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Conserved domains on  [gi|1929576803|gb|QOZ67581|]
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aldehyde dehydrogenase [Bradyrhizobium arachidis]

Protein Classification

thiamine pyrophosphate-dependent enzyme; thiamine pyrophosphate-dependent dehydrogenase E1 component subunit alpha( domain architecture ID 10130131)

thiamine pyrophosphate (TPP)-dependent enzyme uses thiamine pyrophosphate as a cofactor to catalyze various reactions including reversible decarboxylation; thiamine pyrophosphate-dependent dehydrogenase E1 component subunit alpha is part of the E1 component of a multi-enzyme dehydrogenase complex such as branched-chain alpha-keto acid dehydrogenase, which catalyzes the overall conversion of alpha-keto acids to acyl-CoA and carbon dioxide

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TPP_ComE cd03372
Thiamine pyrophosphate (TPP) family, ComE subfamily, TPP-binding module; composed of proteins ...
 9-191 1.41e-76

Thiamine pyrophosphate (TPP) family, ComE subfamily, TPP-binding module; composed of proteins similar to Methanococcus jannaschii sulfopyruvate decarboxylase beta subunit (ComE). M. jannaschii sulfopyruvate decarboxylase (ComDE) is a dodecamer of six alpha (D) subunits and six (E) beta subunits, which catalyzes the decarboxylation of sulfopyruvic acid to sulfoacetaldehyde in the coenzyme M pathway. ComDE requires TPP and divalent metal cation cofactors.


:

Pssm-ID: 239469 [Multi-domain]  Cd Length: 179  Bit Score: 227.17  E-value: 1.41e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929576803   9 RRQVVATLLANRKDVIAIGGLGASTNDMCAAGDHARNFYLWGGMGGAAMIGLGLALAQPKlPVLVITGDGEMLMGMGSLA 88
Cdd:cd03372     1 RRDAIKTLIADLKDELVVSNIGFPSKELYAAGDRPLNFYMLGSMGLASSIGLGLALAQPR-KVIVIDGDGSLLMNLGALA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929576803  89 TIGLQKPANLSIVVLDNEAYGETGGQTSHTSAAADLVGVARACGIKDSRAVttmAEVEAFAKAVHDVSAGPRFVNVKIDN 168
Cdd:cd03372    80 TIAAEKPKNLIIVVLDNGAYGSTGNQPTHAGKKTDLEAVAKACGLDNVATV---ASEEAFEKAVEQALDGPSFIHVKIKP 156

                         170       180
                  ....*....|....*....|...
gi 1929576803 169 ANLERILPTRDGTYILNRIRGDL 191
Cdd:cd03372   157 GNTDVPNIPRDPVEIKNRFMEAL 179
 
Name Accession Description Interval E-value
TPP_ComE cd03372
Thiamine pyrophosphate (TPP) family, ComE subfamily, TPP-binding module; composed of proteins ...
 9-191 1.41e-76

Thiamine pyrophosphate (TPP) family, ComE subfamily, TPP-binding module; composed of proteins similar to Methanococcus jannaschii sulfopyruvate decarboxylase beta subunit (ComE). M. jannaschii sulfopyruvate decarboxylase (ComDE) is a dodecamer of six alpha (D) subunits and six (E) beta subunits, which catalyzes the decarboxylation of sulfopyruvic acid to sulfoacetaldehyde in the coenzyme M pathway. ComDE requires TPP and divalent metal cation cofactors.


Pssm-ID: 239469 [Multi-domain]  Cd Length: 179  Bit Score: 227.17  E-value: 1.41e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929576803   9 RRQVVATLLANRKDVIAIGGLGASTNDMCAAGDHARNFYLWGGMGGAAMIGLGLALAQPKlPVLVITGDGEMLMGMGSLA 88
Cdd:cd03372     1 RRDAIKTLIADLKDELVVSNIGFPSKELYAAGDRPLNFYMLGSMGLASSIGLGLALAQPR-KVIVIDGDGSLLMNLGALA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929576803  89 TIGLQKPANLSIVVLDNEAYGETGGQTSHTSAAADLVGVARACGIKDSRAVttmAEVEAFAKAVHDVSAGPRFVNVKIDN 168
Cdd:cd03372    80 TIAAEKPKNLIIVVLDNGAYGSTGNQPTHAGKKTDLEAVAKACGLDNVATV---ASEEAFEKAVEQALDGPSFIHVKIKP 156

                         170       180
                  ....*....|....*....|...
gi 1929576803 169 ANLERILPTRDGTYILNRIRGDL 191
Cdd:cd03372   157 GNTDVPNIPRDPVEIKNRFMEAL 179
PRK06163 PRK06163
hypothetical protein; Provisional
 1-196 3.47e-33

hypothetical protein; Provisional


Pssm-ID: 235721 [Multi-domain]  Cd Length: 202  Bit Score: 117.62  E-value: 3.47e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929576803   1 MSKANLLDRrqVVATLlanRKDVIAIGGLGASTNDMCAAGDHARNFYLWGGMGGAAMIGLGLALAQPKLPVLVITGDGEM 80
Cdd:PRK06163   13 MNRFDLTCR--LVAKL---KDEEAVIGGIGNTNFDLWAAGQRPQNFYMLGSMGLAFPIALGVALAQPKRRVIALEGDGSL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929576803  81 LMGMGSLATIGLQKPANLSIVVLDNEAYGETGGQTSHTSAAADLVGVARACGIKDSRAVTTMAEVEAFAKAVHDvSAGPR 160
Cdd:PRK06163   88 LMQLGALGTIAALAPKNLTIIVMDNGVYQITGGQPTLTSQTVDVVAIARGAGLENSHWAADEAHFEALVDQALS-GPGPS 166

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1929576803 161 FVNVKIDNAnLERILPTRDGTYILNRIRGDLGF-QPI 196
Cdd:PRK06163  167 FIAVRIDDK-PGVGTTERDPAQIRERFMQGLGVrEPI 202
Ppyr-DeCO2ase TIGR03297
phosphonopyruvate decarboxylase; This family consists of examples of phosphonopyruvate an ...
 4-166 6.61e-29

phosphonopyruvate decarboxylase; This family consists of examples of phosphonopyruvate an decarboxylase enzyme that produces phosphonoacetaldehyde (Pald), the second step in the biosynthesis phosphonate-containing compounds. Since the preceding enzymate step, PEP phosphomutase (AepX, TIGR02320) favors the substrate PEP energetically, the decarboxylase is required to drive the reaction in the direction of phosphonate production. Pald is a precursor of natural products including antibiotics like bialaphos and phosphonothricin in Streptomyces species, phosphonate-modified molecules such as the polysaccharide B of Bacteroides fragilis, the phosphonolipids of Tetrahymena pyroformis, the glycosylinositolphospholipids of Trypanosoma cruzi. This gene generally occurs in prokaryotic organisms adjacent to the gene for AepX. Most often an aminotansferase (aepZ) is also present which leads to the production of the most common phosphonate compound, 2-aminoethylphosphonate (AEP).


