NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1002988495|ref|WP_061433022|]
View 

tryptophan synthase subunit alpha [Microcystis aeruginosa]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
TrpA COG0159
Tryptophan synthase alpha chain [Amino acid transport and metabolism]; Tryptophan synthase ...
 4-264 1.24e-140

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: 395.59  E-value: 1.24e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988495   4 VSECFRSLRSQGNCALIPFITAGDPDLSTTAQALRILDQAGADLIELGVPYSDPLADGPVIQAAATRALNRGVKLEDVLE 83
Cdd:COG0159     3 IDAAFAALKAEGRKALIPYLTAGDPDLETTLEIIKALVEAGADIIELGIPFSDPVADGPVIQAASERALANGVTLDDVFE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988495  84 IVKNAQGEVKAPIILFTYYNPIYHRGIDVFLDQIKAAGVSGLVVPDLPLEEAESLLQPAAAKGIEVILLVAPTSPPERIQ 163
Cdd:COG0159    83 LVREFREDPDTPLVLMGYYNPVFRYGVERFAADAAEAGVDGLIVPDLPPEEAEELRAAADAHGLDLIFLVAPTTSDERIK 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988495 164 AIARQSQGFIYLVSVTGVTGMRNQVATRVEELLDSIRSVTDKPVGVGFGISDPTQALQVKNWgADAVIVGSAMVKRLADN 243
Cdd:COG0159   163 KIAAAASGFVYYVSVTGVTGARTAVSDDLAELVARIRAHTDLPVAVGFGISTPEQAAEVAAY-ADGVIVGSALVKLIEEG 241

                         250       260
                  ....*....|....*....|.
gi 1002988495 244 SPSDGLKSLEEFCRSLKQAIQ 264
Cdd:COG0159   242 GDDEALEALAAFVRELKAALR 262
 
Name Accession Description Interval E-value
TrpA COG0159
Tryptophan synthase alpha chain [Amino acid transport and metabolism]; Tryptophan synthase ...
 4-264 1.24e-140

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: 395.59  E-value: 1.24e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988495   4 VSECFRSLRSQGNCALIPFITAGDPDLSTTAQALRILDQAGADLIELGVPYSDPLADGPVIQAAATRALNRGVKLEDVLE 83
Cdd:COG0159     3 IDAAFAALKAEGRKALIPYLTAGDPDLETTLEIIKALVEAGADIIELGIPFSDPVADGPVIQAASERALANGVTLDDVFE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988495  84 IVKNAQGEVKAPIILFTYYNPIYHRGIDVFLDQIKAAGVSGLVVPDLPLEEAESLLQPAAAKGIEVILLVAPTSPPERIQ 163
Cdd:COG0159    83 LVREFREDPDTPLVLMGYYNPVFRYGVERFAADAAEAGVDGLIVPDLPPEEAEELRAAADAHGLDLIFLVAPTTSDERIK 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988495 164 AIARQSQGFIYLVSVTGVTGMRNQVATRVEELLDSIRSVTDKPVGVGFGISDPTQALQVKNWgADAVIVGSAMVKRLADN 243
Cdd:COG0159   163 KIAAAASGFVYYVSVTGVTGARTAVSDDLAELVARIRAHTDLPVAVGFGISTPEQAAEVAAY-ADGVIVGSALVKLIEEG 241

                         250       260
                  ....*....|....*....|.
gi 1002988495 244 SPSDGLKSLEEFCRSLKQAIQ 264
Cdd:COG0159   242 GDDEALEALAAFVRELKAALR 262
trpA PRK13111
tryptophan synthase subunit alpha; Provisional
 6-264 2.06e-137

