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Conserved domains on  [gi|446459993|ref|WP_000537847|]
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MULTISPECIES: tryptophan synthase subunit alpha [Bacillus]

Protein Classification

tryptophan synthase subunit alpha( domain architecture ID 10793730)

tryptophan synthase (TRPS) alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate

CATH:  3.20.20.70
EC:  4.2.1.20
Gene Ontology:  GO:0004834|GO:0006568
PubMed:  2679363
SCOP:  4003071

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
trpA PRK13111
tryptophan synthase subunit alpha; Provisional
 4-254 1.16e-124

tryptophan synthase subunit alpha; Provisional


:

Pssm-ID: 237285  Cd Length: 258  Bit Score: 354.41  E-value: 1.16e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459993   4 EKIKAVFENGKKAFIPYVMGGDGGLEKLKERIRFLDEAGASIVEIGIPFSDPVADGPTIQRAGKRALDSGVTVKGIFQAL 83
Cdd:PRK13111   1 ALFAALKAEGRKALIPYITAGDPDLETSLEIIKALVEAGADIIELGIPFSDPVADGPVIQAASLRALAAGVTLADVFELV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459993  84 AEVR-KEVQIPFVLMTYVNPVLAFGKEQFIERCLEAGVDGIIVPDLPYEEQNIIAPLLREANIALIPLVTVTSPIERIEK 162
Cdd:PRK13111  81 REIReKDPTIPIVLMTYYNPIFQYGVERFAADAAEAGVDGLIIPDLPPEEAEELRAAAKKHGLDLIFLVAPTTTDERLKK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459993 163 ITSESEGFVYAVTVAGVTGVRQNFKEEIHSYLEKVKSHTHLPVVAGFGISTKEHVEEMITICDGVVVGSKVIELLEN--E 240
Cdd:PRK13111 161 IASHASGFVYYVSRAGVTGARSADAADLAELVARLKAHTDLPVAVGFGISTPEQAAAIAAVADGVIVGSALVKIIEEnpE 240

                        250
                 ....*....|....
gi 446459993 241 KREEICELIQATKQ 254
Cdd:PRK13111 241 ALEALAAFVKELKA 254
 
Name Accession Description Interval E-value
trpA PRK13111
tryptophan synthase subunit alpha; Provisional
 4-254 1.16e-124

tryptophan synthase subunit alpha; Provisional


Pssm-ID: 237285  Cd Length: 258  Bit Score: 354.41  E-value: 1.16e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459993   4 EKIKAVFENGKKAFIPYVMGGDGGLEKLKERIRFLDEAGASIVEIGIPFSDPVADGPTIQRAGKRALDSGVTVKGIFQAL 83
Cdd:PRK13111   1 ALFAALKAEGRKALIPYITAGDPDLETSLEIIKALVEAGADIIELGIPFSDPVADGPVIQAASLRALAAGVTLADVFELV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459993  84 AEVR-KEVQIPFVLMTYVNPVLAFGKEQFIERCLEAGVDGIIVPDLPYEEQNIIAPLLREANIALIPLVTVTSPIERIEK 162
Cdd:PRK13111  81 REIReKDPTIPIVLMTYYNPIFQYGVERFAADAAEAGVDGLIIPDLPPEEAEELRAAAKKHGLDLIFLVAPTTTDERLKK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459993 163 ITSESEGFVYAVTVAGVTGVRQNFKEEIHSYLEKVKSHTHLPVVAGFGISTKEHVEEMITICDGVVVGSKVIELLEN--E 240
Cdd:PRK13111 161 IASHASGFVYYVSRAGVTGARSADAADLAELVARLKAHTDLPVAVGFGISTPEQAAAIAAVADGVIVGSALVKIIEEnpE 240