Pssm-ID: 274508 [Multi-domain]  Cd Length: 361  Bit Score: 110.14  E-value: 6.61e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929576803   4 ANLLDRRQVVATLLANRKDVIAI-GGLGASTNDMCAAGD-----HARNFYLWGGMGGAAMIGLGLALAQPKLPVLVITGD 77
Cdd:TIGR03297 169 ATLMTREEAIAAILDHLPDNTVIvSTTGKTSRELYELRDrigqgHARDFLTVGSMGHASQIALGLALARPDQRVVCLDGD 248

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929576803  78 GEMLMGMGSLATIGLQKPANLSIVVLDNEAYGETGGQTSHtSAAADLVGVARACGIKDSRAVTTMAEVEafaKAVHDVSA 157
Cdd:TIGR03297 249 GAALMHMGGLATIGTQGPANLIHVLFNNGAHDSVGGQPTV-SQHLDFAQIAKACGYAKVYEVSTLEELE---TALTAASS 324

                         170
                  ....*....|.
gi 1929576803 158 --GPRFVNVKI 166
Cdd:TIGR03297 325 anGPRLIEVKV 335
TPP_enzyme_C pfam02775
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
60-164 1.19e-15

Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;


Pssm-ID: 460689 [Multi-domain]  Cd Length: 151  Bit Score: 70.69  E-value: 1.19e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929576803  60 LGLALAQPKLPVLVITGDGEMLMGMGSLATIGlQKPANLSIVVLDNEAYGETGGQTS------------HTSAAADLVGV 127
Cdd:pfam02775  38 IGAKLARPDRPVVAIAGDGGFQMNLQELATAV-RYNLPITVVVLNNGGYGMTRGQQTpfgggrysgpsgKILPPVDFAKL 116

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1929576803 128 ARACGIKdSRAVTTMAEV-EAFAKAVHdvSAGPRFVNV 164
Cdd:pfam02775 117 AEAYGAK-GARVESPEELeEALKEALE--HDGPALIDV 151
IlvB COG0028
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino ...
 60-167 2.60e-14

Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino acid transport and metabolism, Coenzyme transport and metabolism]; Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis


Pssm-ID: 439799 [Multi-domain]  Cd Length: 548  Bit Score: 70.19  E-value: 2.60e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929576803  60 LGLALAQPKLPVLVITGDGEMLMGMGSLATIGLQKpANLSIVVLDNEAYG--------ETGGQTSHTS-AAADLVGVARA 130
Cdd:COG0028   422 IGAKLARPDRPVVAITGDGGFQMNLQELATAVRYG-LPVKVVVLNNGGLGmvrqwqelFYGGRYSGTDlPNPDFAKLAEA 500

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1929576803 131 CGIKdSRAVTTMAEVE-AFAKAVHdvSAGPRFVNVKID 167
Cdd:COG0028   501 FGAK-GERVETPEELEaALEEALA--SDGPALIDVRVD 535
 
Name Accession Description Interval E-value
TPP_ComE cd03372
Thiamine pyrophosphate (TPP) family, ComE subfamily, TPP-binding module; composed of proteins ...
 9-191 1.41e-76

Thiamine pyrophosphate (TPP) family, ComE subfamily, TPP-binding module; composed of proteins similar to Methanococcus jannaschii sulfopyruvate decarboxylase beta subunit (ComE). M. jannaschii sulfopyruvate decarboxylase (ComDE) is a dodecamer of six alpha (D) subunits and six (E) beta subunits, which catalyzes the decarboxylation of sulfopyruvic acid to sulfoacetaldehyde in the coenzyme M pathway. ComDE requires TPP and divalent metal cation cofactors.


Pssm-ID: 239469 [Multi-domain]  Cd Length: 179  Bit Score: 227.17  E-value: 1.41e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929576803   9 RRQVVATLLANRKDVIAIGGLGASTNDMCAAGDHARNFYLWGGMGGAAMIGLGLALAQPKlPVLVITGDGEMLMGMGSLA 88
Cdd:cd03372     1 RRDAIKTLIADLKDELVVSNIGFPSKELYAAGDRPLNFYMLGSMGLASSIGLGLALAQPR-KVIVIDGDGSLLMNLGALA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929576803  89 TIGLQKPANLSIVVLDNEAYGETGGQTSHTSAAADLVGVARACGIKDSRAVttmAEVEAFAKAVHDVSAGPRFVNVKIDN 168
Cdd:cd03372    80 TIAAEKPKNLIIVVLDNGAYGSTGNQPTHAGKKTDLEAVAKACGLDNVATV---ASEEAFEKAVEQALDGPSFIHVKIKP 156

                         170       180
                  ....*....|....*....|...
gi 1929576803 169 ANLERILPTRDGTYILNRIRGDL 191
Cdd:cd03372   157 GNTDVPNIPRDPVEIKNRFMEAL 179
PRK06163 PRK06163
hypothetical protein; Provisional
 1-196 3.47e-33

hypothetical protein; Provisional


Pssm-ID: 235721 [Multi-domain]  Cd Length: 202  Bit Score: 117.62  E-value: 3.47e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929576803   1 MSKANLLDRrqVVATLlanRKDVIAIGGLGASTNDMCAAGDHARNFYLWGGMGGAAMIGLGLALAQPKLPVLVITGDGEM 80
Cdd:PRK06163   13 MNRFDLTCR--LVAKL---KDEEAVIGGIGNTNFDLWAAGQRPQNFYMLGSMGLAFPIALGVALAQPKRRVIALEGDGSL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929576803  81 LMGMGSLATIGLQKPANLSIVVLDNEAYGETGGQTSHTSAAADLVGVARACGIKDSRAVTTMAEVEAFAKAVHDvSAGPR 160
Cdd:PRK06163   88 LMQLGALGTIAALAPKNLTIIVMDNGVYQITGGQPTLTSQTVDVVAIARGAGLENSHWAADEAHFEALVDQALS-GPGPS 166

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1929576803 161 FVNVKIDNAnLERILPTRDGTYILNRIRGDLGF-QPI 196
Cdd:PRK06163  167 FIAVRIDDK-PGVGTTERDPAQIRERFMQGLGVrEPI 202
TPP_PpyrDC cd03371
Thiamine pyrophosphate (TPP) family, PpyrDC subfamily, TPP-binding module; composed of ...
 9-166 2.69e-32

Thiamine pyrophosphate (TPP) family, PpyrDC subfamily, TPP-binding module; composed of proteins similar to phosphonopyruvate decarboxylase (PpyrDC) proteins. PpyrDC is a homotrimeric enzyme which functions in the biosynthesis of C-P compounds such as bialaphos tripeptide in Streptomyces hygroscopicus. These proteins require TPP and divalent metal cation cofactors.