tryptophan synthase subunit alpha; Provisional


Pssm-ID: 237285  Cd Length: 258  Bit Score: 387.16  E-value: 2.06e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988495   6 ECFRSLRSQGNCALIPFITAGDPDLSTTAQALRILDQAGADLIELGVPYSDPLADGPVIQAAATRALNRGVKLEDVLEIV 85
Cdd:PRK13111    1 ALFAALKAEGRKALIPYITAGDPDLETSLEIIKALVEAGADIIELGIPFSDPVADGPVIQAASLRALAAGVTLADVFELV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988495  86 KNA-QGEVKAPIILFTYYNPIYHRGIDVFLDQIKAAGVSGLVVPDLPLEEAESLLQPAAAKGIEVILLVAPTSPPERIQA 164
Cdd:PRK13111   81 REIrEKDPTIPIVLMTYYNPIFQYGVERFAADAAEAGVDGLIIPDLPPEEAEELRAAAKKHGLDLIFLVAPTTTDERLKK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988495 165 IARQSQGFIYLVSVTGVTGMRNQVATRVEELLDSIRSVTDKPVGVGFGISDPTQALQVKNwGADAVIVGSAMVKRLADNs 244
Cdd:PRK13111  161 IASHASGFVYYVSRAGVTGARSADAADLAELVARLKAHTDLPVAVGFGISTPEQAAAIAA-VADGVIVGSALVKIIEEN- 238

                         250       260
                  ....*....|....*....|
gi 1002988495 245 pSDGLKSLEEFCRSLKQAIQ 264
Cdd:PRK13111  239 -PEALEALAAFVKELKAALR 257
Tryptophan_synthase_alpha cd04724
Ttryptophan synthase (TRPS) alpha subunit (TSA). TPRS is a bifunctional tetrameric enzyme (2 ...
 18-260 6.16e-126

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: 357.56  E-value: 6.16e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988495  18 ALIPFITAGDPDLSTTAQALRILDQAGADLIELGVPYSDPLADGPVIQAAATRALNRGVKLEDVLEIVKNAQGEVKAPII 97
Cdd:cd04724     1 ALIPYITAGDPDLETTLEILKALVEAGADIIELGIPFSDPVADGPVIQAASERALANGVTLKDVLELVKEIRKKNTIPIV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988495  98 LFTYYNPIYHRGIDVFLDQIKAAGVSGLVVPDLPLEEAESLLQPAAAKGIEVILLVAPTSPPERIQAIARQSQGFIYLVS 177
Cdd:cd04724    81 LMGYYNPILQYGLERFLRDAKEAGVDGLIIPDLPPEEAEEFREAAKEYGLDLIFLVAPTTPDERIKKIAELASGFIYYVS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988495 178 VTGVTGMRNQVATRVEELLDSIRSVTDKPVGVGFGISDPTQALQVKNWgADAVIVGSAMVKRLADNSPSDGLKSLEEFCR 257
Cdd:cd04724   161 RTGVTGARTELPDDLKELIKRIRKYTDLPIAVGFGISTPEQAAEVAKY-ADGVIVGSALVKIIEEGGEEEALEALKELAE 239


                  ...
gi 1002988495 258 SLK 260
Cdd:cd04724   240 SLK 242
trpA TIGR00262
tryptophan synthase, alpha subunit; Tryptophan synthase catalyzes the last step in the ...
 8-260 7.43e-119

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: 340.09  E-value: 7.43e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988495   8 FRSLRSQGNCALIPFITAGDPDLSTTAQALRILDQAGADLIELGVPYSDPLADGPVIQAAATRALNRGVKLEDVLEIVKN 87
Cdd:TIGR00262   1 FETLKQRGEGAFIPFVTAGDPTLETSLEIIKTLIEAGADALELGVPFSDPLADGPTIQAADLRALRAGMTPEKCFELLKK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988495  88 A-QGEVKAPIILFTYYNPIYHRGIDVFLDQIKAAGVSGLVVPDLPLEEAESLLQPAAAKGIEVILLVAPTSPPERIQAIA 166
Cdd:TIGR00262  81 VrQKHPNIPIGLLTYYNLIFRKGVEEFYAKCKEVGVDGVLVADLPLEESGDLVEAAKKHGVKPIFLVAPNADDERLKQIA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988495 167 RQSQGFIYLVSVTGVTGMRNQVATRVEELLDSIRSVTDKPVGVGFGISDPTQALQVKNWGADAVIVGSAMVKRLADN--S 244
Cdd:TIGR00262 161 EKSQGFVYLVSRAGVTGARNRAASALNELVKRLKAYSAKPVLVGFGISKPEQVKQAIDAGADGVIVGSAIVKIIEENlnT 240