                        250
                 ....*....|....
gi 446459993 241 KREEICELIQATKQ 254
Cdd:PRK13111 241 ALEALAAFVKELKA 254
TrpA COG0159
Tryptophan synthase alpha chain [Amino acid transport and metabolism]; Tryptophan synthase ...
 4-251 1.93e-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: 348.98  E-value: 1.93e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459993   4 EKIKAVFE----NGKKAFIPYVMGGDGGLEKLKERIRFLDEAGASIVEIGIPFSDPVADGPTIQRAGKRALDSGVTVKGI 79
Cdd:COG0159    1 SRIDAAFAalkaEGRKALIPYLTAGDPDLETTLEIIKALVEAGADIIELGIPFSDPVADGPVIQAASERALANGVTLDDV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459993  80 FQALAEVRKEVQIPFVLMTYVNPVLAFGKEQFIERCLEAGVDGIIVPDLPYEEQNIIAPLLREANIALIPLVTVTSPIER 159
Cdd:COG0159   81 FELVREFREDPDTPLVLMGYYNPVFRYGVERFAADAAEAGVDGLIVPDLPPEEAEELRAAADAHGLDLIFLVAPTTSDER 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459993 160 IEKITSESEGFVYAVTVAGVTGVRQNFKEEIHSYLEKVKSHTHLPVVAGFGISTKEHVEEMITICDGVVVGSKVIELLEN 239
Cdd:COG0159  161 IKKIAAAASGFVYYVSVTGVTGARTAVSDDLAELVARIRAHTDLPVAVGFGISTPEQAAEVAAYADGVIVGSALVKLIEE 240

                        250
                 ....*....|..
gi 446459993 240 EKREEICELIQA 251
Cdd:COG0159  241 GGDDEALEALAA 252
Tryptophan_synthase_alpha cd04724
Ttryptophan synthase (TRPS) alpha subunit (TSA). TPRS is a bifunctional tetrameric enzyme (2 ...
 16-253 4.04e-116

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: 332.52  E-value: 4.04e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459993  16 AFIPYVMGGDGGLEKLKERIRFLDEAGASIVEIGIPFSDPVADGPTIQRAGKRALDSGVTVKGIFQALAEVRKEVQIPFV 95
Cdd:cd04724    1 ALIPYITAGDPDLETTLEILKALVEAGADIIELGIPFSDPVADGPVIQAASERALANGVTLKDVLELVKEIRKKNTIPIV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459993  96 LMTYVNPVLAFGKEQFIERCLEAGVDGIIVPDLPYEEQNIIAPLLREANIALIPLVTVTSPIERIEKITSESEGFVYAVT 175
Cdd:cd04724   81 LMGYYNPILQYGLERFLRDAKEAGVDGLIIPDLPPEEAEEFREAAKEYGLDLIFLVAPTTPDERIKKIAELASGFIYYVS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459993 176 VAGVTGVRQNFKEEIHSYLEKVKSHTHLPVVAGFGISTKEHVEEMITICDGVVVGSKVIELLEN----EKREEICELIQA 251
Cdd:cd04724  161 RTGVTGARTELPDDLKELIKRIRKYTDLPIAVGFGISTPEQAAEVAKYADGVIVGSALVKIIEEggeeEALEALKELAES 240


                 ..
gi 446459993 252 TK 253
Cdd:cd04724  241 LK 242
Trp_syntA pfam00290
Tryptophan synthase alpha chain;
11-250 6.59e-99

Tryptophan synthase alpha chain;


