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Conserved domains on  [gi|908618329|ref|WP_049762955|]
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phosphonopyruvate decarboxylase [Shewanella denitrificans]

Protein Classification

thiamine pyrophosphate enzyme family protein( domain architecture ID 11496572)

thiamine pyrophosphate (TPP) enzyme family protein which requires TPP, and may be a phosphonopyruvate (PnPy) decarboxylase which catalyzes the decarboxylation of PnPy to form phosphonoacetaldehyde (PnAA) in the biosynthesis of phosphonate-containing compounds, similar to Streptomyces fradiae putative PnPy decarboxylase Fom2 which may produce PnAA in the fosfomycin biosynthetic pathway

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Ppyr-DeCO2ase TIGR03297
phosphonopyruvate decarboxylase; This family consists of examples of phosphonopyruvate an ...
 13-373 0e+00

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: 537.71  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908618329   13 NITFWSSVPCSILNPLYNVFS-RSDDIRSVTATSEGEAVGIASGAWLA-GERAGVMMQNSGLGNAINPLTSL--NIPFQI 88
Cdd:TIGR03297   1 GFDFFSGVPDSLLKPFCNYITdNNRDLRHVIAANEGAAVGLAAGAYLAtGKRAAVYMQNSGLGNAVNPLTSLadTEVYDI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908618329   89 PLALMITWRGKPGMKDEPQHEFMGKITPSLLSLLEFGAEEISTD-LVRLEQSFRTLAAQLDERKSHALLIPSGILSSQAF 167
Cdd:TIGR03297  81 PLLLIVGWRGEPGVHDEPQHVKQGRITLSLLDALEIPWEVLSTDnDEALAQIERALAHALATSRPYALVVRKGTFASYKL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908618329  168 DVTPSNEIVTtsvqnfldnrgIPTRYKAIEACLDTLPELSAIIATTGKTGRELFTIGDQ-----ERFFYQVGSMGCASAI 242
Cdd:TIGR03297 161 KGGPANPYAT-----------LMTREEAIAAILDHLPDNTVIVSTTGKTSRELYELRDRigqghARDFLTVGSMGHASQI 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908618329  243 GLGVALN-SKLPIVIFDGDGAALMKLGNLATIGNQSPENLIHIIFDNGVYDSTGGQFTHSQTTDFAEIAKACGYCNVYRA 321
Cdd:TIGR03297 230 ALGLALArPDQRVVCLDGDGAALMHMGGLATIGTQGPANLIHVLFNNGAHDSVGGQPTVSQHLDFAQIAKACGYAKVYEV 309

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 908618329  322 NSIEGLRKSVTNAVKESGPNLIHMKIAPGSLKNLARPTVSPSEVAFRFRTFL 373
Cdd:TIGR03297 310 STLEELETALTAASSANGPRLIEVKVRPGSRADLGRPTTSPPENKRRFMRFL 361
 
Name Accession Description Interval E-value
Ppyr-DeCO2ase TIGR03297
phosphonopyruvate decarboxylase; This family consists of examples of phosphonopyruvate an ...
 13-373 0e+00

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: 537.71  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908618329   13 NITFWSSVPCSILNPLYNVFS-RSDDIRSVTATSEGEAVGIASGAWLA-GERAGVMMQNSGLGNAINPLTSL--NIPFQI 88
Cdd:TIGR03297   1 GFDFFSGVPDSLLKPFCNYITdNNRDLRHVIAANEGAAVGLAAGAYLAtGKRAAVYMQNSGLGNAVNPLTSLadTEVYDI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908618329   89 PLALMITWRGKPGMKDEPQHEFMGKITPSLLSLLEFGAEEISTD-LVRLEQSFRTLAAQLDERKSHALLIPSGILSSQAF 167
Cdd:TIGR03297  81 PLLLIVGWRGEPGVHDEPQHVKQGRITLSLLDALEIPWEVLSTDnDEALAQIERALAHALATSRPYALVVRKGTFASYKL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908618329  168 DVTPSNEIVTtsvqnfldnrgIPTRYKAIEACLDTLPELSAIIATTGKTGRELFTIGDQ-----ERFFYQVGSMGCASAI 242
Cdd:TIGR03297 161 KGGPANPYAT-----------LMTREEAIAAILDHLPDNTVIVSTTGKTSRELYELRDRigqghARDFLTVGSMGHASQI 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908618329  243 GLGVALN-SKLPIVIFDGDGAALMKLGNLATIGNQSPENLIHIIFDNGVYDSTGGQFTHSQTTDFAEIAKACGYCNVYRA 321
Cdd:TIGR03297 230 ALGLALArPDQRVVCLDGDGAALMHMGGLATIGTQGPANLIHVLFNNGAHDSVGGQPTVSQHLDFAQIAKACGYAKVYEV 309