Pssm-ID: 239468 [Multi-domain]  Cd Length: 188  Bit Score: 114.72  E-value: 2.69e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929576803   9 RRQVVATLLAN--RKDVIaIGGLGASTNDMCAAGD-----HARNFYLWGGMGGAAMIGLGLALAQPKLPVLVITGDGEML 81
Cdd:cd03371     1 REDAIEIVLSRapATAAV-VSTTGMTSRELFELRDrpgggHAQDFLTVGSMGHASQIALGIALARPDRKVVCIDGDGAAL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929576803  82 MGMGSLATIGLQKPANLSIVVLDNEAYGETGGQTSHtSAAADLVGVARACGIKDSRAVTTMAEVEAfakAVHDVSA--GP 159
Cdd:cd03371    80 MHMGGLATIGGLAPANLIHIVLNNGAHDSVGGQPTV-SFDVSLPAIAKACGYRAVYEVPSLEELVA---ALAKALAadGP 155


                  ....*..
gi 1929576803 160 RFVNVKI 166
Cdd:cd03371   156 AFIEVKV 162
Ppyr-DeCO2ase TIGR03297
phosphonopyruvate decarboxylase; This family consists of examples of phosphonopyruvate an ...
 4-166 6.61e-29

phosphonopyruvate decarboxylase; This family consists of examples of phosphonopyruvate an decarboxylase enzyme that produces phosphonoacetaldehyde (Pald), the second step in the biosynthesis phosphonate-containing compounds. Since the preceding enzymate step, PEP phosphomutase (AepX, TIGR02320) favors the substrate PEP energetically, the decarboxylase is required to drive the reaction in the direction of phosphonate production. Pald is a precursor of natural products including antibiotics like bialaphos and phosphonothricin in Streptomyces species, phosphonate-modified molecules such as the polysaccharide B of Bacteroides fragilis, the phosphonolipids of Tetrahymena pyroformis, the glycosylinositolphospholipids of Trypanosoma cruzi. This gene generally occurs in prokaryotic organisms adjacent to the gene for AepX. Most often an aminotansferase (aepZ) is also present which leads to the production of the most common phosphonate compound, 2-aminoethylphosphonate (AEP).


Pssm-ID: 274508 [Multi-domain]  Cd Length: 361  Bit Score: 110.14  E-value: 6.61e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929576803   4 ANLLDRRQVVATLLANRKDVIAI-GGLGASTNDMCAAGD-----HARNFYLWGGMGGAAMIGLGLALAQPKLPVLVITGD 77
Cdd:TIGR03297 169 ATLMTREEAIAAILDHLPDNTVIvSTTGKTSRELYELRDrigqgHARDFLTVGSMGHASQIALGLALARPDQRVVCLDGD 248

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929576803  78 GEMLMGMGSLATIGLQKPANLSIVVLDNEAYGETGGQTSHtSAAADLVGVARACGIKDSRAVTTMAEVEafaKAVHDVSA 157
Cdd:TIGR03297 249 GAALMHMGGLATIGTQGPANLIHVLFNNGAHDSVGGQPTV-SQHLDFAQIAKACGYAKVYEVSTLEELE---TALTAASS 324

                         170
                  ....*....|.
gi 1929576803 158 --GPRFVNVKI 166
Cdd:TIGR03297 325 anGPRLIEVKV 335
TPP_ComE_PpyrDC cd02001
Thiamine pyrophosphate (TPP) family, ComE and PpyrDC subfamily, TPP-binding module; composed ...
 9-166 3.41e-22

Thiamine pyrophosphate (TPP) family, ComE and PpyrDC subfamily, TPP-binding module; composed of proteins similar to sulfopyruvate decarboxylase beta subunit (ComE) and phosphonopyruvate decarboxylase (Ppyr decarboxylase). Methanococcus jannaschii sulfopyruvate decarboxylase (ComDE) is a dodecamer of six alpha (D) subunits and six (E) beta subunits which, catalyzes the decarboxylation of sulfopyruvic acid to sulfoacetaldehyde in the coenzyme M pathway. Ppyr decarboxylase is a homotrimeric enzyme which functions in the biosynthesis of C-P compounds such as bialaphos tripeptide in Streptomyces hygroscopicus. Ppyr decarboxylase and ComDE require TPP and divalent metal cation cofactors.


Pssm-ID: 238959 [Multi-domain]  Cd Length: 157  Bit Score: 87.93  E-value: 3.41e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929576803   9 RRQVVATLLANRKDVIAIGGLGASTNDMCAAGDHARNFYLWGGMGGAAMIGLGLALAQPKlPVLVITGDGEMLMGMGSLA 88
Cdd:cd02001     1 RIAAIAEIIEASGDTPIVSTTGYASRELYDVQDRDGHFYMLGSMGLAGSIGLGLALGLSR-KVIVVDGDGSLLMNPGVLL 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1929576803  89 TIGLQKPANLSIVVLDNEAYGETGGQTSHTSaAADLVGVARACGIKDSRAVTTMAEVEAFAKAVhdVSAGPRFVNVKI 166
Cdd:cd02001    80 TAGEFTPLNLILVVLDNRAYGSTGGQPTPSS-NVNLEAWAAACGYLVLSAPLLGGLGSEFAGLL--ATTGPTLLHAPI 154
TPP_enzyme_C pfam02775
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
60-164 1.19e-15

Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;


Pssm-ID: 460689 [Multi-domain]  Cd Length: 151  Bit Score: 70.69  E-value: 1.19e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929576803  60 LGLALAQPKLPVLVITGDGEMLMGMGSLATIGlQKPANLSIVVLDNEAYGETGGQTS------------HTSAAADLVGV 127
Cdd:pfam02775  38 IGAKLARPDRPVVAIAGDGGFQMNLQELATAV-RYNLPITVVVLNNGGYGMTRGQQTpfgggrysgpsgKILPPVDFAKL 116

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1929576803 128 ARACGIKdSRAVTTMAEV-EAFAKAVHdvSAGPRFVNV 164
Cdd:pfam02775 117 AEAYGAK-GARVESPEELeEALKEALE--HDGPALIDV 151
IlvB COG0028
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino ...
 60-167 2.60e-14

Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino acid transport and metabolism, Coenzyme transport and metabolism]; Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis


Pssm-ID: 439799 [Multi-domain]  Cd Length: 548  Bit Score: 70.19  E-value: 2.60e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929576803  60 LGLALAQPKLPVLVITGDGEMLMGMGSLATIGLQKpANLSIVVLDNEAYG--------ETGGQTSHTS-AAADLVGVARA 130
Cdd:COG0028   422 IGAKLARPDRPVVAITGDGGFQMNLQELATAVRYG-LPVKVVVLNNGGLGmvrqwqelFYGGRYSGTDlPNPDFAKLAEA 500

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1929576803 131 CGIKdSRAVTTMAEVE-AFAKAVHdvSAGPRFVNVKID 167
Cdd:COG0028   501 FGAK-GERVETPEELEaALEEALA--SDGPALIDVRVD 535
TPP_enzymes cd00568
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ...
 60-166 1.73e-13

Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. These enzymes include, among others, the E1 components of the pyruvate, the acetoin and the branched chain alpha-keto acid dehydrogenase complexes.