Pssm-ID: 395227  Cd Length: 258  Bit Score: 289.21  E-value: 6.59e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459993   11 ENGKKAFIPYVMGGDGGLEKLKERIRFLDEAGASIVEIGIPFSDPVADGPTIQRAGKRALDSGVTVKGIFQALAEVR-KE 89
Cdd:pfam00290   6 AENRAAFVPYVTAGDPDLEQSLEILKTLEKAGADAIELGVPFSDPLADGPTIQRANLRALASGVTLQSTLEMVREVRsKG 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459993   90 VQIPFVLMTYVNPVLAFGKEQFIERCLEAGVDGIIVPDLPYEEQNIIAPLLREANIALIPLVTVTSPIERIEKITSESEG 169
Cdd:pfam00290  86 VEVPIVLMTYYNPVLNYGIERFYALAAEAGVDGLIVPDLPPEEADSLRQAAKDHGLELVFLVAPTTSDERLKTVVEQAEG 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459993  170 FVYAVTVAGVTGVRQNFKEEIHSYLEKVKSHTHLPVVAGFGISTKEHVEEMITICDGVVVGSKVIELLENEKREEICELI 249
Cdd:pfam00290 166 FVYLVSRAGVTGAENAVNAQVDELVERLKKYTAVPVAVGFGISTPEHVKQAAAGADGVIVGSALVRIIEEAADGPEQGLA 245


                  .
gi 446459993  250 Q 250
Cdd:pfam00290 246 R 246
trpA TIGR00262
tryptophan synthase, alpha subunit; Tryptophan synthase catalyzes the last step in the ...
 13-253 2.13e-84

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: 252.65  E-value: 2.13e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459993   13 GKKAFIPYVMGGDGGLEKLKERIRFLDEAGASIVEIGIPFSDPVADGPTIQRAGKRALDSGVTVKGIFQALAEVRKE-VQ 91
Cdd:TIGR00262   8 GEGAFIPFVTAGDPTLETSLEIIKTLIEAGADALELGVPFSDPLADGPTIQAADLRALRAGMTPEKCFELLKKVRQKhPN 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459993   92 IPFVLMTYVNPVLAFGKEQFIERCLEAGVDGIIVPDLPYEEQNiiaPLLREA---NIALIPLVTVTSPIERIEKITSESE 168
Cdd:TIGR00262  88 IPIGLLTYYNLIFRKGVEEFYAKCKEVGVDGVLVADLPLEESG---DLVEAAkkhGVKPIFLVAPNADDERLKQIAEKSQ 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459993  169 GFVYAVTVAGVTGVRQNFKEEIHSYLEKVKSHTHLPVVAGFGISTKEHVEEMITI-CDGVVVGS---KVIE-LLENEKR- 242
Cdd:TIGR00262 165 GFVYLVSRAGVTGARNRAASALNELVKRLKAYSAKPVLVGFGISKPEQVKQAIDAgADGVIVGSaivKIIEeNLNTPEKm 244

                         250
                  ....*....|..
gi 446459993  243 -EEICELIQATK 253
Cdd:TIGR00262 245 lQALEEFVQNLK 256
 
Name Accession Description Interval E-value
trpA PRK13111
tryptophan synthase subunit alpha; Provisional
 4-254 1.16e-124

tryptophan synthase subunit alpha; Provisional


Pssm-ID: 237285  Cd Length: 258  Bit Score: 354.41  E-value: 1.16e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459993   4 EKIKAVFENGKKAFIPYVMGGDGGLEKLKERIRFLDEAGASIVEIGIPFSDPVADGPTIQRAGKRALDSGVTVKGIFQAL 83
Cdd:PRK13111   1 ALFAALKAEGRKALIPYITAGDPDLETSLEIIKALVEAGADIIELGIPFSDPVADGPVIQAASLRALAAGVTLADVFELV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459993  84 AEVR-KEVQIPFVLMTYVNPVLAFGKEQFIERCLEAGVDGIIVPDLPYEEQNIIAPLLREANIALIPLVTVTSPIERIEK 162
Cdd:PRK13111  81 REIReKDPTIPIVLMTYYNPIFQYGVERFAADAAEAGVDGLIIPDLPPEEAEELRAAAKKHGLDLIFLVAPTTTDERLKK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459993 163 ITSESEGFVYAVTVAGVTGVRQNFKEEIHSYLEKVKSHTHLPVVAGFGISTKEHVEEMITICDGVVVGSKVIELLEN--E 240
Cdd:PRK13111 161 IASHASGFVYYVSRAGVTGARSADAADLAELVARLKAHTDLPVAVGFGISTPEQAAAIAAVADGVIVGSALVKIIEEnpE 240