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 908618329  322 NSIEGLRKSVTNAVKESGPNLIHMKIAPGSLKNLARPTVSPSEVAFRFRTFL 373
Cdd:TIGR03297 310 STLEELETALTAASSANGPRLIEVKVRPGSRADLGRPTTSPPENKRRFMRFL 361
TPP_PpyrDC cd03371
Thiamine pyrophosphate (TPP) family, PpyrDC subfamily, TPP-binding module; composed of ...
 192-373 9.80e-98

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: 288.44  E-value: 9.80e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908618329 192 RYKAIEACLDTLPELSAIIATTGKTGRELFTIGDQ-----ERFFYQVGSMGCASAIGLGVALNSK-LPIVIFDGDGAALM 265
Cdd:cd03371    1 REDAIEIVLSRAPATAAVVSTTGMTSRELFELRDRpggghAQDFLTVGSMGHASQIALGIALARPdRKVVCIDGDGAALM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908618329 266 KLGNLATIGNQSPENLIHIIFDNGVYDSTGGQFTHSQTTDFAEIAKACGYCNVYRANSIEGLRKSVTNAVKESGPNLIHM 345
Cdd:cd03371   81 HMGGLATIGGLAPANLIHIVLNNGAHDSVGGQPTVSFDVSLPAIAKACGYRAVYEVPSLEELVAALAKALAADGPAFIEV 160

                        170       180
                 ....*....|....*....|....*...
gi 908618329 346 KIAPGSLKNLARPTVSPSEVAFRFRTFL 373
Cdd:cd03371  161 KVRPGSRSDLGRPTTSPIENKERFMAFL 188
COG4032 COG4032
Sulfopyruvate decarboxylase, TPP-binding subunit (coenzyme M biosynthesis) [Coenzyme transport ...
 3-167 1.64e-52

Sulfopyruvate decarboxylase, TPP-binding subunit (coenzyme M biosynthesis) [Coenzyme transport and metabolism];


Pssm-ID: 443210  Cd Length: 168  Bit Score: 171.93  E-value: 1.64e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908618329   3 SAIIEHVKLQNITFWSSVPCSILNPLYNVFSRSDDIRSVTATSEGEAVGIASGAWLAGERAGVMMQNSGLGNAINPLTSL 82
Cdd:COG4032    5 EAVVDALKEAGIDFVAYVPCSVLKPLINLLEADPDIRHVPVTREEEAVGIAAGAYLGGKRPVVLMQNSGLGNSINALASL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908618329  83 NIPFQIPLALMITWRGKPGmKDEPQHEFMGKITPSLLSLLEFGAEEIST--DLVRLEQSFRTLAaqLDERKSHALLIPSG 160
Cdd:COG4032   85 NLTYRIPLLMLVSWRGEPG-EDNPAQVPMGRITPPLLDAMGIPYFVLDTpeDVEPVIARAIEHA--FETGRPVAVLLSPG 161


                 ....*..
gi 908618329 161 ILSSQAF 167
Cdd:COG4032  162 LWGGKAL 168
PRK06163 PRK06163
hypothetical protein; Provisional
 185-347 4.44e-29

hypothetical protein; Provisional


Pssm-ID: 235721 [Multi-domain]  Cd Length: 202  Bit Score: 111.85  E-value: 4.44e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908618329 185 DNRGIPTRYKAIEACLDTLPELSAIIATTGKTGRELFTIGDQERFFYQVGSMGCASAIGLGVAL-NSKLPIVIFDGDGAA 263
Cdd:PRK06163   8 SNAKVMNRFDLTCRLVAKLKDEEAVIGGIGNTNFDLWAAGQRPQNFYMLGSMGLAFPIALGVALaQPKRRVIALEGDGSL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908618329 264 LMKLGNLATIGNQSPENLIHIIFDNGVYDSTGGQFT-HSQTTDFAEIAKACGYCNVYRANSIEGLRKSVTNAVKESGPNL 342
Cdd:PRK06163  88 LMQLGALGTIAALAPKNLTIIVMDNGVYQITGGQPTlTSQTVDVVAIARGAGLENSHWAADEAHFEALVDQALSGPGPSF 167


                 ....*
gi 908618329 343 IHMKI 347
Cdd:PRK06163 168 IAVRI 172
TPP_enzyme_C pfam02775
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
234-344 9.15e-18

Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;


Pssm-ID: 460689 [Multi-domain]  Cd Length: 151  Bit Score: 79.55  E-value: 9.15e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908618329  234 GSMGCASAIGLGVAL-NSKLPIVIFDGDGAALMKLGNLATIGnQSPENLIHIIFDNGVYDSTGGQ------FTHSQTT-- 304
Cdd:pfam02775  28 GTMGYGLPAAIGAKLaRPDRPVVAIAGDGGFQMNLQELATAV-RYNLPITVVVLNNGGYGMTRGQqtpfggGRYSGPSgk 106