Pssm-ID: 238318 [Multi-domain]  Cd Length: 168  Bit Score: 65.35  E-value: 1.73e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929576803  60 LGLALAQPKLPVLVITGDGEMLMGMGSLATIGlQKPANLSIVVLDNEAYGET--------GGQTSHTS-AAADLVGVARA 130
Cdd:cd00568    56 IGAALAAPDRPVVCIAGDGGFMMTGQELATAV-RYGLPVIVVVFNNGGYGTIrmhqeafyGGRVSGTDlSNPDFAALAEA 134

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1929576803 131 CGIKdSRAVTTMAEVE-AFAKAVhdVSAGPRFVNVKI 166
Cdd:cd00568   135 YGAK-GVRVEDPEDLEaALAEAL--AAGGPALIEVKT 168
TPP_AHAS cd02015
Thiamine pyrophosphate (TPP) family, Acetohydroxyacid synthase (AHAS) subfamily, TPP-binding ...
 60-176 1.41e-11

Thiamine pyrophosphate (TPP) family, Acetohydroxyacid synthase (AHAS) subfamily, TPP-binding module; composed of proteins similar to the large catalytic subunit of AHAS. AHAS catalyzes the condensation of two molecules of pyruvate to give the acetohydroxyacid, 2-acetolactate. 2-Acetolactate is the precursor of the branched chain amino acids, valine and leucine. AHAS also catalyzes the condensation of pyruvate and 2-ketobutyrate to form 2-aceto-2-hydroxybutyrate in isoleucine biosynthesis. In addition to requiring TPP and a divalent metal ion as cofactors, AHAS requires FAD.


Pssm-ID: 238973 [Multi-domain]  Cd Length: 186  Bit Score: 60.20  E-value: 1.41e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929576803  60 LGLALAQPKLPVLVITGDGEMLMGMGSLATIGLQKpANLSIVVLDNEAYG--------ETGGQTSHTSAA--ADLVGVAR 129
Cdd:cd02015    60 IGAKVARPDKTVICIDGDGSFQMNIQELATAAQYN-LPVKIVILNNGSLGmvrqwqelFYEGRYSHTTLDsnPDFVKLAE 138

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1929576803 130 ACGIKdSRAVTTMAEVE-AFAKAVHdvSAGPRFVNVKIDNAnlERILP 176
Cdd:cd02015   139 AYGIK-GLRVEKPEELEaALKEALA--SDGPVLLDVLVDPE--ENVLP 181
PRK11867 PRK11867
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed
 61-120 4.08e-10

2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed


Pssm-ID: 237006 [Multi-domain]  Cd Length: 286  Bit Score: 57.54  E-value: 4.08e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1929576803  61 GLALAQPKLPVLVITGDGEML-MGMGSL--AtigLQKPANLSIVVLDNEAYGETGGQTSHTSA 120
Cdd:PRK11867   80 GLKLANPDLTVIVVTGDGDALaIGGNHFihA---LRRNIDITYILFNNQIYGLTKGQYSPTSP 139
PorB COG1013
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta ...
 61-164 1.51e-09

Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta subunit [Energy production and conversion]; Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta subunit is part of the Pathway/BioSystem: Pyruvate oxidation


Pssm-ID: 440637 [Multi-domain]  Cd Length: 262  Bit Score: 55.92  E-value: 1.51e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929576803  61 GLALAQPKLPVLVITGDGEML-MGMGSLatIGlqkpA-----NLSIVVLDNEAYGETGGQTSHTS--------------- 119
Cdd:COG1013    75 GIKLANPDLTVIVFGGDGDTYdIGGNHL--IH----AarrneDITYIVYDNEIYGNTGGQRSPTTplgakttttpygkpe 148

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1929576803 120 ---------AAADLVGVARAcgikdsrAVTTMAE-VEAFAKAV-HDvsaGPRFVNV 164
Cdd:COG1013   149 ppkdpaeiaAAHGATYVARA-------SVGDPKDlKKKIKKAIeHK---GFSFIEV 194
TPP_POX cd02014
Thiamine pyrophosphate (TPP) family, Pyruvate oxidase (POX) subfamily, TPP-binding module; ...
 60-168 7.81e-09

Thiamine pyrophosphate (TPP) family, Pyruvate oxidase (POX) subfamily, TPP-binding module; composed of proteins similar to Lactobacillus plantarum POX, which plays a key role in controlling acetate production under aerobic conditions. POX decarboxylates pyruvate, producing hydrogen peroxide and the energy-storage metabolite acetylphosphate. It requires FAD in addition to TPP and a divalent cation as cofactors.


Pssm-ID: 238972 [Multi-domain]  Cd Length: 178  Bit Score: 52.92  E-value: 7.81e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929576803  60 LGLALAQPKLPVLVITGDGEMLMGMGSLATIGLQKPAnLSIVVLDNEAYG------ETGGQ----TSHTsaAADLVGVAR 129
Cdd:cd02014    61 IAAKLAYPDRQVIALSGDGGFAMLMGDLITAVKYNLP-VIVVVFNNSDLGfikweqEVMGQpefgVDLP--NPDFAKIAE 137

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1929576803 130 ACGIKDSRaVTTMAEVE-AFAKAVHdvSAGPRFVNVKIDN 168
Cdd:cd02014   138 AMGIKGIR-VEDPDELEaALDEALA--ADGPVVIDVVTDP 174
TPP_Xsc_like cd02013
Thiamine pyrophosphate (TPP) family, Xsc-like subfamily, TPP-binding module; composed of ...
 60-167 3.62e-08

Thiamine pyrophosphate (TPP) family, Xsc-like subfamily, TPP-binding module; composed of proteins similar to Alcaligenes defragrans sulfoacetaldehyde acetyltransferase (Xsc). Xsc plays a key role in the degradation of taurine, catalyzing the desulfonation of 2-sulfoacetaldehyde into sulfite and acetyl phosphate. This enzyme requires TPP and divalent metal ions for activity.


Pssm-ID: 238971 [Multi-domain]  Cd Length: 196  Bit Score: 51.36  E-value: 3.62e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929576803  60 LGLALAQPKLPVLVITGDGEMLMGMGSLATIGLQKPAnLSIVVLDNEAYG-ETGGQT---SHTSAAADL-----VGVARA 130
Cdd:cd02013    63 IGAKAAAPDRPVVAIAGDGAWGMSMMEIMTAVRHKLP-VTAVVFRNRQWGaEKKNQVdfyNNRFVGTELesesfAKIAEA 141

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1929576803 131 CGIKDSRAVTTMAEVEAFAKAVHDVSAG-PRFVNVKID 167
Cdd:cd02013   142 CGAKGITVDKPEDVGPALQKAIAMMAEGkTTVIEIVCD 179
TPP_OGFOR cd03375
Thiamine pyrophosphate (TPP family), 2-oxoglutarate ferredoxin oxidoreductase (OGFOR) ...
 61-119 3.60e-07

Thiamine pyrophosphate (TPP family), 2-oxoglutarate ferredoxin oxidoreductase (OGFOR) subfamily, TPP-binding module; OGFOR catalyzes the oxidative decarboxylation of 2-oxo-acids, with ferredoxin acting as an electron acceptor. In the TCA cycle, OGFOR catalyzes the oxidative decarboxylation of 2-oxoglutarate to succinyl-CoA. In the reductive tricarboxylic acid cycle found in the anaerobic autotroph Hydrogenobacter thermophilus, OGFOR catalyzes the reductive carboxylation of succinyl-CoA to produce 2-oxoglutarate. Thauera aromatica OGFOR has been shown to provide reduced ferredoxin to benzoyl-CoA reductase, a key enzyme in the anaerobic metabolism of aromatic compounds. OGFOR is dependent on TPP and a divalent metal cation for activity.