                        250
                 ....*....|....
gi 446459993 241 KREEICELIQATKQ 254
Cdd:PRK13111 241 ALEALAAFVKELKA 254
TrpA COG0159
Tryptophan synthase alpha chain [Amino acid transport and metabolism]; Tryptophan synthase ...
 4-251 1.93e-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: 348.98  E-value: 1.93e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459993   4 EKIKAVFE----NGKKAFIPYVMGGDGGLEKLKERIRFLDEAGASIVEIGIPFSDPVADGPTIQRAGKRALDSGVTVKGI 79
Cdd:COG0159    1 SRIDAAFAalkaEGRKALIPYLTAGDPDLETTLEIIKALVEAGADIIELGIPFSDPVADGPVIQAASERALANGVTLDDV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459993  80 FQALAEVRKEVQIPFVLMTYVNPVLAFGKEQFIERCLEAGVDGIIVPDLPYEEQNIIAPLLREANIALIPLVTVTSPIER 159
Cdd:COG0159   81 FELVREFREDPDTPLVLMGYYNPVFRYGVERFAADAAEAGVDGLIVPDLPPEEAEELRAAADAHGLDLIFLVAPTTSDER 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459993 160 IEKITSESEGFVYAVTVAGVTGVRQNFKEEIHSYLEKVKSHTHLPVVAGFGISTKEHVEEMITICDGVVVGSKVIELLEN 239
Cdd:COG0159  161 IKKIAAAASGFVYYVSVTGVTGARTAVSDDLAELVARIRAHTDLPVAVGFGISTPEQAAEVAAYADGVIVGSALVKLIEE 240

                        250
                 ....*....|..
gi 446459993 240 EKREEICELIQA 251
Cdd:COG0159  241 GGDDEALEALAA 252
Tryptophan_synthase_alpha cd04724
Ttryptophan synthase (TRPS) alpha subunit (TSA). TPRS is a bifunctional tetrameric enzyme (2 ...
 16-253 4.04e-116

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: 332.52  E-value: 4.04e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459993  16 AFIPYVMGGDGGLEKLKERIRFLDEAGASIVEIGIPFSDPVADGPTIQRAGKRALDSGVTVKGIFQALAEVRKEVQIPFV 95
Cdd:cd04724    1 ALIPYITAGDPDLETTLEILKALVEAGADIIELGIPFSDPVADGPVIQAASERALANGVTLKDVLELVKEIRKKNTIPIV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459993  96 LMTYVNPVLAFGKEQFIERCLEAGVDGIIVPDLPYEEQNIIAPLLREANIALIPLVTVTSPIERIEKITSESEGFVYAVT 175
Cdd:cd04724   81 LMGYYNPILQYGLERFLRDAKEAGVDGLIIPDLPPEEAEEFREAAKEYGLDLIFLVAPTTPDERIKKIAELASGFIYYVS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459993 176 VAGVTGVRQNFKEEIHSYLEKVKSHTHLPVVAGFGISTKEHVEEMITICDGVVVGSKVIELLEN----EKREEICELIQA 251
Cdd:cd04724  161 RTGVTGARTELPDDLKELIKRIRKYTDLPIAVGFGISTPEQAAEVAKYADGVIVGSALVKIIEEggeeEALEALKELAES 240


                 ..
gi 446459993 252 TK 253
Cdd:cd04724  241 LK 242
Trp_syntA pfam00290
Tryptophan synthase alpha chain;
11-250 6.59e-99

Tryptophan synthase alpha chain;