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 908618329  305 -----DFAEIAKACGyCNVYRANSIEGLRKSVTNAVKESGPNLIH 344
Cdd:pfam02775 107 ilppvDFAKLAEAYG-AKGARVESPEELEEALKEALEHDGPALID 150
 
Name Accession Description Interval E-value
Ppyr-DeCO2ase TIGR03297
phosphonopyruvate decarboxylase; This family consists of examples of phosphonopyruvate an ...
 13-373 0e+00

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: 537.71  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908618329   13 NITFWSSVPCSILNPLYNVFS-RSDDIRSVTATSEGEAVGIASGAWLA-GERAGVMMQNSGLGNAINPLTSL--NIPFQI 88
Cdd:TIGR03297   1 GFDFFSGVPDSLLKPFCNYITdNNRDLRHVIAANEGAAVGLAAGAYLAtGKRAAVYMQNSGLGNAVNPLTSLadTEVYDI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908618329   89 PLALMITWRGKPGMKDEPQHEFMGKITPSLLSLLEFGAEEISTD-LVRLEQSFRTLAAQLDERKSHALLIPSGILSSQAF 167
Cdd:TIGR03297  81 PLLLIVGWRGEPGVHDEPQHVKQGRITLSLLDALEIPWEVLSTDnDEALAQIERALAHALATSRPYALVVRKGTFASYKL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908618329  168 DVTPSNEIVTtsvqnfldnrgIPTRYKAIEACLDTLPELSAIIATTGKTGRELFTIGDQ-----ERFFYQVGSMGCASAI 242
Cdd:TIGR03297 161 KGGPANPYAT-----------LMTREEAIAAILDHLPDNTVIVSTTGKTSRELYELRDRigqghARDFLTVGSMGHASQI 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908618329  243 GLGVALN-SKLPIVIFDGDGAALMKLGNLATIGNQSPENLIHIIFDNGVYDSTGGQFTHSQTTDFAEIAKACGYCNVYRA 321
Cdd:TIGR03297 230 ALGLALArPDQRVVCLDGDGAALMHMGGLATIGTQGPANLIHVLFNNGAHDSVGGQPTVSQHLDFAQIAKACGYAKVYEV 309

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 908618329  322 NSIEGLRKSVTNAVKESGPNLIHMKIAPGSLKNLARPTVSPSEVAFRFRTFL 373
Cdd:TIGR03297 310 STLEELETALTAASSANGPRLIEVKVRPGSRADLGRPTTSPPENKRRFMRFL 361
TPP_PpyrDC cd03371
Thiamine pyrophosphate (TPP) family, PpyrDC subfamily, TPP-binding module; composed of ...
 192-373 9.80e-98

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: 288.44  E-value: 9.80e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908618329 192 RYKAIEACLDTLPELSAIIATTGKTGRELFTIGDQ-----ERFFYQVGSMGCASAIGLGVALNSK-LPIVIFDGDGAALM 265
Cdd:cd03371    1 REDAIEIVLSRAPATAAVVSTTGMTSRELFELRDRpggghAQDFLTVGSMGHASQIALGIALARPdRKVVCIDGDGAALM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908618329 266 KLGNLATIGNQSPENLIHIIFDNGVYDSTGGQFTHSQTTDFAEIAKACGYCNVYRANSIEGLRKSVTNAVKESGPNLIHM 345
Cdd:cd03371   81 HMGGLATIGGLAPANLIHIVLNNGAHDSVGGQPTVSFDVSLPAIAKACGYRAVYEVPSLEELVAALAKALAADGPAFIEV 160

                        170       180
                 ....*....|....*....|....*...
gi 908618329 346 KIAPGSLKNLARPTVSPSEVAFRFRTFL 373
Cdd:cd03371  161 KVRPGSRSDLGRPTTSPIENKERFMAFL 188
TPP_ComE_PpyrDC cd02001
Thiamine pyrophosphate (TPP) family, ComE and PpyrDC subfamily, TPP-binding module; composed ...
 192-350 3.03e-53

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: 173.44  E-value: 3.03e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908618329 192 RYKAIEACLDTLPELsAIIATTGKTGRELFTIGDQERFFYQVGSMGCASAIGLGVALNSKLPIVIFDGDGAALMKLGNLA 271
Cdd:cd02001    1 RIAAIAEIIEASGDT-PIVSTTGYASRELYDVQDRDGHFYMLGSMGLAGSIGLGLALGLSRKVIVVDGDGSLLMNPGVLL 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 908618329 272 TIGNQSPENLIHIIFDNGVYDSTGGQFTHSQTTDFAEIAKACGYcNVYRANSIEGLRKSVTNAVKESGPNLIHMKIAPG 350
Cdd:cd02001   80 TAGEFTPLNLILVVLDNRAYGSTGGQPTPSSNVNLEAWAAACGY-LVLSAPLLGGLGSEFAGLLATTGPTLLHAPIAPG 157
COG4032 COG4032
Sulfopyruvate decarboxylase, TPP-binding subunit (coenzyme M biosynthesis) [Coenzyme transport ...
 3-167 1.64e-52