Pssm-ID: 239470 [Multi-domain]  Cd Length: 193  Bit Score: 48.29  E-value: 3.60e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929576803  61 GLALAQPKLPVLVITGDGEMLmGMGSLATI-GLQKPANLSIVVLDNEAYGETGGQTSHTS 119
Cdd:cd03375    62 GVKLANPDLTVIVVSGDGDLA-AIGGNHFIhAARRNIDITVIVHNNQIYGLTKGQASPTT 120
PRK05778 PRK05778
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated
 61-119 1.06e-06

2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated


Pssm-ID: 235604 [Multi-domain]  Cd Length: 301  Bit Score: 47.57  E-value: 1.06e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929576803  61 GLALAQPKLPVLVITGDGEML-MGMGSLATIGLQKPaNLSIVVLDNEAYGETGGQTSHTS 119
Cdd:PRK05778   81 GAKLANPDLEVIVVGGDGDLAsIGGGHFIHAGRRNI-DITVIVENNGIYGLTKGQASPTT 139
PLN02470 PLN02470
acetolactate synthase
 60-176 3.71e-06

acetolactate synthase


Pssm-ID: 215261 [Multi-domain]  Cd Length: 585  Bit Score: 46.65  E-value: 3.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929576803  60 LGLALAQPKLPVLVITGDGEMLMGMGSLATIGLQKpANLSIVVLDNEAYGET--------GGQTSHT-----SAAA---- 122
Cdd:PLN02470  436 IGAAAANPDAIVVDIDGDGSFIMNIQELATIHVEN-LPVKIMVLNNQHLGMVvqwedrfyKANRAHTylgdpDAEAeifp 514

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1929576803 123 DLVGVARACGIKDSRaVTTMAEVEAFAKAVHDvSAGPRFVNVKIdnANLERILP 176
Cdd:PLN02470  515 DFLKFAEGCKIPAAR-VTRKSDLREAIQKMLD-TPGPYLLDVIV--PHQEHVLP 564
TPP_BZL_OCoD_HPCL cd02004
Thiamine pyrophosphate (TPP) family, BZL_OCoD_HPCL subfamily, TPP-binding module; composed of ...
 60-167 9.13e-06

Thiamine pyrophosphate (TPP) family, BZL_OCoD_HPCL subfamily, TPP-binding module; composed of proteins similar to benzaldehyde lyase (BZL), oxalyl-CoA decarboxylase (OCoD) and 2-hydroxyphytanoyl-CoA lyase (2-HPCL). Pseudomonas fluorescens biovar I BZL cleaves the acyloin linkage of benzoin producing 2 molecules of benzaldehyde and enabling the Pseudomonas to grow on benzoin as the sole carbon and energy source. OCoD has a role in the detoxification of oxalate, catalyzing the decarboxylation of oxalyl-CoA to formate. 2-HPCL is a peroxisomal enzyme which plays a role in the alpha-oxidation of 3-methyl-branched fatty acids, catalyzing the cleavage of 2-hydroxy-3-methylacyl-CoA into formyl-CoA and a 2-methyl-branched fatty aldehyde. All these enzymes depend on Mg2+ and TPP for activity.


Pssm-ID: 238962 [Multi-domain]  Cd Length: 172  Bit Score: 44.06  E-value: 9.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929576803  60 LGLALAQPKLPVLVITGDGEMLMGMGSLATIGLQKPANLSIVVLDNEAYGETGGQ---------TSHTSAAADLVGVARA 130
Cdd:cd02004    58 IAAALARPDKRVVLVEGDGAFGFSGMELETAVRYNLPIVVVVGNNGGWYQGLDGQqlsyglglpVTTLLPDTRYDLVAEA 137

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1929576803 131 CGIKDSRaVTTMAEVE-AFAKAVhdVSAGPRFVNVKID 167
Cdd:cd02004   138 FGGKGEL-VTTPEELKpALKRAL--ASGKPALINVIID 172
TPP_IOR_alpha cd02008
Thiamine pyrophosphate (TPP) family, IOR-alpha subfamily, TPP-binding module; composed of ...
 61-152 1.18e-05

Thiamine pyrophosphate (TPP) family, IOR-alpha subfamily, TPP-binding module; composed of proteins similar to indolepyruvate ferredoxin oxidoreductase (IOR) alpha subunit. IOR catalyzes the oxidative decarboxylation of arylpyruvates, such as indolepyruvate or phenylpyruvate, which are generated by the transamination of aromatic amino acids, to the corresponding aryl acetyl-CoA.


Pssm-ID: 238966 [Multi-domain]  Cd Length: 178  Bit Score: 43.81  E-value: 1.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929576803  61 GLALAQPKLPVLVITGDGeMLMGMGSLATIG-LQKPANLSIVVLDNEAYGETGGQTSHTSAAA--------DLVGVARAC 131
Cdd:cd02008    62 GMAKASEDKKVVAVIGDS-TFFHSGILGLINaVYNKANITVVILDNRTTAMTGGQPHPGTGKTltepttviDIEALVRAI 140

                          90       100
                  ....*....|....*....|....
gi 1929576803 132 GIKDSRAVTTM---AEVEAFAKAV 152
Cdd:cd02008   141 GVKRVVVVDPYdlkAIREELKEAL 164
TPP_BFDC cd02002
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins ...
 60-166 2.44e-05

Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins similar to Pseudomonas putida benzoylformate decarboxylase (BFDC). P. putida BFDC plays a role in the mandelate pathway, catalyzing the conversion of benzoylformate to benzaldehyde and carbon dioxide. This enzyme is dependent on TPP and a divalent metal cation as cofactors.


Pssm-ID: 238960 [Multi-domain]  Cd Length: 178  Bit Score: 42.97  E-value: 2.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929576803  60 LGLALAQPKLPVLVITGDGEMLMGMGSLATIGlQKPANLSIVVLDNEAYG----ETGGQTSHTSAAA------------D 123
Cdd:cd02002    59 VGAALANPDRKVVAIIGDGSFMYTIQALWTAA-RYGLPVTVVILNNRGYGalrsFLKRVGPEGPGENapdgldlldpgiD 137

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1929576803 124 LVGVARACGIKDSRAVTTMAEVEAFAKAVHDvsAGPRFVNVKI 166
Cdd:cd02002   138 FAAIAKAFGVEAERVETPEELDEALREALAE--GGPALIEVVV 178
TPP_IolD cd02003
Thiamine pyrophosphate (TPP) family, IolD subfamily, TPP-binding module; composed of proteins ...
 60-167 2.54e-05

Thiamine pyrophosphate (TPP) family, IolD subfamily, TPP-binding module; composed of proteins similar to Rhizobium leguminosarum bv. viciae IolD. IolD plays an important role in myo-inositol catabolism.