Pssm-ID: 395227  Cd Length: 258  Bit Score: 289.21  E-value: 6.59e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459993   11 ENGKKAFIPYVMGGDGGLEKLKERIRFLDEAGASIVEIGIPFSDPVADGPTIQRAGKRALDSGVTVKGIFQALAEVR-KE 89
Cdd:pfam00290   6 AENRAAFVPYVTAGDPDLEQSLEILKTLEKAGADAIELGVPFSDPLADGPTIQRANLRALASGVTLQSTLEMVREVRsKG 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459993   90 VQIPFVLMTYVNPVLAFGKEQFIERCLEAGVDGIIVPDLPYEEQNIIAPLLREANIALIPLVTVTSPIERIEKITSESEG 169
Cdd:pfam00290  86 VEVPIVLMTYYNPVLNYGIERFYALAAEAGVDGLIVPDLPPEEADSLRQAAKDHGLELVFLVAPTTSDERLKTVVEQAEG 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459993  170 FVYAVTVAGVTGVRQNFKEEIHSYLEKVKSHTHLPVVAGFGISTKEHVEEMITICDGVVVGSKVIELLENEKREEICELI 249
Cdd:pfam00290 166 FVYLVSRAGVTGAENAVNAQVDELVERLKKYTAVPVAVGFGISTPEHVKQAAAGADGVIVGSALVRIIEEAADGPEQGLA 245


                  .
gi 446459993  250 Q 250
Cdd:pfam00290 246 R 246
trpA TIGR00262
tryptophan synthase, alpha subunit; Tryptophan synthase catalyzes the last step in the ...
 13-253 2.13e-84

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: 252.65  E-value: 2.13e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459993   13 GKKAFIPYVMGGDGGLEKLKERIRFLDEAGASIVEIGIPFSDPVADGPTIQRAGKRALDSGVTVKGIFQALAEVRKE-VQ 91
Cdd:TIGR00262   8 GEGAFIPFVTAGDPTLETSLEIIKTLIEAGADALELGVPFSDPLADGPTIQAADLRALRAGMTPEKCFELLKKVRQKhPN 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459993   92 IPFVLMTYVNPVLAFGKEQFIERCLEAGVDGIIVPDLPYEEQNiiaPLLREA---NIALIPLVTVTSPIERIEKITSESE 168
Cdd:TIGR00262  88 IPIGLLTYYNLIFRKGVEEFYAKCKEVGVDGVLVADLPLEESG---DLVEAAkkhGVKPIFLVAPNADDERLKQIAEKSQ 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459993  169 GFVYAVTVAGVTGVRQNFKEEIHSYLEKVKSHTHLPVVAGFGISTKEHVEEMITI-CDGVVVGS---KVIE-LLENEKR- 242
Cdd:TIGR00262 165 GFVYLVSRAGVTGARNRAASALNELVKRLKAYSAKPVLVGFGISKPEQVKQAIDAgADGVIVGSaivKIIEeNLNTPEKm 244

                         250
                  ....*....|..
gi 446459993  243 -EEICELIQATK 253
Cdd:TIGR00262 245 lQALEEFVQNLK 256
PLN02591 PLN02591
tryptophan synthase
 14-237 5.56e-73

tryptophan synthase


Pssm-ID: 178201  Cd Length: 250  Bit Score: 223.39  E-value: 5.56e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459993  14 KKAFIPYVMGGDGGLEKLKERIRFLDEAGASIVEIGIPFSDPVADGPTIQRAGKRALDSGVTVKGIFQALAEVRKEVQIP 93
Cdd:PLN02591   1 KVAFIPYITAGDPDLDTTAEALRLLDACGADVIELGVPYSDPLADGPVIQAAATRALEKGTTLDSVISMLKEVAPQLSCP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459993  94 FVLMTYVNPVLAFGKEQFIERCLEAGVDGIIVPDLPYEEQNIIAPLLREANIALIPLVTVTSPIERIEKITSESEGFVYA 173
Cdd:PLN02591  81 IVLFTYYNPILKRGIDKFMATIKEAGVHGLVVPDLPLEETEALRAEAAKNGIELVLLTTPTTPTERMKAIAEASEGFVYL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446459993 174 VTVAGVTGVRQNFKEEIHSYLEKVKSHTHLPVVAGFGISTKEHVEEMITI-CDGVVVGSKVIELL 237
Cdd:PLN02591 161 VSSTGVTGARASVSGRVESLLQELKEVTDKPVAVGFGISKPEHAKQIAGWgADGVIVGSAMVKAL 225
trpA CHL00200
tryptophan synthase alpha subunit; Provisional
 6-253 2.80e-71