Sulfopyruvate decarboxylase, TPP-binding subunit (coenzyme M biosynthesis) [Coenzyme transport and metabolism];


Pssm-ID: 443210  Cd Length: 168  Bit Score: 171.93  E-value: 1.64e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908618329   3 SAIIEHVKLQNITFWSSVPCSILNPLYNVFSRSDDIRSVTATSEGEAVGIASGAWLAGERAGVMMQNSGLGNAINPLTSL 82
Cdd:COG4032    5 EAVVDALKEAGIDFVAYVPCSVLKPLINLLEADPDIRHVPVTREEEAVGIAAGAYLGGKRPVVLMQNSGLGNSINALASL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908618329  83 NIPFQIPLALMITWRGKPGmKDEPQHEFMGKITPSLLSLLEFGAEEIST--DLVRLEQSFRTLAaqLDERKSHALLIPSG 160
Cdd:COG4032   85 NLTYRIPLLMLVSWRGEPG-EDNPAQVPMGRITPPLLDAMGIPYFVLDTpeDVEPVIARAIEHA--FETGRPVAVLLSPG 161


                 ....*..
gi 908618329 161 ILSSQAF 167
Cdd:COG4032  162 LWGGKAL 168
TPP_ComE cd03372
Thiamine pyrophosphate (TPP) family, ComE subfamily, TPP-binding module; composed of proteins ...
 192-373 1.31e-51

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: 170.16  E-value: 1.31e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908618329 192 RYKAIEACLDTLPElSAIIATTGKTGRELFTIGDQERFFYQVGSMGCASAIGLGVALNSKLPIVIFDGDGAALMKLGNLA 271
Cdd:cd03372    1 RRDAIKTLIADLKD-ELVVSNIGFPSKELYAAGDRPLNFYMLGSMGLASSIGLGLALAQPRKVIVIDGDGSLLMNLGALA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908618329 272 TIGNQSPENLIHIIFDNGVYDSTGGQFTHS-QTTDFAEIAKACGYCNVYRANSIEGLRKSVTNAVKesGPNLIHMKIAPG 350
Cdd:cd03372   80 TIAAEKPKNLIIVVLDNGAYGSTGNQPTHAgKKTDLEAVAKACGLDNVATVASEEAFEKAVEQALD--GPSFIHVKIKPG 157

                        170       180
                 ....*....|....*....|...
gi 908618329 351 SLKnLARPTVSPSEVAFRFRTFL 373
Cdd:cd03372  158 NTD-VPNIPRDPVEIKNRFMEAL 179
PRK06163 PRK06163
hypothetical protein; Provisional
 185-347 4.44e-29

hypothetical protein; Provisional


Pssm-ID: 235721 [Multi-domain]  Cd Length: 202  Bit Score: 111.85  E-value: 4.44e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908618329 185 DNRGIPTRYKAIEACLDTLPELSAIIATTGKTGRELFTIGDQERFFYQVGSMGCASAIGLGVAL-NSKLPIVIFDGDGAA 263
Cdd:PRK06163   8 SNAKVMNRFDLTCRLVAKLKDEEAVIGGIGNTNFDLWAAGQRPQNFYMLGSMGLAFPIALGVALaQPKRRVIALEGDGSL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908618329 264 LMKLGNLATIGNQSPENLIHIIFDNGVYDSTGGQFT-HSQTTDFAEIAKACGYCNVYRANSIEGLRKSVTNAVKESGPNL 342
Cdd:PRK06163  88 LMQLGALGTIAALAPKNLTIIVMDNGVYQITGGQPTlTSQTVDVVAIARGAGLENSHWAADEAHFEALVDQALSGPGPSF 167


                 ....*
gi 908618329 343 IHMKI 347
Cdd:PRK06163 168 IAVRI 172
sulfopyru_alph TIGR03845
sulfopyruvate decarboxylase, alpha subunit; This model represents the alpha subunit, or the ...
 4-157 6.48e-28

sulfopyruvate decarboxylase, alpha subunit; This model represents the alpha subunit, or the N-terminal region, of sulfopyruvate decarboxylase, an enzyme of coenzyme M biosynthesis. Coenzyme M is found almost exclusively in the methanogenic archaea. However, the enzyme also occurs in Roseovarius nubinhibens ISM in a degradative pathway, where the resulting sulfoacetaldehyde is desulfonated to acetyl phosphate, then converted to acetyl-CoA (see ). [Biosynthesis of cofactors, prosthetic groups, and carriers, Other, Energy metabolism, Methanogenesis]