Pssm-ID: 238961 [Multi-domain]  Cd Length: 205  Bit Score: 43.06  E-value: 2.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929576803  60 LGLALAQPKLPVLVITGDGEMLMGMGSLATIgLQKPANLSIVVLDNEAYGETGG-QTSHTSAA----------------- 121
Cdd:cd02003    58 LGAKLAKPDREVYVLVGDGSYLMLHSEIVTA-VQEGLKIIIVLFDNHGFGCINNlQESTGSGSfgtefrdrdqesgqldg 136

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1929576803 122 ----ADLVGVARACGIkDSRAVTTMAEV-EAFAKAvhDVSAGPRFVNVKID 167
Cdd:cd02003   137 allpVDFAANARSLGA-RVEKVKTIEELkAALAKA--KASDRTTVIVIKTD 184
PRK08527 PRK08527
acetolactate synthase large subunit;
60-176 3.62e-05

acetolactate synthase large subunit;


Pssm-ID: 181458 [Multi-domain]  Cd Length: 563  Bit Score: 43.55  E-value: 3.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929576803  60 LGLALAQPKLPVLVITGDGEMLMGMGSLATIGLQKPANLSIvVLDNEAYG-----ET---GGQTSHT--SAAADLVGVAR 129
Cdd:PRK08527  424 LGAKLAVPDKVVINFTGDGSILMNIQELMTAVEYKIPVINI-ILNNNFLGmvrqwQTffyEERYSETdlSTQPDFVKLAE 502

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1929576803 130 ACGIKDSRAVTTMAEVEAFAKAVHdvSAGPRFVNVKIDnaNLERILP 176
Cdd:PRK08527  503 SFGGIGFRVTTKEEFDKALKEALE--SDKVALIDVKID--RFENVLP 545
PRK06546 PRK06546
pyruvate dehydrogenase; Provisional
 60-169 4.36e-05

pyruvate dehydrogenase; Provisional


Pssm-ID: 180614 [Multi-domain]  Cd Length: 578  Bit Score: 43.44  E-value: 4.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929576803  60 LGLALAQPKLPVLVITGDGEMLMGMGSLATIGL-QKPANlsIVVLDNEAYGET------GGQTSH--TSAAADLVGVARA 130
Cdd:PRK06546  418 IGAQLADPGRQVISMSGDGGLSMLLGELLTVKLyDLPVK--VVVFNNSTLGMVklemlvDGLPDFgtDHPPVDYAAIAAA 495

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1929576803 131 CGIKDSRaVTTMAEVE-AFAKAV-HDvsaGPRFVNVKID-NA 169
Cdd:PRK06546  496 LGIHAVR-VEDPKDVRgALREAFaHP---GPALVDVVTDpNA 533
PRK07525 PRK07525
sulfoacetaldehyde acetyltransferase; Validated
 60-166 5.14e-05

sulfoacetaldehyde acetyltransferase; Validated


Pssm-ID: 236042 [Multi-domain]  Cd Length: 588  Bit Score: 43.06  E-value: 5.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929576803  60 LGLALAQPKLPVLVITGDGEMLMGMGSLATIGlQKPANLSIVVLDNEAYG-ETGGQT---SHTSAAADL------VGVAR 129
Cdd:PRK07525  445 IGAKIACPDRPVVGFAGDGAWGISMNEVMTAV-RHNWPVTAVVFRNYQWGaEKKNQVdfyNNRFVGTELdnnvsyAGIAE 523

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1929576803 130 ACGIKDSRaVTTMAEV-EAFAKAVHDVSAG-PRFVNVKI 166
Cdd:PRK07525  524 AMGAEGVV-VDTQEELgPALKRAIDAQNEGkTTVIEIMC 561
ilvB CHL00099
acetohydroxyacid synthase large subunit
 60-134 1.03e-04

acetohydroxyacid synthase large subunit


Pssm-ID: 214363 [Multi-domain]  Cd Length: 585  Bit Score: 41.99  E-value: 1.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929576803  60 LGLALAQPKLPVLVITGDGEMLMGMGSLATIGlQKPANLSIVVLDN----------EA-YGETGGQTSHTSAAADLVGVA 128
Cdd:CHL00099  440 IGAQIAHPNELVICISGDASFQMNLQELGTIA-QYNLPIKIIIINNkwqgmvrqwqQAfYGERYSHSNMEEGAPDFVKLA 518


                  ....*.
gi 1929576803 129 RACGIK 134
Cdd:CHL00099  519 EAYGIK 524
PRK08266 PRK08266
hypothetical protein; Provisional
 60-166 1.76e-04

hypothetical protein; Provisional


Pssm-ID: 181337 [Multi-domain]  Cd Length: 542  Bit Score: 41.54  E-value: 1.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929576803  60 LGLALAQPKLPVLVITGDGEMLMGMGSLATiGLQKPANLSIVVLDNEAYG--------ETGGQTshtsAAADL-----VG 126
Cdd:PRK08266  412 LGAKVANPDRPVVSITGDGGFMFGVQELAT-AVQHNIGVVTVVFNNNAYGnvrrdqkrRFGGRV----VASDLvnpdfVK 486

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1929576803 127 VARACGIKDSRAVTTMAEVEAFAKAVHDvsAGPRFVNVKI 166
Cdd:PRK08266  487 LAESFGVAAFRVDSPEELRAALEAALAH--GGPVLIEVPV 524
PRK06276 PRK06276
acetolactate synthase large subunit;
60-188 1.89e-04

acetolactate synthase large subunit;


Pssm-ID: 235766 [Multi-domain]  Cd Length: 586  Bit Score: 41.28  E-value: 1.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929576803  60 LGLALAQPKLPVLVITGDGEMLMGMGSLATIGlQKPANLSIVVLDNEAYGET--------GGQTSHT--SAAADLVGVAR 129
Cdd:PRK06276  429 IGAKVAKPDANVIAITGDGGFLMNSQELATIA-EYDIPVVICIFDNRTLGMVyqwqnlyyGKRQSEVhlGETPDFVKLAE 507

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1929576803 130 ACGIKDSRaVTTMAEV-EAFAKAVHdvSAGPRFVNVKIDNANLERILPTRDG-TYILNRIR 188
Cdd:PRK06276  508 SYGVKADR-VEKPDEIkEALKEAIK--SGEPYLLDIIIDPAEALPMVPPGGNlTNILGPYR 565
PRK08199 PRK08199
thiamine pyrophosphate protein; Validated
 60-188 2.08e-04

thiamine pyrophosphate protein; Validated


Pssm-ID: 181285 [Multi-domain]  Cd Length: 557  Bit Score: 41.40  E-value: 2.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929576803  60 LGLALAQPKLPVLVITGDGEMLMGMGSLATiGLQKPANLSIVVLDNEAYG--------ETGGQTSHTS-AAADLVGVARA 130
Cdd:PRK08199  425 IAAKLLFPERTVVAFAGDGCFLMNGQELAT-AVQYGLPIIVIVVNNGMYGtirmhqerEYPGRVSGTDlTNPDFAALARA 503

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1929576803 131 CGIKDSRAVTTMAEVEAFAKAVHdvSAGPRFVNVKIDNanlERILPTRDgtyiLNRIR 188
Cdd:PRK08199  504 YGGHGETVERTEDFAPAFERALA--SGKPALIEIRIDP---EAITPTAT----LSQIR 552
PRK07064 PRK07064
thiamine pyrophosphate-binding protein;
60-109 3.15e-04

thiamine pyrophosphate-binding protein;


Pssm-ID: 180820 [Multi-domain]  Cd Length: 544  Bit Score: 40.74  E-value: 3.15e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1929576803  60 LGLALAQPKLPVLVITGDGEMLMGMGSLATIgLQKPANLSIVVLDNEAYG 109
Cdd:PRK07064  415 IGAALAGPGRKTVGLVGDGGLMLNLGELATA-VQENANMVIVLMNDGGYG 463
TPP_PFOR cd02018
Thiamine pyrophosphate (TPP family), Pyruvate ferredoxin/flavodoxin oxidoreductase (PFOR) ...
 64-119 3.89e-04

Thiamine pyrophosphate (TPP family), Pyruvate ferredoxin/flavodoxin oxidoreductase (PFOR) subfamily, TPP-binding module; PFOR catalyzes the oxidative decarboxylation of pyruvate to form acetyl-CoA, a crucial step in many metabolic pathways. Archaea, anaerobic bacteria and eukaryotes that lack mitochondria (and therefore pyruvate dehydrogenase) use PFOR to oxidatively decarboxylate pyruvate, with ferredoxin or flavodoxin as the electron acceptor. PFORs can be homodimeric, heterodimeric, or heterotetrameric, depending on the organism. These enzymes are dependent on TPP and a divalent metal cation as cofactors.