                         250
                  ....*....|....*.
gi 1002988495 245 PSDGLKSLEEFCRSLK 260
Cdd:TIGR00262 241 PEKMLQALEEFVQNLK 256
Trp_syntA pfam00290
Tryptophan synthase alpha chain;
8-263 1.92e-110

Tryptophan synthase alpha chain;


Pssm-ID: 395227  Cd Length: 258  Bit Score: 318.87  E-value: 1.92e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988495   8 FRSLRSQGNCALIPFITAGDPDLSTTAQALRILDQAGADLIELGVPYSDPLADGPVIQAAATRALNRGVKLEDVLEIVKN 87
Cdd:pfam00290   1 FANLKAENRAAFVPYVTAGDPDLEQSLEILKTLEKAGADAIELGVPFSDPLADGPTIQRANLRALASGVTLQSTLEMVRE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988495  88 A-QGEVKAPIILFTYYNPIYHRGIDVFLDQIKAAGVSGLVVPDLPLEEAESLLQPAAAKGIEVILLVAPTSPPERIQAIA 166
Cdd:pfam00290  81 VrSKGVEVPIVLMTYYNPVLNYGIERFYALAAEAGVDGLIVPDLPPEEADSLRQAAKDHGLELVFLVAPTTSDERLKTVV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988495 167 RQSQGFIYLVSVTGVTGMRNQVATRVEELLDSIRSVTDKPVGVGFGISDPTQALQVkNWGADAVIVGSAMVKRLADN--S 244
Cdd:pfam00290 161 EQAEGFVYLVSRAGVTGAENAVNAQVDELVERLKKYTAVPVAVGFGISTPEHVKQA-AAGADGVIVGSALVRIIEEAadG 239

                         250
                  ....*....|....*....
gi 1002988495 245 PSDGLKSLEEFCRSLKQAI 263
Cdd:pfam00290 240 PEQGLARLEELAGEMKAAA 258
 
Name Accession Description Interval E-value
TrpA COG0159
Tryptophan synthase alpha chain [Amino acid transport and metabolism]; Tryptophan synthase ...
 4-264 1.24e-140

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: 395.59  E-value: 1.24e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988495   4 VSECFRSLRSQGNCALIPFITAGDPDLSTTAQALRILDQAGADLIELGVPYSDPLADGPVIQAAATRALNRGVKLEDVLE 83
Cdd:COG0159     3 IDAAFAALKAEGRKALIPYLTAGDPDLETTLEIIKALVEAGADIIELGIPFSDPVADGPVIQAASERALANGVTLDDVFE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988495  84 IVKNAQGEVKAPIILFTYYNPIYHRGIDVFLDQIKAAGVSGLVVPDLPLEEAESLLQPAAAKGIEVILLVAPTSPPERIQ 163
Cdd:COG0159    83 LVREFREDPDTPLVLMGYYNPVFRYGVERFAADAAEAGVDGLIVPDLPPEEAEELRAAADAHGLDLIFLVAPTTSDERIK 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988495 164 AIARQSQGFIYLVSVTGVTGMRNQVATRVEELLDSIRSVTDKPVGVGFGISDPTQALQVKNWgADAVIVGSAMVKRLADN 243
Cdd:COG0159   163 KIAAAASGFVYYVSVTGVTGARTAVSDDLAELVARIRAHTDLPVAVGFGISTPEQAAEVAAY-ADGVIVGSALVKLIEEG 241