Pssm-ID: 163557  Cd Length: 157  Bit Score: 107.36  E-value: 6.48e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908618329    4 AIIEHVKLQNITFWSSVPCSILNPLYNVFSrsDDIRSVTATSEGEAVGIASGAWLAGERAGVMMQNSGLGNAINPLTSLN 83
Cdd:TIGR03845   3 AVYNILKDAGIDLVASVPCDNLKNLLPLIE--KDFRHIPLTREEEGVGICAGAYLAGKKPAILMQSSGLGNSINALASLN 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 908618329   84 IPFQIPLALMITWRGKPGMKDEPQHEfMGKITPSLLSLLEFGAEEIST--DLVRLEQSFRtlaAQLDERKSHALLI 157
Cdd:TIGR03845  81 KTYGIPLPILASWRGVYKEKIPAQIP-MGRATPKLLDTLGIPYTIPREpeEAKLIEKAIS---DAYENSRPVAALL 152
TPP_enzymes cd00568
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ...
 196-347 7.32e-20

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: 85.77  E-value: 7.32e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908618329 196 IEACLDTLPELSAIIATTG---KTGRELFTIGDQERFFYQ--VGSMGCASAIGLGVAL-NSKLPIVIFDGDGAALMKLGN 269
Cdd:cd00568    3 LAALRAALPEDAIVVNDAGnsaYWAYRYLPLRRGRRFLTStgFGAMGYGLPAAIGAALaAPDRPVVCIAGDGGFMMTGQE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908618329 270 LATIGnQSPENLIHIIFDNGVYDSTGGQ----------FTHSQTTDFAEIAKACGyCNVYRANSIEGLRKSVTNAVKESG 339
Cdd:cd00568   83 LATAV-RYGLPVIVVVFNNGGYGTIRMHqeafyggrvsGTDLSNPDFAALAEAYG-AKGVRVEDPEDLEAALAEALAAGG 160


                 ....*...
gi 908618329 340 PNLIHMKI 347
Cdd:cd00568  161 PALIEVKT 168
TPP_PYR_POX_like cd07035
Pyrimidine (PYR) binding domain of POX and related proteins; Thiamine pyrophosphate (TPP ...
 4-115 1.00e-18

Pyrimidine (PYR) binding domain of POX and related proteins; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) binding domain of pyruvate oxidase (POX) and related protiens subfamily. The PYR domain is found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. TPP binds in the cleft formed by a PYR domain and a PP domain. The PYR domain, binds the aminopyrimidine ring of TPP, the PP domain binds the diphosphate residue. A polar interaction between the conserved glutamate of the PYR domain and the N1' of the TPP aminopyrimidine ring is shared by most TPP-dependent enzymes, and participates in the activation of TPP. For glyoxylate carboligase, which belongs to this subfamily, but lacks this conserved glutamate, the rate of the initial TPP activation step is reduced but the ensuing steps of the enzymic reaction proceed efficiently. The PYR and PP domains have a common fold, but do not share strong sequence conservation. The PP domain is not included in this sub-family. Most TPP-dependent enzymes have the PYR and PP domains on the same subunit although these domains can be alternatively arranged in the primary structure. TPP-dependent enzymes are multisubunit proteins, the smallest catalytic unit being a dimer-of-active sites, for many the active sites lie between PP and PYR domains on different subunits. POX decarboxylates pyruvate, producing hydrogen peroxide and the energy-storage metabolite acetylphosphate. This subfamily includes pyruvate decarboxylase (PDC) and indolepyruvate decarboxylase (IPDC). PDC catalyzes the conversion of pyruvate to acetaldehyde and CO2 in alcoholic fermentation. IPDC plays a role in the indole-3-pyruvic acid (IPA) pathway in plants and various plant-associated bacteria, it catalyzes the decarboxylation of IPA to IAA. This subfamily also includes the large catalytic subunit of acetohydroxyacid synthase (AHAS). AHAS catalyzes the condensation of two molecules of pyruvate to give the acetohydroxyacid, 2-acetolactate, a 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. Methanococcus jannaschii sulfopyruvate decarboxylase (MjComDE) and phosphonopyruvate decarboxylase (PpyrDc) also belong to this subfamily. PpyrDc is a homotrimeric enzyme having the PP and PYR domains tandemly arranged on the same subunit. It functions in the biosynthesis of C-P compounds such as bialaphos tripeptide in Streptomyces hygroscopicus. MjComDE is a dodecamer having the PYR and PP domains on different subunits, it has six alpha (PYR/ComD) subunits and six beta (PP/ComE) subunits. MjComDE catalyzes the decarboxylation of sulfopyruvic acid to sulfoacetaldehyde in the coenzyme M pathway.


