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Conserved domains on  [gi|2523679366|ref|WP_286162342|]
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MULTISPECIES: tryptophan synthase subunit alpha [unclassified Olsenella]

Protein Classification

beta/alpha barrel domain-containing protein( domain architecture ID 229392)

beta/alpha barrel domain-containing protein belongs to a large superfamily with a wide variety of enzymatic functions

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TIM super family cl21457
TIM-like beta/alpha barrel domains; A large family of domains similar to triose phosphate ...
 9-242 7.10e-32

TIM-like beta/alpha barrel domains; A large family of domains similar to triose phosphate isomerase (TIM) which, in general, share an eight beta/alpha closed barrel structure.


The actual alignment was detected with superfamily member cd04724:

Pssm-ID: 473867  Cd Length: 242  Bit Score: 116.81  E-value: 7.10e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2523679366   9 LILYLSNGYPTIESSIEMAKTYVDAGCDMIEMDFPSRNPFLEGEFIAGRMAKALENEPNYDKYMEGMAKARKLLpDTKFI 88
Cdd:cd04724     2 LIPYITAGDPDLETTLEILKALVEAGADIIELGIPFSDPVADGPVIQAASERALANGVTLKDVLELVKEIRKKN-TIPIV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2523679366  89 IMTYENTVLEIGVSRFVAFCKENGFEDIILvgPD-----GDTVKNELIDSGLKiscYVQF---NLPEEEVRQALE-SNGF 159
Cdd:cd04724    81 LMGYYNPILQYGLERFLRDAKEAGVDGLII--PDlppeeAEEFREAAKEYGLD---LIFLvapTTPDERIKKIAElASGF 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2523679366 160 TYMQAV-PAPGQATSQHPTLRSCIDYLRERGlKNPIYCGVGVHTPEDAQMVKEAgGDGIFVGSTILK-LHDNVPA-LIEK 236
Cdd:cd04724   156 IYYVSRtGVTGARTELPDDLKELIKRIRKYT-DLPIAVGFGISTPEQAAEVAKY-ADGVIVGSALVKiIEEGGEEeALEA 233


                  ....*.
gi 2523679366 237 IHEFKE 242
Cdd:cd04724   234 LKELAE 239
 
Name Accession Description Interval E-value
Tryptophan_synthase_alpha cd04724
Ttryptophan synthase (TRPS) alpha subunit (TSA). TPRS is a bifunctional tetrameric enzyme (2 ...
 9-242 7.10e-32

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: 116.81  E-value: 7.10e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2523679366   9 LILYLSNGYPTIESSIEMAKTYVDAGCDMIEMDFPSRNPFLEGEFIAGRMAKALENEPNYDKYMEGMAKARKLLpDTKFI 88
Cdd:cd04724     2 LIPYITAGDPDLETTLEILKALVEAGADIIELGIPFSDPVADGPVIQAASERALANGVTLKDVLELVKEIRKKN-TIPIV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2523679366  89 IMTYENTVLEIGVSRFVAFCKENGFEDIILvgPD-----GDTVKNELIDSGLKiscYVQF---NLPEEEVRQALE-SNGF 159
Cdd:cd04724    81 LMGYYNPILQYGLERFLRDAKEAGVDGLII--PDlppeeAEEFREAAKEYGLD---LIFLvapTTPDERIKKIAElASGF 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2523679366 160 TYMQAV-PAPGQATSQHPTLRSCIDYLRERGlKNPIYCGVGVHTPEDAQMVKEAgGDGIFVGSTILK-LHDNVPA-LIEK 236
Cdd:cd04724   156 IYYVSRtGVTGARTELPDDLKELIKRIRKYT-DLPIAVGFGISTPEQAAEVAKY-ADGVIVGSALVKiIEEGGEEeALEA 233


                  ....*.
gi 2523679366 237 IHEFKE 242
Cdd:cd04724   234 LKELAE 239
trpA TIGR00262
tryptophan synthase, alpha subunit; Tryptophan synthase catalyzes the last step in the ...
 3-240 5.87e-30