                         250       260
                  ....*....|....*....|.
gi 1002988495 244 SPSDGLKSLEEFCRSLKQAIQ 264
Cdd:COG0159   242 GDDEALEALAAFVRELKAALR 262
trpA PRK13111
tryptophan synthase subunit alpha; Provisional
 6-264 2.06e-137

tryptophan synthase subunit alpha; Provisional


Pssm-ID: 237285  Cd Length: 258  Bit Score: 387.16  E-value: 2.06e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988495   6 ECFRSLRSQGNCALIPFITAGDPDLSTTAQALRILDQAGADLIELGVPYSDPLADGPVIQAAATRALNRGVKLEDVLEIV 85
Cdd:PRK13111    1 ALFAALKAEGRKALIPYITAGDPDLETSLEIIKALVEAGADIIELGIPFSDPVADGPVIQAASLRALAAGVTLADVFELV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988495  86 KNA-QGEVKAPIILFTYYNPIYHRGIDVFLDQIKAAGVSGLVVPDLPLEEAESLLQPAAAKGIEVILLVAPTSPPERIQA 164
Cdd:PRK13111   81 REIrEKDPTIPIVLMTYYNPIFQYGVERFAADAAEAGVDGLIIPDLPPEEAEELRAAAKKHGLDLIFLVAPTTTDERLKK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988495 165 IARQSQGFIYLVSVTGVTGMRNQVATRVEELLDSIRSVTDKPVGVGFGISDPTQALQVKNwGADAVIVGSAMVKRLADNs 244
Cdd:PRK13111  161 IASHASGFVYYVSRAGVTGARSADAADLAELVARLKAHTDLPVAVGFGISTPEQAAAIAA-VADGVIVGSALVKIIEEN- 238

                         250       260
                  ....*....|....*....|
gi 1002988495 245 pSDGLKSLEEFCRSLKQAIQ 264
Cdd:PRK13111  239 -PEALEALAAFVKELKAALR 257
PLN02591 PLN02591
tryptophan synthase
 17-264 5.98e-137

tryptophan synthase


Pssm-ID: 178201  Cd Length: 250  Bit Score: 385.56  E-value: 5.98e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988495  17 CALIPFITAGDPDLSTTAQALRILDQAGADLIELGVPYSDPLADGPVIQAAATRALNRGVKLEDVLEIVKNAQGEVKAPI 96
Cdd:PLN02591    2 VAFIPYITAGDPDLDTTAEALRLLDACGADVIELGVPYSDPLADGPVIQAAATRALEKGTTLDSVISMLKEVAPQLSCPI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988495  97 ILFTYYNPIYHRGIDVFLDQIKAAGVSGLVVPDLPLEEAESLLQPAAAKGIEVILLVAPTSPPERIQAIARQSQGFIYLV 176
Cdd:PLN02591   82 VLFTYYNPILKRGIDKFMATIKEAGVHGLVVPDLPLEETEALRAEAAKNGIELVLLTTPTTPTERMKAIAEASEGFVYLV 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988495 177 SVTGVTGMRNQVATRVEELLDSIRSVTDKPVGVGFGISDPTQALQVKNWGADAVIVGSAMVKRLAD-NSPSDGLKSLEEF 255
Cdd:PLN02591  162 SSTGVTGARASVSGRVESLLQELKEVTDKPVAVGFGISKPEHAKQIAGWGADGVIVGSAMVKALGEaKSPEEGLKRLEKL 241


                  ....*....
gi 1002988495 256 CRSLKQAIQ 264
Cdd:PLN02591  242 AKSLKAALP 250
Tryptophan_synthase_alpha cd04724
Ttryptophan synthase (TRPS) alpha subunit (TSA). TPRS is a bifunctional tetrameric enzyme (2 ...
 18-260 6.16e-126