Pssm-ID: 132918 [Multi-domain]  Cd Length: 155  Bit Score: 82.19  E-value: 1.00e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908618329   4 AIIEHVKLQNITFWSSVPCSILNPLYNVFSRSDdIRSVTATSEGEAVGIASGAWLAGERAGV-MMQ-NSGLGNAINPLTS 81
Cdd:cd07035    2 ALVEALKAEGVDHVFGVPGGAILPLLDALARSG-IRYILVRHEQGAVGMADGYARATGKPGVvLVTsGPGLTNAVTGLAN 80

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 908618329  82 LNIPfQIPLALMITWRGKPGMK-----DEPQHEFMGKIT 115
Cdd:cd07035   81 AYLD-SIPLLVITGQRPTAGEGrgafqEIDQVALFRPIT 118
TPP_enzyme_C pfam02775
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
234-344 9.15e-18

Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;


Pssm-ID: 460689 [Multi-domain]  Cd Length: 151  Bit Score: 79.55  E-value: 9.15e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908618329  234 GSMGCASAIGLGVAL-NSKLPIVIFDGDGAALMKLGNLATIGnQSPENLIHIIFDNGVYDSTGGQ------FTHSQTT-- 304
Cdd:pfam02775  28 GTMGYGLPAAIGAKLaRPDRPVVAIAGDGGFQMNLQELATAV-RYNLPITVVVLNNGGYGMTRGQqtpfggGRYSGPSgk 106

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 908618329  305 -----DFAEIAKACGyCNVYRANSIEGLRKSVTNAVKESGPNLIH 344
Cdd:pfam02775 107 ilppvDFAKLAEAYG-AKGARVESPEELEEALKEALEHDGPALID 150
IlvB COG0028
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino ...
 234-349 2.31e-12

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: 68.26  E-value: 2.31e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908618329 234 GSMGCA--SAIGLGVAlNSKLPIVIFDGDGAALMKLGNLATIGNQSPeNLIHIIFDNGVY--------DSTGGQFTHS-- 301
Cdd:COG0028  412 GTMGYGlpAAIGAKLA-RPDRPVVAITGDGGFQMNLQELATAVRYGL-PVKVVVLNNGGLgmvrqwqeLFYGGRYSGTdl 489

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 908618329 302 QTTDFAEIAKACGyCNVYRANSIEGLRKSVTNAVKESGPNLIHMKIAP 349
Cdd:COG0028  490 PNPDFAKLAEAFG-AKGERVETPEELEAALEEALASDGPALIDVRVDP 536
TPP_AHAS cd02015
Thiamine pyrophosphate (TPP) family, Acetohydroxyacid synthase (AHAS) subfamily, TPP-binding ...
 234-349 2.39e-09

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: 56.35  E-value: 2.39e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908618329 234 GSMGCA--SAIGLGVALNSKLPIVIfDGDGAALMKLGNLATIgnqSPENL--IHIIFDNGV-----------YDstgGQF 298
Cdd:cd02015   50 GTMGFGlpAAIGAKVARPDKTVICI-DGDGSFQMNIQELATA---AQYNLpvKIVILNNGSlgmvrqwqelfYE---GRY 122

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 908618329 299 THSQ---TTDFAEIAKACGyCNVYRANSIEGLRKSVTNAVKESGPNLIHMKIAP 349
Cdd:cd02015  123 SHTTldsNPDFVKLAEAYG-IKGLRVEKPEELEAALKEALASDGPVLLDVLVDP 175
TPP_POX cd02014
Thiamine pyrophosphate (TPP) family, Pyruvate oxidase (POX) subfamily, TPP-binding module; ...
 234-349 7.93e-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: 54.46  E-value: 7.93e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908618329 234 GSMGCASAIGLGVALNS-KLPIVIFDGDGAALMKLGNLATI-GNQSPenLIHIIFDNGVYdstgGQFTHSQT-------- 303
Cdd:cd02014   51 ATMGNGLPGAIAAKLAYpDRQVIALSGDGGFAMLMGDLITAvKYNLP--VIVVVFNNSDL----GFIKWEQEvmgqpefg 124

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 908618329 304 -----TDFAEIAKACGYcNVYRANSIEGLRKSVTNAVKESGPNLIHMKIAP 349
Cdd:cd02014  125 vdlpnPDFAKIAEAMGI-KGIRVEDPDELEAALDEALAADGPVVIDVVTDP 174
PRK06456 PRK06456
acetolactate synthase large subunit;
183-362 7.62e-08

acetolactate synthase large subunit;