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: 112.05  E-value: 5.87e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2523679366   3 EAHKMKLILYLSNGYPTIESSIEMAKTYVDAGCDMIEMDFPSRNPFLEGEFIAGRMAKALENEPNYDKYMEGMAKARKLL 82
Cdd:TIGR00262   6 QRGEGAFIPFVTAGDPTLETSLEIIKTLIEAGADALELGVPFSDPLADGPTIQAADLRALRAGMTPEKCFELLKKVRQKH 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2523679366  83 PDTKFIIMTYENTVLEIGVSRFVAFCKENGFeDIILVgPD-----GDTVKNELIDSGLKISCYVQFNLPEEEVRQALE-S 156
Cdd:TIGR00262  86 PNIPIGLLTYYNLIFRKGVEEFYAKCKEVGV-DGVLV-ADlpleeSGDLVEAAKKHGVKPIFLVAPNADDERLKQIAEkS 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2523679366 157 NGFTYMQAVPAPGQATSQ-HPTLRSCIDYLRERGLKnPIYCGVGVHTPEDAQMVKEAGGDGIFVGSTILKL----HDNVP 231
Cdd:TIGR00262 164 QGFVYLVSRAGVTGARNRaASALNELVKRLKAYSAK-PVLVGFGISKPEQVKQAIDAGADGVIVGSAIVKIieenLNTPE 242


                  ....*....
gi 2523679366 232 ALIEKIHEF 240
Cdd:TIGR00262 243 KMLQALEEF 251
TrpA COG0159
Tryptophan synthase alpha chain [Amino acid transport and metabolism]; Tryptophan synthase ...
 9-240 4.70e-28

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: 107.46  E-value: 4.70e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2523679366   9 LILYLSNGYPTIESSIEMAKTYVDAGCDMIEMDFPSRNPFLEGEFIAGRMAKALENEPNYDKYMEGMAKARKlLPDTKFI 88
Cdd:COG0159    18 LIPYLTAGDPDLETTLEIIKALVEAGADIIELGIPFSDPVADGPVIQAASERALANGVTLDDVFELVREFRE-DPDTPLV 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2523679366  89 IMTYENTVLEIGVSRFVAFCKENGFEDIILvgPD-----GDTVKNELIDSGLKIscyVQF---NLPEEEVRQALE-SNGF 159
Cdd:COG0159    97 LMGYYNPVFRYGVERFAADAAEAGVDGLIV--PDlppeeAEELRAAADAHGLDL---IFLvapTTSDERIKKIAAaASGF 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2523679366 160 TYMQAVPAP-GQATSQHPTLRSCIDYLRERGlKNPIYCGVGVHTPEDAQMVKEAgGDGIFVGSTILKL--HDNVPALIEK 236
Cdd:COG0159   172 VYYVSVTGVtGARTAVSDDLAELVARIRAHT-DLPVAVGFGISTPEQAAEVAAY-ADGVIVGSALVKLieEGGDDEALEA 249


                  ....
gi 2523679366 237 IHEF 240
Cdd:COG0159   250 LAAF 253
Trp_syntA pfam00290
Tryptophan synthase alpha chain;
9-244 7.84e-28

Tryptophan synthase alpha chain;


Pssm-ID: 395227  Cd Length: 258  Bit Score: 106.63  E-value: 7.84e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2523679366   9 LILYLSNGYPTIESSIEMAKTYVDAGCDMIEMDFPSRNPFLEGEFIAGRMAKALENEPNYDKYMEGMAKARKLLPDTKFI 88
Cdd:pfam00290  12 FVPYVTAGDPDLEQSLEILKTLEKAGADAIELGVPFSDPLADGPTIQRANLRALASGVTLQSTLEMVREVRSKGVEVPIV 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2523679366  89 IMTYENTVLEIGVSRFVAFCKENGFEDIILvgPD-----GDTVKNELIDSGLKISCYVQFNLPEEEVRQALE-SNGFTYM 162
Cdd:pfam00290  92 LMTYYNPVLNYGIERFYALAAEAGVDGLIV--PDlppeeADSLRQAAKDHGLELVFLVAPTTSDERLKTVVEqAEGFVYL 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2523679366 163 QAVPApgqATSQHPTLRSCIDYLRERgLKN----PIYCGVGVHTPEDAQMVKeAGGDGIFVGSTILK-LHDNVPALIEKI 237
Cdd:pfam00290 170 VSRAG---VTGAENAVNAQVDELVER-LKKytavPVAVGFGISTPEHVKQAA-AGADGVIVGSALVRiIEEAADGPEQGL 244