Pssm-ID: 238976 [Multi-domain]  Cd Length: 237  Bit Score: 39.78  E-value: 3.89e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1929576803  64 LAQPKlPVLVITGDGEML-MGMGSLATIgLQKPANLSIVVLDNEAYGETGGQTSHTS 119
Cdd:cd02018    84 LDKKK-DVVVIGGDGATYdIGFGALSHS-LFRGEDITVIVLDNEVYSNTGGQRSGAT 138
PRK08155 PRK08155
acetolactate synthase large subunit;
60-109 4.01e-04

acetolactate synthase large subunit;


Pssm-ID: 181257 [Multi-domain]  Cd Length: 564  Bit Score: 40.46  E-value: 4.01e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1929576803  60 LGLALAQPKLPVLVITGDGEMLMGMGSLATIGlQKPANLSIVVLDNEAYG 109
Cdd:PRK08155  429 IGAALANPERKVLCFSGDGSLMMNIQEMATAA-ENQLDVKIILMNNEALG 477
oorB PRK09628
2-oxoglutarate ferredoxin oxidoreductase subunit beta;
61-119 5.69e-04

2-oxoglutarate ferredoxin oxidoreductase subunit beta;


Pssm-ID: 182003 [Multi-domain]  Cd Length: 277  Bit Score: 39.71  E-value: 5.69e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929576803  61 GLALAQPKLPVLVITGDGEMLmGMGSLATI-GLQKPANLSIVVLDNEAYGETGGQTSHTS 119
Cdd:PRK09628   79 GIKLANPDKHVIVVSGDGDGL-AIGGNHTIhGCRRNIDLNFILINNFIYGLTNSQTSPTT 137
PRK08978 PRK08978
acetolactate synthase 2 catalytic subunit; Reviewed
 60-169 6.15e-04

acetolactate synthase 2 catalytic subunit; Reviewed


Pssm-ID: 181601 [Multi-domain]  Cd Length: 548  Bit Score: 39.86  E-value: 6.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929576803  60 LGLALAQPKLPVLVITGDGEMLMGMGSLATIGlQKPANLSIVVLDNEAYGET--------GGQTSHT--SAAADLVGVAR 129
Cdd:PRK08978  411 IGAQVARPDDTVICVSGDGSFMMNVQELGTIK-RKQLPVKIVLLDNQRLGMVrqwqqlffDERYSETdlSDNPDFVMLAS 489

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1929576803 130 ACGIKdSRAVTTMAEVEAFAKAVHDvSAGPRFVNVKIDNA 169
Cdd:PRK08978  490 AFGIP-GQTITRKDQVEAALDTLLN-SEGPYLLHVSIDEL 527
PRK11866 PRK11866
2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional
 10-119 2.18e-03

2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional


Pssm-ID: 183347 [Multi-domain]  Cd Length: 279  Bit Score: 37.81  E-value: 2.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929576803  10 RQVVATLLANRKDVIAIGGLGAST------NDMCAAGDHARnfylwggmggAAMIGLGLALAQPKLPVLVITGDGEmlmG 83
Cdd:PRK11866   23 RKALAELGIPPENVVVVSGIGCSSnlpeflNTYGIHGIHGR----------VLPIATGVKWANPKLTVIGYGGDGD---G 89

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1929576803  84 MGslatIGLQ-------KPANLSIVVLDNEAYGETGGQTSHTS 119
Cdd:PRK11866   90 YG----IGLGhlphaarRNVDITYIVSNNQVYGLTTGQASPTT 128
TPP_SHCHC_synthase cd02009
Thiamine pyrophosphate (TPP) family, SHCHC synthase subfamily, TPP-binding module; composed of ...
 60-167 2.23e-03

Thiamine pyrophosphate (TPP) family, SHCHC synthase subfamily, TPP-binding module; composed of proteins similar to Escherichia coli 2-succinyl-6-hydroxyl-2,4-cyclohexadiene-1-carboxylic acid (SHCHC) synthase (also called MenD). SHCHC synthase plays a key role in the menaquinone biosynthetic pathway, converting isochorismate and 2-oxoglutarate to SHCHC, pyruvate and carbon dioxide. The enzyme requires TPP and a divalent metal cation for activity.


Pssm-ID: 238967 [Multi-domain]  Cd Length: 175  Bit Score: 37.19  E-value: 2.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929576803  60 LGLALAQPKlPVLVITGDGEMLMGMGSLAtIGLQKPANLSIVVLDN------------------EAYGETgGQTSHTSAA 121
Cdd:cd02009    61 LGIALATDK-PTVLLTGDLSFLHDLNGLL-LGKQEPLNLTIVVINNngggifsllpqasfedefERLFGT-PQGLDFEHL 137

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1929576803 122 ADLVGVaracgikDSRAVTTMAEV-EAFAKAVHdvSAGPRFVNVKID 167
Cdd:cd02009   138 AKAYGL-------EYRRVSSLDELeQALESALA--QDGPHVIEVKTD 175
PRK06112 PRK06112
acetolactate synthase catalytic subunit; Validated
 60-167 2.55e-03

acetolactate synthase catalytic subunit; Validated


Pssm-ID: 235700 [Multi-domain]  Cd Length: 578  Bit Score: 37.82  E-value: 2.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929576803  60 LGLALAQPKLPVLVITGDGEMLMGMGSLATIGLQKpANLSIVVLDNEAYG-----ETGGQTSHTSA----AADLVGVARA 130
Cdd:PRK06112  447 IGAKVARPGAPVICLVGDGGFAHVWAELETARRMG-VPVTIVVLNNGILGfqkhaETVKFGTHTDAchfaAVDHAAIARA 525

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1929576803 131 CGIKDSRaVTTMAEVeAFAKAVHDVSAGPRFVNVKID 167
Cdd:PRK06112  526 CGCDGVR-VEDPAEL-AQALAAAMAAPGPTLIEVITD 560
PRK06965 PRK06965
acetolactate synthase 3 catalytic subunit; Validated
 60-132 4.04e-03

acetolactate synthase 3 catalytic subunit; Validated


Pssm-ID: 180780 [Multi-domain]  Cd Length: 587  Bit Score: 37.47  E-value: 4.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929576803  60 LGLALAQPKLPVLVITGDGEMLMGMGSLATIgLQKPANLSIVVLDNEAYG--------ETGGQTSHT--SAAADLVGVAR 129
Cdd:PRK06965  447 MGIKMAHPDDDVVCITGEGSIQMCIQELSTC-LQYDTPVKIISLNNRYLGmvrqwqeiEYSKRYSHSymDALPDFVKLAE 525


                  ...
gi 1929576803 130 ACG 132
Cdd:PRK06965  526 AYG 528
pyruv_ox_red TIGR02176
pyruvate:ferredoxin (flavodoxin) oxidoreductase, homodimeric; This model represents a single ...
 68-135 4.26e-03

pyruvate:ferredoxin (flavodoxin) oxidoreductase, homodimeric; This model represents a single chain form of pyruvate:ferredoxin (or flavodoxin) oxidoreductase. This enzyme may transfer electrons to nitrogenase in nitrogen-fixing species. Portions of this protein are homologous to gamma subunit of the four subunit pyruvate:ferredoxin (flavodoxin) oxidoreductase.