Pssm-ID: 180569 [Multi-domain]  Cd Length: 572  Bit Score: 54.07  E-value: 7.62e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908618329 183 FLDNRGIPTRYKAIEACLDTLPELSaiIATTG----KTGRELFTIGDQERFFYQVGSMGC-----ASAIGLGVALNSKLp 253
Cdd:PRK06456 365 YTEENGKLKPWKIMKTIRQALPRDA--IVTTGvgqhQMWAEVFWEVLEPRTFLTSSGMGTmgfglPAAMGAKLARPDKV- 441

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908618329 254 IVIFDGDGAALMKLGNLATIGNqspENL--IHIIFDN---GVYDSTGGQF--------THSQTTDFAEIAKACGYCNvYR 320
Cdd:PRK06456 442 VVDLDGDGSFLMTGTNLATAVD---EHIpvISVIFDNrtlGLVRQVQDLFfgkrivgvDYGPSPDFVKLAEAFGALG-FN 517

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 908618329 321 ANSIEGLRKSVTNAVKESGPNLIHMkiaPGSLKNLARPTVSP 362
Cdd:PRK06456 518 VTTYEDIEKSLKSAIKEDIPAVIRV---PVDKEELALPTLPP 556
PorB COG1013
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta ...
 237-344 1.95e-07

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: 51.68  E-value: 1.95e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908618329 237 GCASAIGLGVAL-NSKLPIVIFDGDGAAlmklgnlATIGNQS-------PENLIHIIFDNGVYDSTGGQFthSQTT---- 304
Cdd:COG1013   67 GRAAAVATGIKLaNPDLTVIVFGGDGDT-------YDIGGNHlihaarrNEDITYIVYDNEIYGNTGGQR--SPTTplga 137

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 908618329 305 --------------DFAEIAKACGYCNVYRANS--IEGLRKSVTNAVKESGPNLIH 344
Cdd:COG1013  138 kttttpygkpeppkDPAEIAAAHGATYVARASVgdPKDLKKKIKKAIEHKGFSFIE 193
PRK05778 PRK05778
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated
 237-318 2.70e-06

2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated


Pssm-ID: 235604 [Multi-domain]  Cd Length: 301  Bit Score: 48.72  E-value: 2.70e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908618329 237 GCASAIGLGVAL-NSKLPIVIFDGDGaalmklgNLATIG-NQspenLIH----------IIFDNGVYDSTGGQFthSQTT 304
Cdd:PRK05778  73 GRAIAFATGAKLaNPDLEVIVVGGDG-------DLASIGgGH----FIHagrrniditvIVENNGIYGLTKGQA--SPTT 139

                         90
                 ....*....|....
gi 908618329 305 DFAEIAKACGYCNV 318
Cdd:PRK05778 140 PEGSKTKTAPYGNI 153
TPP_OGFOR cd03375
Thiamine pyrophosphate (TPP family), 2-oxoglutarate ferredoxin oxidoreductase (OGFOR) ...
 237-320 2.16e-04

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: 41.74  E-value: 2.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908618329 237 GCASAIGLGVAL-NSKLPIVIFDGDGaalmklgNLATIG-NQspenLIH----------IIFDNGVYDSTGGQFthSQTT 304
Cdd:cd03375   54 GRALAVATGVKLaNPDLTVIVVSGDG-------DLAAIGgNH----FIHaarrniditvIVHNNQIYGLTKGQA--SPTT 120

                         90
                 ....*....|....*.
gi 908618329 305 DFAEIAKACGYCNVYR 320
Cdd:cd03375  121 PEGFKTKTTPYGNIEE 136
PRK09124 PRK09124
ubiquinone-dependent pyruvate dehydrogenase;
234-343 6.56e-04

ubiquinone-dependent pyruvate dehydrogenase;


Pssm-ID: 181661 [Multi-domain]  Cd Length: 574  Bit Score: 41.51  E-value: 6.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908618329 234 GSMGCASAIGLGV-ALNSKLPIVIFDGDGAALMKLGNLATIG-NQSPENLIhiIFDNGV------------YDSTGgqfT 299
Cdd:PRK09124 408 GSMANAMPQALGAqAAHPGRQVVALSGDGGFSMLMGDFLSLVqLKLPVKIV--VFNNSVlgfvamemkaggYLTDG---T 482

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 908618329 300 HSQTTDFAEIAKACGYCNVyRANSIEGLRKSVTNAVKESGPNLI 343
Cdd:PRK09124 483 DLHNPDFAAIAEACGITGI-RVEKASELDGALQRAFAHDGPALV 525
PRK09259 PRK09259
putative oxalyl-CoA decarboxylase; Validated
 234-355 1.26e-03

putative oxalyl-CoA decarboxylase; Validated


Pssm-ID: 236433 [Multi-domain]  Cd Length: 569  Bit Score: 40.74  E-value: 1.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908618329 234 GSMGCASAIGLGVALNSKLPIVIFDGDGAALMKLGNLATIGNQspeNL--IHIIFDN-GVY---DSTGGQFTHSQTTDFA 307
Cdd:PRK09259 424 GVMGIGMGYAIAAAVETGKPVVAIEGDSAFGFSGMEVETICRY---NLpvTVVIFNNgGIYrgdDVNLSGAGDPSPTVLV 500

