        250
                 ....*....|....
gi 489914040 272 RDLAAKVEALSEGI 285
Cdd:PLN02591 236 KRLEKLAKSLKAAL 249
trpA CHL00200
tryptophan synthase alpha subunit; Provisional
 30-286 2.62e-61

tryptophan synthase alpha subunit; Provisional


Pssm-ID: 214394  Cd Length: 263  Bit Score: 194.98  E-value: 2.62e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489914040  30 KAENKPAFIGYLPYGFPNPDISLDALRTMIEHGVDAVEIGLPYSDPVMDGPVIQAASQIALNNGESINGVFKAVETVANA 109
Cdd:CHL00200  10 KLDKQCALIPFITAGDPDIVITKKALKILDKKGADIIELGIPYSDPLADGPIIQEASNRALKQGINLNKILSILSEVNGE 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489914040 110 GGVPLIM-SYWNLIYHYGVERFACDFENAGGAGLITPDLIPDEAGEWIEASDRHGLDRIFLVSPDSASERLELVARNARG 188
Cdd:CHL00200  90 IKAPIVIfTYYNPVLHYGINKFIKKISQAGVKGLIIPDLPYEESDYLISVCNLYNIELILLIAPTSSKSRIQKIARAAPG 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489914040 189 FVYAASRMGVTGERDTISASPETLVERARNAGARNVCVGIGVSTPEQGAKVGAY-ADGVIVGSALVHTLLDDdnvtakAP 267
Cdd:CHL00200 170 CIYLVSTTGVTGLKTELDKKLKKLIETIKKMTNKPIILGFGISTSEQIKQIKGWnINGIVIGSACVQILLGS------SP 243

                        250
                 ....*....|....*....
gi 489914040 268 KEGLRDLAAKVEALSEGIH 286
Cdd:CHL00200 244 EKGLDQLSEFCKVAKKSII 262
trpA PRK13125
tryptophan synthase subunit alpha; Provisional
 34-253 3.16e-25

tryptophan synthase subunit alpha; Provisional


Pssm-ID: 237286  Cd Length: 244  Bit Score: 100.50  E-value: 3.16e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489914040  34 KPAFIGYLPYGFPNPDISLDALRTMIEHgVDAVEIGLPYSDPVMDGPVIQAASQIAlnngeSINGVFKAVETVANAGGVP 113
Cdd:PRK13125   3 RPGLVVYLTAGYPNVESFKEFIIGLVEL-VDILELGIPPKYPKYDGPVIRKSHRKV-----KGLDIWPLLEEVRKDVSVP 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489914040 114 LI-MSYWNliyHYgVERFACDFENA---GGAGLITPDLI---PDEAGEWIEASDRHGLDRIFLVSPDSASERLELVARNA 186
Cdd:PRK13125  77 IIlMTYLE---DY-VDSLDNFLNMArdvGADGVLFPDLLidyPDDLEKYVEIIKNKGLKPVFFTSPKFPDLLIHRLSKLS 152

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489914040 187 RGFVYAASRmGVTGERdtISASPETLVERARN-AGARNVCVGIGVSTPEQGAK-VGAYADGVIVGSALV 253
Cdd:PRK13125 153 PLFIYYGLR-PATGVP--LPVSVERNIKRVRNlVGNKYLVVGFGLDSPEDARDaLSAGADGVVVGTAFI 218
TIM_phosphate_binding cd04722
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ...
 46-250 2.45e-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: 44.11  E-value: 2.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489914040  46 PNPDISLDALRTMIEHGVDAVEIGLPYSDPVMDGPVIQAASQIalnngesingvfkavetVANAGGVPLIMSYWNLIYHY 125
Cdd:cd04722    9 GPSGDPVELAKAAAEAGADAIIVGTRSSDPEEAETDDKEVLKE-----------------VAAETDLPLGVQLAINDAAA 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489914040 126 GVERFACDFENAGGAGLITPDLIPDEAGEWIEASDRH-----GLDRIFLVSPDSASERLELVARNArGFVYAASRMGVTG 200
Cdd:cd04722   72 AVDIAAAAARAAGADGVEIHGAVGYLAREDLELIRELreavpDVKVVVKLSPTGELAAAAAEEAGV-DEVGLGNGGGGGG 150

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 489914040 201 ERDTISASPETLVERARNAGaRNVCVGIGVSTPEQGAKVGA-YADGVIVGS 250
Cdd:cd04722  151 GRDAVPIADLLLILAKRGSK-VPVIAGGGINDPEDAAEALAlGADGVIVGS 200
BtpA COG0434
Membrane biogenesis protein, BtpA/SgcQ family [Cell wall/membrane/envelope biogenesis];
198-252 4.66e-03

Membrane biogenesis protein, BtpA/SgcQ family [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440203  Cd Length: 268  Bit Score: 37.84  E-value: 4.66e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 489914040 198 VTGERDTISASPETLVERARNAGARNVCVGIGVsTPEQGAKVGAYADGVIVGSAL 252
Cdd:COG0434  189 VSGARTGEATDLEDLKRVKEAAPDVPVLVGSGV-TPENVAELLSVADGAIVGSSL 242
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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