                  ....*..
gi 2523679366 238 HEFKEKC 244
Cdd:pfam00290 245 ARLEELA 251
PLN02591 PLN02591
tryptophan synthase
 6-226 1.81e-20

tryptophan synthase


Pssm-ID: 178201  Cd Length: 250  Bit Score: 87.03  E-value: 1.81e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2523679366   6 KMKLILYLSNGYPTIESSIEMAKTYVDAGCDMIEMDFPSRNPFLEGEFIAGRMAKALENEPNYDKYMEGMakaRKLLPDT 85
Cdd:PLN02591    1 KVAFIPYITAGDPDLDTTAEALRLLDACGADVIELGVPYSDPLADGPVIQAAATRALEKGTTLDSVISML---KEVAPQL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2523679366  86 K--FIIMTYENTVLEIGVSRFVAFCKENGFEDiiLVGPD-----GDTVKNELIDSGLKISCYVQFNLPEEEVRQALE-SN 157
Cdd:PLN02591   78 ScpIVLFTYYNPILKRGIDKFMATIKEAGVHG--LVVPDlpleeTEALRAEAAKNGIELVLLTTPTTPTERMKAIAEaSE 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2523679366 158 GFTYMQAVPA-PGQATSQHPTLRSCIDYLRERGLKnPIYCGVGVHTPEDAQMVKEAGGDGIFVGSTILKL 226
Cdd:PLN02591  156 GFVYLVSSTGvTGARASVSGRVESLLQELKEVTDK-PVAVGFGISKPEHAKQIAGWGADGVIVGSAMVKA 224
 
Name Accession Description Interval E-value
Tryptophan_synthase_alpha cd04724
Ttryptophan synthase (TRPS) alpha subunit (TSA). TPRS is a bifunctional tetrameric enzyme (2 ...
 9-242 7.10e-32

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: 116.81  E-value: 7.10e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2523679366   9 LILYLSNGYPTIESSIEMAKTYVDAGCDMIEMDFPSRNPFLEGEFIAGRMAKALENEPNYDKYMEGMAKARKLLpDTKFI 88
Cdd:cd04724     2 LIPYITAGDPDLETTLEILKALVEAGADIIELGIPFSDPVADGPVIQAASERALANGVTLKDVLELVKEIRKKN-TIPIV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2523679366  89 IMTYENTVLEIGVSRFVAFCKENGFEDIILvgPD-----GDTVKNELIDSGLKiscYVQF---NLPEEEVRQALE-SNGF 159
Cdd:cd04724    81 LMGYYNPILQYGLERFLRDAKEAGVDGLII--PDlppeeAEEFREAAKEYGLD---LIFLvapTTPDERIKKIAElASGF 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2523679366 160 TYMQAV-PAPGQATSQHPTLRSCIDYLRERGlKNPIYCGVGVHTPEDAQMVKEAgGDGIFVGSTILK-LHDNVPA-LIEK 236
Cdd:cd04724   156 IYYVSRtGVTGARTELPDDLKELIKRIRKYT-DLPIAVGFGISTPEQAAEVAKY-ADGVIVGSALVKiIEEGGEEeALEA 233


                  ....*.
gi 2523679366 237 IHEFKE 242
Cdd:cd04724   234 LKELAE 239
trpA TIGR00262
tryptophan synthase, alpha subunit; Tryptophan synthase catalyzes the last step in the ...
 3-240 5.87e-30