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 908618329 308 ------EIAKACGYCNvYRANSIEGLRKSVTNAVKESGPNLIHMKIAP------GSLKNL 355
Cdd:PRK09259 501 hharydKMMEAFGGVG-YNVTTPDELRHALTEAIASGKPTLINVVIDPaagtesGHITNL 559
PRK07064 PRK07064
thiamine pyrophosphate-binding protein;
217-353 1.38e-03

thiamine pyrophosphate-binding protein;


Pssm-ID: 180820 [Multi-domain]  Cd Length: 544  Bit Score: 40.74  E-value: 1.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908618329 217 GRELFTIGDQERFFYQVGS---MGCASAIGLGVAlNSKLPIVIFDGDGAALMKLGNLATIGnQSPENLIHIIFDNGVY-- 291
Cdd:PRK07064 387 GNRLLPIFEPRANVHALGGgigQGLAMAIGAALA-GPGRKTVGLVGDGGLMLNLGELATAV-QENANMVIVLMNDGGYgv 464

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 908618329 292 ------DSTGGQFTHSQ--TTDFAEIAKACGyCNVYRANSIEGLRKSVTNAVKESGPNLIHMKI-APGSLK 353
Cdd:PRK07064 465 irniqdAQYGGRRYYVElhTPDFALLAASLG-LPHWRVTSADDFEAVLREALAKEGPVLVEVDMlSIGPFA 534
TPP_PFOR cd02018
Thiamine pyrophosphate (TPP family), Pyruvate ferredoxin/flavodoxin oxidoreductase (PFOR) ...
 254-344 1.90e-03

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: 39.39  E-value: 1.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908618329 254 IVIFDGDGAALmKLGNLATIGN-QSPENLIHIIFDNGVYDSTGGQFTHSQTT----------------DFAEIAKACGyc 316
Cdd:cd02018   90 VVVIGGDGATY-DIGFGALSHSlFRGEDITVIVLDNEVYSNTGGQRSGATPLgadskmapagkkedkkDLVLIAATHG-- 166

                         90       100       110
                 ....*....|....*....|....*....|...
gi 908618329 317 NVYRANSIEGLRKSVTNAVKES-----GPNLIH 344
Cdd:cd02018  167 CVYVARLSPALKKHFLKVVKEAisrtdGPTFIH 199
PRK06276 PRK06276
acetolactate synthase large subunit;
234-362 3.59e-03

acetolactate synthase large subunit;


Pssm-ID: 235766 [Multi-domain]  Cd Length: 586  Bit Score: 39.35  E-value: 3.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908618329 234 GSMGCA--SAIGLGVALNSKlPIVIFDGDGAALMKLGNLATIGNQSPENLIhIIFDN---GV--------YDSTGGQFTH 300
Cdd:PRK06276 419 GTMGFGfpAAIGAKVAKPDA-NVIAITGDGGFLMNSQELATIAEYDIPVVI-CIFDNrtlGMvyqwqnlyYGKRQSEVHL 496

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 908618329 301 SQTTDFAEIAKACGyCNVYRANSIEGLRKSVTNAVKESGPNLIHMKIAPGSlknlARPTVSP 362
Cdd:PRK06276 497 GETPDFVKLAESYG-VKADRVEKPDEIKEALKEAIKSGEPYLLDIIIDPAE----ALPMVPP 553
PRK08155 PRK08155
acetolactate synthase large subunit;
234-349 3.66e-03

acetolactate synthase large subunit;


Pssm-ID: 181257 [Multi-domain]  Cd Length: 564  Bit Score: 39.31  E-value: 3.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908618329 234 GSMGCASAIGLGVAL-NSKLPIVIFDGDGAALMKLGNLAT------------IGNQSpENLIH----IIFDNGVYDStgg 296
Cdd:PRK08155 419 GTMGFGLPAAIGAALaNPERKVLCFSGDGSLMMNIQEMATaaenqldvkiilMNNEA-LGLVHqqqsLFYGQRVFAA--- 494

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 908618329 297 qfTHSQTTDFAEIAKACGY--CNVyraNSIEGLRKSVTNAVKESGPNLIHMKIAP 349
Cdd:PRK08155 495 --TYPGKINFMQIAAGFGLetCDL---NNEADPQAALQEAINRPGPALIHVRIDA 544
 
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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