tryptophan synthase alpha subunit; Provisional


Pssm-ID: 214394  Cd Length: 263  Bit Score: 219.25  E-value: 2.80e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459993   6 IKAVFENGKK--AFIPYVMGGDGGLEKLKERIRFLDEAGASIVEIGIPFSDPVADGPTIQRAGKRALDSGVTVKGIFQAL 83
Cdd:CHL00200   4 ISNVFEKLDKqcALIPFITAGDPDIVITKKALKILDKKGADIIELGIPYSDPLADGPIIQEASNRALKQGINLNKILSIL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459993  84 AEVRKEVQIPFVLMTYVNPVLAFGKEQFIERCLEAGVDGIIVPDLPYEEQNIIAPLLREANIALIPLVTVTSPIERIEKI 163
Cdd:CHL00200  84 SEVNGEIKAPIVIFTYYNPVLHYGINKFIKKISQAGVKGLIIPDLPYEESDYLISVCNLYNIELILLIAPTSSKSRIQKI 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459993 164 TSESEGFVYAVTVAGVTGVRQNFKEEIHSYLEKVKSHTHLPVVAGFGISTKEHVEEMITI-CDGVVVGSKVIELLENEKR 242
Cdd:CHL00200 164 ARAAPGCIYLVSTTGVTGLKTELDKKLKKLIETIKKMTNKPIILGFGISTSEQIKQIKGWnINGIVIGSACVQILLGSSP 243

                        250
                 ....*....|....*
gi 446459993 243 EE----ICELIQATK 253
Cdd:CHL00200 244 EKgldqLSEFCKVAK 258
trpA PRK13125
tryptophan synthase subunit alpha; Provisional
 14-254 6.04e-20

tryptophan synthase subunit alpha; Provisional


Pssm-ID: 237286  Cd Length: 244  Bit Score: 85.86  E-value: 6.04e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459993  14 KKAFIPYVMGGDGGLEKLKERIRFLDEAgASIVEIGIPFSDPVADGPTIQRAGKraldsGVTVKGIFQALAEVRKEVQIP 93
Cdd:PRK13125   3 RPGLVVYLTAGYPNVESFKEFIIGLVEL-VDILELGIPPKYPKYDGPVIRKSHR-----KVKGLDIWPLLEEVRKDVSVP 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459993  94 FVLMTYVNPVLAfGKEQFIERCLEAGVDGIIVPDLPY---EEQNIIAPLLREANIALIPLVTVTSPIERIEKITSESEGF 170
Cdd:PRK13125  77 IILMTYLEDYVD-SLDNFLNMARDVGADGVLFPDLLIdypDDLEKYVEIIKNKGLKPVFFTSPKFPDLLIHRLSKLSPLF 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459993 171 VYaVTVAGVTGVrqnfkeEIHSYLEK-VKSHTHL----PVVAGFGISTKEHVEEMITI-CDGVVVGSKVIELLENEKREE 244
Cdd:PRK13125 156 IY-YGLRPATGV------PLPVSVERnIKRVRNLvgnkYLVVGFGLDSPEDARDALSAgADGVVVGTAFIEELEKNGVES 228