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: 112.05  E-value: 5.87e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2523679366   3 EAHKMKLILYLSNGYPTIESSIEMAKTYVDAGCDMIEMDFPSRNPFLEGEFIAGRMAKALENEPNYDKYMEGMAKARKLL 82
Cdd:TIGR00262   6 QRGEGAFIPFVTAGDPTLETSLEIIKTLIEAGADALELGVPFSDPLADGPTIQAADLRALRAGMTPEKCFELLKKVRQKH 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2523679366  83 PDTKFIIMTYENTVLEIGVSRFVAFCKENGFeDIILVgPD-----GDTVKNELIDSGLKISCYVQFNLPEEEVRQALE-S 156
Cdd:TIGR00262  86 PNIPIGLLTYYNLIFRKGVEEFYAKCKEVGV-DGVLV-ADlpleeSGDLVEAAKKHGVKPIFLVAPNADDERLKQIAEkS 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2523679366 157 NGFTYMQAVPAPGQATSQ-HPTLRSCIDYLRERGLKnPIYCGVGVHTPEDAQMVKEAGGDGIFVGSTILKL----HDNVP 231
Cdd:TIGR00262 164 QGFVYLVSRAGVTGARNRaASALNELVKRLKAYSAK-PVLVGFGISKPEQVKQAIDAGADGVIVGSAIVKIieenLNTPE 242


                  ....*....
gi 2523679366 232 ALIEKIHEF 240
Cdd:TIGR00262 243 KMLQALEEF 251
TrpA COG0159
Tryptophan synthase alpha chain [Amino acid transport and metabolism]; Tryptophan synthase ...
 9-240 4.70e-28

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: 107.46  E-value: 4.70e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2523679366   9 LILYLSNGYPTIESSIEMAKTYVDAGCDMIEMDFPSRNPFLEGEFIAGRMAKALENEPNYDKYMEGMAKARKlLPDTKFI 88
Cdd:COG0159    18 LIPYLTAGDPDLETTLEIIKALVEAGADIIELGIPFSDPVADGPVIQAASERALANGVTLDDVFELVREFRE-DPDTPLV 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2523679366  89 IMTYENTVLEIGVSRFVAFCKENGFEDIILvgPD-----GDTVKNELIDSGLKIscyVQF---NLPEEEVRQALE-SNGF 159
Cdd:COG0159    97 LMGYYNPVFRYGVERFAADAAEAGVDGLIV--PDlppeeAEELRAAADAHGLDL---IFLvapTTSDERIKKIAAaASGF 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2523679366 160 TYMQAVPAP-GQATSQHPTLRSCIDYLRERGlKNPIYCGVGVHTPEDAQMVKEAgGDGIFVGSTILKL--HDNVPALIEK 236
Cdd:COG0159   172 VYYVSVTGVtGARTAVSDDLAELVARIRAHT-DLPVAVGFGISTPEQAAEVAAY-ADGVIVGSALVKLieEGGDDEALEA 249


                  ....
gi 2523679366 237 IHEF 240
Cdd:COG0159   250 LAAF 253
Trp_syntA pfam00290
Tryptophan synthase alpha chain;
9-244 7.84e-28

Tryptophan synthase alpha chain;


Pssm-ID: 395227  Cd Length: 258  Bit Score: 106.63  E-value: 7.84e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2523679366   9 LILYLSNGYPTIESSIEMAKTYVDAGCDMIEMDFPSRNPFLEGEFIAGRMAKALENEPNYDKYMEGMAKARKLLPDTKFI 88
Cdd:pfam00290  12 FVPYVTAGDPDLEQSLEILKTLEKAGADAIELGVPFSDPLADGPTIQRANLRALASGVTLQSTLEMVREVRSKGVEVPIV 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2523679366  89 IMTYENTVLEIGVSRFVAFCKENGFEDIILvgPD-----GDTVKNELIDSGLKISCYVQFNLPEEEVRQALE-SNGFTYM 162
Cdd:pfam00290  92 LMTYYNPVLNYGIERFYALAAEAGVDGLIV--PDlppeeADSLRQAAKDHGLELVFLVAPTTSDERLKTVVEqAEGFVYL 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2523679366 163 QAVPApgqATSQHPTLRSCIDYLRERgLKN----PIYCGVGVHTPEDAQMVKeAGGDGIFVGSTILK-LHDNVPALIEKI 237
Cdd:pfam00290 170 VSRAG---VTGAENAVNAQVDELVER-LKKytavPVAVGFGISTPEHVKQAA-AGADGVIVGSALVRiIEEAADGPEQGL 244