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: 357.56  E-value: 6.16e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988495  18 ALIPFITAGDPDLSTTAQALRILDQAGADLIELGVPYSDPLADGPVIQAAATRALNRGVKLEDVLEIVKNAQGEVKAPII 97
Cdd:cd04724     1 ALIPYITAGDPDLETTLEILKALVEAGADIIELGIPFSDPVADGPVIQAASERALANGVTLKDVLELVKEIRKKNTIPIV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988495  98 LFTYYNPIYHRGIDVFLDQIKAAGVSGLVVPDLPLEEAESLLQPAAAKGIEVILLVAPTSPPERIQAIARQSQGFIYLVS 177
Cdd:cd04724    81 LMGYYNPILQYGLERFLRDAKEAGVDGLIIPDLPPEEAEEFREAAKEYGLDLIFLVAPTTPDERIKKIAELASGFIYYVS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988495 178 VTGVTGMRNQVATRVEELLDSIRSVTDKPVGVGFGISDPTQALQVKNWgADAVIVGSAMVKRLADNSPSDGLKSLEEFCR 257
Cdd:cd04724   161 RTGVTGARTELPDDLKELIKRIRKYTDLPIAVGFGISTPEQAAEVAKY-ADGVIVGSALVKIIEEGGEEEALEALKELAE 239


                  ...
gi 1002988495 258 SLK 260
Cdd:cd04724   240 SLK 242
trpA TIGR00262
tryptophan synthase, alpha subunit; Tryptophan synthase catalyzes the last step in the ...
 8-260 7.43e-119

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: 340.09  E-value: 7.43e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988495   8 FRSLRSQGNCALIPFITAGDPDLSTTAQALRILDQAGADLIELGVPYSDPLADGPVIQAAATRALNRGVKLEDVLEIVKN 87
Cdd:TIGR00262   1 FETLKQRGEGAFIPFVTAGDPTLETSLEIIKTLIEAGADALELGVPFSDPLADGPTIQAADLRALRAGMTPEKCFELLKK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988495  88 A-QGEVKAPIILFTYYNPIYHRGIDVFLDQIKAAGVSGLVVPDLPLEEAESLLQPAAAKGIEVILLVAPTSPPERIQAIA 166
Cdd:TIGR00262  81 VrQKHPNIPIGLLTYYNLIFRKGVEEFYAKCKEVGVDGVLVADLPLEESGDLVEAAKKHGVKPIFLVAPNADDERLKQIA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988495 167 RQSQGFIYLVSVTGVTGMRNQVATRVEELLDSIRSVTDKPVGVGFGISDPTQALQVKNWGADAVIVGSAMVKRLADN--S 244
Cdd:TIGR00262 161 EKSQGFVYLVSRAGVTGARNRAASALNELVKRLKAYSAKPVLVGFGISKPEQVKQAIDAGADGVIVGSAIVKIIEENlnT 240

                         250
                  ....*....|....*.
gi 1002988495 245 PSDGLKSLEEFCRSLK 260
Cdd:TIGR00262 241 PEKMLQALEEFVQNLK 256
trpA CHL00200
tryptophan synthase alpha subunit; Provisional
 1-263 5.21e-118

tryptophan synthase alpha subunit; Provisional


Pssm-ID: 214394  Cd Length: 263  Bit Score: 338.28  E-value: 5.21e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988495   1 MTAVSECFRSLRSQgnCALIPFITAGDPDLSTTAQALRILDQAGADLIELGVPYSDPLADGPVIQAAATRALNRGVKLED 80
Cdd:CHL00200    1 MNTISNVFEKLDKQ--CALIPFITAGDPDIVITKKALKILDKKGADIIELGIPYSDPLADGPIIQEASNRALKQGINLNK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988495  81 VLEIVKNAQGEVKAPIILFTYYNPIYHRGIDVFLDQIKAAGVSGLVVPDLPLEEAESLLQPAAAKGIEVILLVAPTSPPE 160
Cdd:CHL00200   79 ILSILSEVNGEIKAPIVIFTYYNPVLHYGINKFIKKISQAGVKGLIIPDLPYEESDYLISVCNLYNIELILLIAPTSSKS 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988495 161 RIQAIARQSQGFIYLVSVTGVTGMRNQVATRVEELLDSIRSVTDKPVGVGFGISDPTQALQVKNWGADAVIVGSAMVKRL 240
Cdd:CHL00200  159 RIQKIARAAPGCIYLVSTTGVTGLKTELDKKLKKLIETIKKMTNKPIILGFGISTSEQIKQIKGWNINGIVIGSACVQIL 238