                        250
                 ....*....|
gi 446459993 245 ICELIQATKQ 254
Cdd:PRK13125 229 ALNLLKKIRG 238
TIM_phosphate_binding cd04722
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ...
 17-231 2.73e-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: 52.59  E-value: 2.73e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459993  17 FIPYVMGGdGGLEKLKERIRFLDEAGASIVEIGIPFSDPVADGPTIQRAgkraldsgvtvkgifqaLAEVRKEVQIPFVL 96
Cdd:cd04722    1 VILALLAG-GPSGDPVELAKAAAEAGADAIIVGTRSSDPEEAETDDKEV-----------------LKEVAAETDLPLGV 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459993  97 MTYVNPVLAFGKEQFiERCLEAGVDGIIVPDLPYEEQNIIAPLLREANIAL--IPLVTVTSPIERIEKITSESEG--FVY 172
Cdd:cd04722   63 QLAINDAAAAVDIAA-AAARAAGADGVEIHGAVGYLAREDLELIRELREAVpdVKVVVKLSPTGELAAAAAEEAGvdEVG 141

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459993 173 AVTVAGVTGvRQNFKEEIHSYLEKVKSHTHLPVVAGFGISTKEHVEEMI-TICDGVVVGS 231
Cdd:cd04722  142 LGNGGGGGG-GRDAVPIADLLLILAKRGSKVPVIAGGGINDPEDAAEALaLGADGVIVGS 200
NPD_like cd04730
2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes ...
 75-231 1.67e-03

2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes oxidative denitrification of nitroalkanes to their corresponding carbonyl compounds and nitrites. NDP is a member of the NAD(P)H-dependent flavin oxidoreductase family that reduce a range of alternative electron acceptors. Most use FAD/FMN as a cofactor and NAD(P)H as electron donor. Some contain 4Fe-4S cluster to transfer electron from FAD to FMN.


Pssm-ID: 240081 [Multi-domain]  Cd Length: 236  Bit Score: 38.62  E-value: 1.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459993  75 TVKGIFQALAEVRKEVQIPF-V-LMTYVNPVLAfgkEQFIERCLEAGVDGIIV---PDLPYEEQniiaplLREANIALIP 149
Cdd:cd04730   37 TPEALRAEIRKIRALTDKPFgVnLLVPSSNPDF---EALLEVALEEGVPVVSFsfgPPAEVVER------LKAAGIKVIP 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459993 150 lvTVTSPIErieKITSESEGfVYAVTVAGVT--GVRQNFKEEIHSYLEKVKSHTHLPVVAGFGISTKEHVEEMITI-CDG 226
Cdd:cd04730  108 --TVTSVEE---ARKAEAAG-ADALVAQGAEagGHRGTFDIGTFALVPEVRDAVDIPVIAAGGIADGRGIAAALALgADG 181


                 ....*
gi 446459993 227 VVVGS 231
Cdd:cd04730  182 VQMGT 186
BtpA COG0434
Membrane biogenesis protein, BtpA/SgcQ family [Cell wall/membrane/envelope biogenesis];
194-231 2.15e-03

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


Pssm-ID: 440203  Cd Length: 268  Bit Score: 38.61  E-value: 2.15e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 446459993 194 LEKVKSHT-HLPVVAGFGIsTKEHVEEMITICDGVVVGS 231
Cdd:COG0434  203 LKRVKEAApDVPVLVGSGV-TPENVAELLSVADGAIVGS 240
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
 80-125 9.64e-03

CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator Spo0F [Signal transduction mechanisms];


Pssm-ID: 440547 [Multi-domain]  Cd Length: 128  Bit Score: 35.21  E-value: 9.64e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 446459993  80 FQALAEVRKEVQ---IPFVLMTyvnpvlAFGKEQFIERCLEAGVDGIIV 125
Cdd:COG0784   65 LELLRRIRALPRlpdIPIIALT------AYADEEDRERALEAGADDYLT 107
 
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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