                  ....*..
gi 2523679366 238 HEFKEKC 244
Cdd:pfam00290 245 ARLEELA 251
PLN02591 PLN02591
tryptophan synthase
 6-226 1.81e-20

tryptophan synthase


Pssm-ID: 178201  Cd Length: 250  Bit Score: 87.03  E-value: 1.81e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2523679366   6 KMKLILYLSNGYPTIESSIEMAKTYVDAGCDMIEMDFPSRNPFLEGEFIAGRMAKALENEPNYDKYMEGMakaRKLLPDT 85
Cdd:PLN02591    1 KVAFIPYITAGDPDLDTTAEALRLLDACGADVIELGVPYSDPLADGPVIQAAATRALEKGTTLDSVISML---KEVAPQL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2523679366  86 K--FIIMTYENTVLEIGVSRFVAFCKENGFEDiiLVGPD-----GDTVKNELIDSGLKISCYVQFNLPEEEVRQALE-SN 157
Cdd:PLN02591   78 ScpIVLFTYYNPILKRGIDKFMATIKEAGVHG--LVVPDlpleeTEALRAEAAKNGIELVLLTTPTTPTERMKAIAEaSE 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2523679366 158 GFTYMQAVPA-PGQATSQHPTLRSCIDYLRERGLKnPIYCGVGVHTPEDAQMVKEAGGDGIFVGSTILKL 226
Cdd:PLN02591  156 GFVYLVSSTGvTGARASVSGRVESLLQELKEVTDK-PVAVGFGISKPEHAKQIAGWGADGVIVGSAMVKA 224
trpA CHL00200
tryptophan synthase alpha subunit; Provisional
 9-240 5.92e-14

tryptophan synthase alpha subunit; Provisional


Pssm-ID: 214394  Cd Length: 263  Bit Score: 69.41  E-value: 5.92e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2523679366   9 LILYLSNGYPTIESSIEMAKTYVDAGCDMIEMDFPSRNPFLEGEFIAGRMAKALENEPNYDKYMEGMakaRKLLPDTK-- 86
Cdd:CHL00200   17 LIPFITAGDPDIVITKKALKILDKKGADIIELGIPYSDPLADGPIIQEASNRALKQGINLNKILSIL---SEVNGEIKap 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2523679366  87 FIIMTYENTVLEIGVSRFVAFCKENGFEDIILvgPD-----GDTVKN-------ELIdsgLKISCYVQFNLPEEEVRQAl 154
Cdd:CHL00200   94 IVIFTYYNPVLHYGINKFIKKISQAGVKGLII--PDlpyeeSDYLISvcnlyniELI---LLIAPTSSKSRIQKIARAA- 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2523679366 155 esNGFTYMqaVPAPGqATSQHPTLRSCIDYLRE---RGLKNPIYCGVGVHTPEDAQMVKEAGGDGIFVGSTILK-LHDNV 230
Cdd:CHL00200  168 --PGCIYL--VSTTG-VTGLKTELDKKLKKLIEtikKMTNKPIILGFGISTSEQIKQIKGWNINGIVIGSACVQiLLGSS 242

                         250
                  ....*....|.
gi 2523679366 231 P-ALIEKIHEF 240
Cdd:CHL00200  243 PeKGLDQLSEF 253
Sbm COG2185
Methylmalonyl-CoA mutase, C-terminal domain/subunit (cobalamin-binding) [Lipid transport and ...
 143-239 3.39e-04

Methylmalonyl-CoA mutase, C-terminal domain/subunit (cobalamin-binding) [Lipid transport and metabolism];


Pssm-ID: 441788 [Multi-domain]  Cd Length: 134  Bit Score: 39.36  E-value: 3.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2523679366 143 FNLPEEEVRQALESN----GFTYMQAvpapgqatsQHPTL-RSCIDYLRERGLKN-PIYCGvGVHTPEDAQMVKEAGGDG 216
Cdd:COG2185    47 FQTPEEIVRAAIEEDadviGVSSLDG---------GHLELvPELIELLKEAGAGDiLVVVG-GVIPPEDIEALKAAGVDA 116

                          90       100
                  ....*....|....*....|....
gi 2523679366 217 IF-VGstilklhDNVPALIEKIHE 239
Cdd:COG2185   117 VFgPG-------TDLEEIIEDLLE 133
IGPS cd00331
Indole-3-glycerol phosphate synthase (IGPS); an enzyme in the tryptophan biosynthetic pathway, ...
 199-237 1.46e-03