                         250       260
                  ....*....|....*....|...
gi 1002988495 241 ADNSPSDGLKSLEEFCRSLKQAI 263
Cdd:CHL00200  239 LGSSPEKGLDQLSEFCKVAKKSI 261
Trp_syntA pfam00290
Tryptophan synthase alpha chain;
8-263 1.92e-110

Tryptophan synthase alpha chain;


Pssm-ID: 395227  Cd Length: 258  Bit Score: 318.87  E-value: 1.92e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988495   8 FRSLRSQGNCALIPFITAGDPDLSTTAQALRILDQAGADLIELGVPYSDPLADGPVIQAAATRALNRGVKLEDVLEIVKN 87
Cdd:pfam00290   1 FANLKAENRAAFVPYVTAGDPDLEQSLEILKTLEKAGADAIELGVPFSDPLADGPTIQRANLRALASGVTLQSTLEMVRE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988495  88 A-QGEVKAPIILFTYYNPIYHRGIDVFLDQIKAAGVSGLVVPDLPLEEAESLLQPAAAKGIEVILLVAPTSPPERIQAIA 166
Cdd:pfam00290  81 VrSKGVEVPIVLMTYYNPVLNYGIERFYALAAEAGVDGLIVPDLPPEEADSLRQAAKDHGLELVFLVAPTTSDERLKTVV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988495 167 RQSQGFIYLVSVTGVTGMRNQVATRVEELLDSIRSVTDKPVGVGFGISDPTQALQVkNWGADAVIVGSAMVKRLADN--S 244
Cdd:pfam00290 161 EQAEGFVYLVSRAGVTGAENAVNAQVDELVERLKKYTAVPVAVGFGISTPEHVKQA-AAGADGVIVGSALVRIIEEAadG 239

                         250
                  ....*....|....*....
gi 1002988495 245 PSDGLKSLEEFCRSLKQAI 263
Cdd:pfam00290 240 PEQGLARLEELAGEMKAAA 258
trpA PRK13125
tryptophan synthase subunit alpha; Provisional
 18-255 6.54e-33

tryptophan synthase subunit alpha; Provisional


Pssm-ID: 237286  Cd Length: 244  Bit Score: 120.15  E-value: 6.54e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988495  18 ALIPFITAGDPDLSTTAQALRILDQAgADLIELGVPYSDPLADGPVIqaaatRALNRGVKLEDVLEIVKNAQGEVKAPII 97
Cdd:PRK13125    5 GLVVYLTAGYPNVESFKEFIIGLVEL-VDILELGIPPKYPKYDGPVI-----RKSHRKVKGLDIWPLLEEVRKDVSVPII 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988495  98 LFTYYNPiYHRGIDVFLDQIKAAGVSGLVVPDLPL---EEAESLLQPAAAKGIEVILLVAPTSPPERIQAIARQSQGFIY 174
Cdd:PRK13125   79 LMTYLED-YVDSLDNFLNMARDVGADGVLFPDLLIdypDDLEKYVEIIKNKGLKPVFFTSPKFPDLLIHRLSKLSPLFIY 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988495 175 LvSVTGVTGMRNQVAtrVEELLDSIRS-VTDKPVGVGFGISDPTQALQVKNWGADAVIVGSAMVKRLADNSPSDGLKSLE 253
Cdd:PRK13125  158 Y-GLRPATGVPLPVS--VERNIKRVRNlVGNKYLVVGFGLDSPEDARDALSAGADGVVVGTAFIEELEKNGVESALNLLK 234


                  ..
gi 1002988495 254 EF 255
Cdd:PRK13125  235 KI 236
TIM_phosphate_binding cd04722
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ...
 22-234 6.68e-10