Pssm-ID: 131231 [Multi-domain]  Cd Length: 1165  Bit Score: 37.44  E-value: 4.26e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1929576803   68 KLPVLVITGDGEML-MGMGSLATIgLQKPANLSIVVLDNEAYGETGGQTSH---TSAAADLVGVARACGIKD 135
Cdd:TIGR02176  951 KKSVWIIGGDGWAYdIGYGGLDHV-LASGKDVNVLVMDTEVYSNTGGQSSKatpTGAIAKFAAAGKRTSKKD 1021
PRK11869 PRK11869
2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional
 65-119 5.32e-03

2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional


Pssm-ID: 183349 [Multi-domain]  Cd Length: 280  Bit Score: 36.68  E-value: 5.32e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1929576803  65 AQPKLPVLVITGDGEMLMGMGSLATIGLQKPANLSIVVLDNEAYGETGGQTSHTS 119
Cdd:PRK11869   75 TNPELTVIAEGGDGDMYAEGGNHLIHAIRRNPDITVLVHNNQVYGLTKGQASPTT 129
TPP_PFOR_PNO cd03377
Thiamine pyrophosphate (TPP family), PFOR_PNO subfamily, TPP-binding module; composed of ...
 97-148 5.72e-03

Thiamine pyrophosphate (TPP family), PFOR_PNO subfamily, TPP-binding module; composed of proteins similar to the single subunit pyruvate ferredoxin oxidoreductase (PFOR) of Desulfovibrio Africanus, present in bacteria and amitochondriate eukaryotes. This subfamily also includes proteins characterized as pyruvate NADP+ oxidoreductase (PNO). These enzymes are dependent on TPP and a divalent metal cation as cofactors. PFOR and PNO catalyze the oxidative decarboxylation of pyruvate to form acetyl-CoA, a crucial step in many metabolic pathways. Archaea, anaerobic bacteria and eukaryotes that lack mitochondria (and therefore pyruvate dehydrogenase) use PFOR to oxidatively decarboxylate pyruvate, with ferredoxin or flavodoxin as the electron acceptor. The PFOR from cyanobacterium Anabaena (NifJ) is required for the transfer of electrons from pyruvate to flavodoxin, which reduces nitrogenase. The facultative anaerobic mitochondrion of the photosynthetic protist Euglena gracilis oxidizes pyruvate with PNO.


Pssm-ID: 239472  Cd Length: 365  Bit Score: 36.81  E-value: 5.72e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1929576803  97 NLSIVVLDNEAYGETGGQTS---HTSAAA------------DL---------VGVAR-ACGIKDSRAVTTMAEVEAF 148
Cdd:cd03377   180 NVNILVLDTEVYSNTGGQASkatPLGAVAkfaaagkrtgkkDLgmiamsygnVYVAQiALGANDNQTLKAFREAEAY 256
TPP_PFOR_porB_like cd03376
Thiamine pyrophosphate (TPP family), PFOR porB-like subfamily, TPP-binding module; composed of ...
 71-116 7.48e-03

Thiamine pyrophosphate (TPP family), PFOR porB-like subfamily, TPP-binding module; composed of proteins similar to the beta subunit (porB) of the Helicobacter pylori four-subunit pyruvate ferredoxin oxidoreductase (PFOR), which are also found in archaea and some hyperthermophilic bacteria. PFOR catalyzes the oxidative decarboxylation of pyruvate to form acetyl-CoA, a crucial step in many metabolic pathways. Archaea, anaerobic bacteria and eukaryotes that lack mitochondria (and therefore pyruvate dehydrogenase) use PFOR to oxidatively decarboxylate pyruvate, with ferredoxin or flavodoxin as the electron acceptor. The 36-kDa porB subunit contains the binding sites for the cofactors, TPP and a divalent metal cation, which are required for activity.


Pssm-ID: 239471 [Multi-domain]  Cd Length: 235  Bit Score: 36.06  E-value: 7.48e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1929576803  71 VLVITGDG-EMLMGMGSLatIG-LQKPANLSIVVLDNEAYGETGGQTS 116
Cdd:cd03376    83 VVAFAGDGgTADIGFQAL--SGaAERGHDILYICYDNEAYMNTGIQRS 128
PRK08611 PRK08611
pyruvate oxidase; Provisional
 63-167 8.47e-03

pyruvate oxidase; Provisional


Pssm-ID: 181502 [Multi-domain]  Cd Length: 576  Bit Score: 36.52  E-value: 8.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929576803  63 ALAQPKLPVLVITGDGEMLMGMGSLAT-IGLQKPanLSIVVLDNEAYG------ETGGQTSHTSAAADL--VGVARACGI 133
Cdd:PRK08611  421 KIAFPDRQAIAICGDGGFSMVMQDFVTaVKYKLP--IVVVVLNNQQLAfikyeqQAAGELEYAIDLSDMdyAKFAEACGG 498

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1929576803 134 KDSRaVTTMAEV-EAFAKAVHdvSAGPRFVNVKID 167
Cdd:PRK08611  499 KGYR-VEKAEELdPAFEEALA--QDKPVIIDVYVD 530
PDC1 COG3961
TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase [Carbohydrate ...
 60-167 8.54e-03

TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase [Carbohydrate transport and metabolism, Coenzyme transport and metabolism, General function prediction only]; TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase is part of the Pathway/BioSystem: Pyruvate oxidation


Pssm-ID: 443161 [Multi-domain]  Cd Length: 545  Bit Score: 36.29  E-value: 8.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929576803  60 LGLALAQPKLPVLVITGDGE-MLMGMgSLATIGL--QKPAnlsIVVLDNEAYG-EtggQTSHTSAAA-------DLVGVA 128
Cdd:COG3961   418 LGAALAAPDRRVILLVGDGAfQLTAQ-ELSTMLRygLKPI---IFVLNNDGYTiE---RAIHGPDGPyndianwDYAKLP 490

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1929576803 129 RACGIKDSRA--VTTMAE-VEAFAKAVHDvSAGPRFVNVKID 167
Cdd:COG3961   491 EAFGGGNALGfrVTTEGElEEALAAAEAN-TDRLTLIEVVLD 531
 
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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