Indole-3-glycerol phosphate synthase (IGPS); an enzyme in the tryptophan biosynthetic pathway, catalyzing the ring closure reaction of 1-(o-carboxyphenylamino)-1-deoxyribulose-5-phosphate (CdRP) to indole-3-glycerol phosphate (IGP), accompanied by the release of carbon dioxide and water. IGPS is active as a separate monomer in most organisms, but is also found fused to other enzymes as part of a bifunctional or multifunctional enzyme involved in tryptophan biosynthesis.


Pssm-ID: 238203  Cd Length: 217  Bit Score: 38.60  E-value: 1.46e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2523679366 199 GVHTPEDAQMVKEAGGDGIFVGSTILKlHDNVPALIEKI 237
Cdd:cd00331   180 GISTPEDVKRLAEAGADAVLIGESLMR-APDPGAALREL 217
pdxS cd04727
PdxS is a subunit of the pyridoxal 5'-phosphate (PLP) synthase, an important enzyme in ...
 199-225 1.58e-03

PdxS is a subunit of the pyridoxal 5'-phosphate (PLP) synthase, an important enzyme in deoxyxylulose 5-phosphate (DXP)-independent pathway for de novo biosynthesis of PLP, present in some eubacteria, in archaea, fungi, plants, plasmodia, and some metazoa. Together with PdxT, PdxS forms the PLP synthase, a heteromeric glutamine amidotransferase (GATase), whereby PdxT produces ammonia from glutamine and PdxS combines ammonia with five- and three-carbon phosphosugars to form PLP. PLP is the biologically active form of vitamin B6, an essential cofactor in many biochemical processes. PdxS subunits form two hexameric rings.


Pssm-ID: 240078  Cd Length: 283  Bit Score: 38.77  E-value: 1.58e-03
                          10        20
                  ....*....|....*....|....*..
gi 2523679366 199 GVHTPEDAQMVKEAGGDGIFVGSTILK 225
Cdd:cd04727   204 GVATPADAALMMQLGADGVFVGSGIFK 230
MM_CoA_mut_B12_BD cd02071
methylmalonyl CoA mutase B12 binding domain. This domain binds to B12 (adenosylcobamide), ...
 143-218 1.72e-03

methylmalonyl CoA mutase B12 binding domain. This domain binds to B12 (adenosylcobamide), which initiates the conversion of succinyl CoA and methylmalonyl CoA by forming an adenosyl radical, which then undergoes a rearrangement exchanging a hydrogen atom with a group attached to a neighboring carbon atom. This family is present in both mammals and bacteria. Bacterial members are heterodimers and involved in the fermentation of pyruvate to propionate. Mammalian members are homodimers and responsible for the conversion of odd-chain fatty acids and branched-chain amino acids via propionyl CoA to succinyl CoA for further degradation.


Pssm-ID: 239022 [Multi-domain]  Cd Length: 122  Bit Score: 37.19  E-value: 1.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2523679366 143 FNLPEEEVRQALESN----GFTYMQAvpapgqatsQHPTL-RSCIDYLRERGLKNPIYCGVGVHTPEDAQMVKEAGGDGI 217
Cdd:cd02071    36 RQTPEEIVEAAIQEDvdviGLSSLSG---------GHMTLfPEVIELLRELGAGDILVVGGGIIPPEDYELLKEMGVAEI 106


                  .
gi 2523679366 218 F 218
Cdd:cd02071   107 F 107
PRK04180 PRK04180
pyridoxal 5'-phosphate synthase lyase subunit PdxS;
199-225 2.31e-03

pyridoxal 5'-phosphate synthase lyase subunit PdxS;


Pssm-ID: 179769  Cd Length: 293  Bit Score: 38.58  E-value: 2.31e-03
                          10        20
                  ....*....|....*....|....*..
gi 2523679366 199 GVHTPEDAQMVKEAGGDGIFVGSTILK 225
Cdd:PRK04180  213 GIATPADAALMMQLGADGVFVGSGIFK 239
 
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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