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: 57.21  E-value: 6.68e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988495  22 FITAGD--PDLSTTAQALRILDQAGADLIELGVPYSDPLADGPVIQAAATRALNrgvkledvleivknaqgEVKAPIILF 99
Cdd:cd04722     1 VILALLagGPSGDPVELAKAAAEAGADAIIVGTRSSDPEEAETDDKEVLKEVAA-----------------ETDLPLGVQ 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988495 100 TYYNPIYHRgIDVFLDQIKAAGVSGLVVPDLPLEEAESLLQP-----AAAKGIEVILLVAPTSPPERIQAIARQSqGFIY 174
Cdd:cd04722    64 LAINDAAAA-VDIAAAAARAAGADGVEIHGAVGYLAREDLELirelrEAVPDVKVVVKLSPTGELAAAAAEEAGV-DEVG 141

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988495 175 LVSVTGVTGMRnQVATRVEELLDSIRSVTDKPVGVGFGISDPTQALQVKNWGADAVIVGS 234
Cdd:cd04722   142 LGNGGGGGGGR-DAVPIADLLLILAKRGSKVPVIAGGGINDPEDAAEALALGADGVIVGS 200
NanE cd04729
N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to ...
 57-235 3.31e-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: 37.94  E-value: 3.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988495  57 PLADGPVIQAAATRALNRGVK------LEDVLEIvknaQGEVKAPIIlftyynPIYHRGI---DVFL-------DQIKAA 120
Cdd:cd04729    22 PLHSPEIMAAMALAAVQGGAVgirangVEDIRAI----RARVDLPII------GLIKRDYpdsEVYItptieevDALAAA 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988495 121 GVSglVV---------PD-LPLEEaesLLQPAAAKGieVILLVAPTSPPEriQAIARQSQGFiYLVSVT--GVTGMRNQV 188
Cdd:cd04729    92 GAD--IIaldatdrprPDgETLAE---LIKRIHEEY--NCLLMADISTLE--EALNAAKLGF-DIIGTTlsGYTEETAKT 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1002988495 189 ATRVEELLDSIRSVTDKPVGVGFGISDPTQALQVKNWGADAVIVGSA 235
Cdd:cd04729   162 EDPDFELLKELRKALGIPVIAEGRINSPEQAAKALELGADAVVVGSA 208
TIGR00007 TIGR00007
phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; This protein family ...
 156-255 6.76e-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: 36.79  E-value: 6.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988495 156 TSPPERIQAIARQSQGFIYLVSVTGVTGmrnqVATRVEELLDSIRSVTDKPVGVGFGISDPTQALQVKNWGADAVIVGSA 235
Cdd:TIGR00007  28 DDPVEAAKKWEEEGAERIHVVDLDGAKE----GGPVNLPVIKKIVRETGVPVQVGGGIRSLEDVEKLLDLGVDRVIIGTA 103

                          90       100
                  ....*....|....*....|
gi 1002988495 236 MVKRladnsPSDGLKSLEEF 255
Cdd:TIGR00007 104 AVEN-----PDLVKELLKEY 118
His_biosynth pfam00977
Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine ...
 194-247 6.89e-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: 37.07  E-value: 6.89e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988495 194 ELLDSIRSVTDKPVGVGFGISDPTQALQVKNWGADAVIVGSA------MVKRLADNSPSD 247
Cdd:pfam00977  63 DVVEEIAEEVFIPVQVGGGIRSLEDVERLLSAGADRVIIGTAavknpeLIKEAAEKFGSQ 122
HisA_HisF cd04723
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase (HisA) ...
 193-236 9.40e-03

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: 36.48  E-value: 9.40e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1002988495 193 EELLDSIRSVTDKPVGVGFGISDPTQALQVKNWGADAVIVGSAM 236
Cdd:cd04723   178 LELLERLAARADIPVIAAGGVRSVEDLELLKKLGASGALVASAL 221
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH