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Conserved domains on  [gi|1387289096|gb|AWI10178|]
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phosphonopyruvate decarboxylase [Ereboglobus luteus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Ppyr-DeCO2ase super family cl37240
phosphonopyruvate decarboxylase; This family consists of examples of phosphonopyruvate an ...
 15-362 2.21e-141

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).


The actual alignment was detected with superfamily member TIGR03297:

Pssm-ID: 274508 [Multi-domain]  Cd Length: 361  Bit Score: 405.59  E-value: 2.21e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387289096  15 GYTFYSGVPCSFLKDLINYAINECE---YVMAANEGDAAAICAGASLA-GKKNVLLMQNSGLGNAVSPLTSL--NKVFDI 88
Cdd:TIGR03297   1 GFDFFSGVPDSLLKPFCNYITDNNRdlrHVIAANEGAAVGLAAGAYLAtGKRAAVYMQNSGLGNAVNPLTSLadTEVYDI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387289096  89 PVLGFVSLRGEQGIPDEPQHELMGRITEAMLATMEIDWDYLSADFEEAQKQLEKADDYI-NANKSFFFVVRKNTFSKVLL 167
Cdd:TIGR03297  81 PLLLIVGWRGEPGVHDEPQHVKQGRITLSLLDALEIPWEVLSTDNDEALAQIERALAHAlATSRPYALVVRKGTFASYKL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387289096 168 NKNNE-PNAGLPKRGELIETVLNTCAGDTAFIATTGFTGRELSQIKD-----GANNFYMVGSLGCASSLALGLSLAKPSQ 241
Cdd:TIGR03297 161 KGGPAnPYATLMTREEAIAAILDHLPDNTVIVSTTGKTSRELYELRDrigqgHARDFLTVGSMGHASQIALGLALARPDQ 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387289096 242 KVVVFDGDSALLMRMGALAVNAYYAPKNFCHIVFDNQAHESTGGQFNVSCNMDYEGLAKSCGYKTVKTVATKDELQSLLA 321
Cdd:TIGR03297 241 RVVCLDGDGAALMHMGGLATIGTQGPANLIHVLFNNGAHDSVGGQPTVSQHLDFAQIAKACGYAKVYEVSTLEELETALT 320

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 1387289096 322 DWNANGGMMFIHAKIAQGTLENLERPKTKPREVAKRFSTYI 362
Cdd:TIGR03297 321 AASSANGPRLIEVKVRPGSRADLGRPTTSPPENKRRFMRFL 361
 
Name Accession Description Interval E-value
Ppyr-DeCO2ase TIGR03297
phosphonopyruvate decarboxylase; This family consists of examples of phosphonopyruvate an ...
 15-362 2.21e-141

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: 405.59  E-value: 2.21e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387289096  15 GYTFYSGVPCSFLKDLINYAINECE---YVMAANEGDAAAICAGASLA-GKKNVLLMQNSGLGNAVSPLTSL--NKVFDI 88
Cdd:TIGR03297   1 GFDFFSGVPDSLLKPFCNYITDNNRdlrHVIAANEGAAVGLAAGAYLAtGKRAAVYMQNSGLGNAVNPLTSLadTEVYDI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387289096  89 PVLGFVSLRGEQGIPDEPQHELMGRITEAMLATMEIDWDYLSADFEEAQKQLEKADDYI-NANKSFFFVVRKNTFSKVLL 167
Cdd:TIGR03297  81 PLLLIVGWRGEPGVHDEPQHVKQGRITLSLLDALEIPWEVLSTDNDEALAQIERALAHAlATSRPYALVVRKGTFASYKL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387289096 168 NKNNE-PNAGLPKRGELIETVLNTCAGDTAFIATTGFTGRELSQIKD-----GANNFYMVGSLGCASSLALGLSLAKPSQ 241
Cdd:TIGR03297 161 KGGPAnPYATLMTREEAIAAILDHLPDNTVIVSTTGKTSRELYELRDrigqgHARDFLTVGSMGHASQIALGLALARPDQ 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387289096 242 KVVVFDGDSALLMRMGALAVNAYYAPKNFCHIVFDNQAHESTGGQFNVSCNMDYEGLAKSCGYKTVKTVATKDELQSLLA 321
Cdd:TIGR03297 241 RVVCLDGDGAALMHMGGLATIGTQGPANLIHVLFNNGAHDSVGGQPTVSQHLDFAQIAKACGYAKVYEVSTLEELETALT 320

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 1387289096 322 DWNANGGMMFIHAKIAQGTLENLERPKTKPREVAKRFSTYI 362
Cdd:TIGR03297 321 AASSANGPRLIEVKVRPGSRADLGRPTTSPPENKRRFMRFL 361
TPP_PpyrDC cd03371
Thiamine pyrophosphate (TPP) family, PpyrDC subfamily, TPP-binding module; composed of ...
 180-361 6.94e-70

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: 216.80  E-value: 6.94e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387289096 180 RGELIETVLNTCAGDTAFIATTGFTGRELSQIKD-----GANNFYMVGSLGCASSLALGLSLAKPSQKVVVFDGDSALLM 254
Cdd:cd03371     1 REDAIEIVLSRAPATAAVVSTTGMTSRELFELRDrpgggHAQDFLTVGSMGHASQIALGIALARPDRKVVCIDGDGAALM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387289096 255 RMGALAVNAYYAPKNFCHIVFDNQAHESTGGQFNVSCNMDYEGLAKSCGYKTVKTVATKDELQSLLADWNANGGMMFIHA 334
Cdd:cd03371    81 HMGGLATIGGLAPANLIHIVLNNGAHDSVGGQPTVSFDVSLPAIAKACGYRAVYEVPSLEELVAALAKALAADGPAFIEV 160

                         170       180
                  ....*....|....*....|....*..
gi 1387289096 335 KIAQGTLENLERPKTKPREVAKRFSTY 361
Cdd:cd03371   161 KVRPGSRSDLGRPTTSPIENKERFMAF 187
COG4032 COG4032
Sulfopyruvate decarboxylase, TPP-binding subunit (coenzyme M biosynthesis) [Coenzyme transport ...
 11-146 8.59e-53

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


Pssm-ID: 443210  Cd Length: 168  Bit Score: 172.32  E-value: 8.59e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387289096  11 LKQKGYTFYSGVPCSFLKDLINYAINECE--YVMAANEGDAAAICAGASLAGKKNVLLMQNSGLGNAVSPLTSLNKVFDI 88
Cdd:COG4032    11 LKEAGIDFVAYVPCSVLKPLINLLEADPDirHVPVTREEEAVGIAAGAYLGGKRPVVLMQNSGLGNSINALASLNLTYRI 90

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1387289096  89 PVLGFVSLRGEQGiPDEPQHELMGRITEAMLATMEIDWDYLSADfEEAQKQLEKADDY 146
Cdd:COG4032    91 PLLMLVSWRGEPG-EDNPAQVPMGRITPPLLDAMGIPYFVLDTP-EDVEPVIARAIEH 146
PRK06163 PRK06163
hypothetical protein; Provisional
 194-336 3.29e-23

hypothetical protein; Provisional


Pssm-ID: 235721 [Multi-domain]  Cd Length: 202  Bit Score: 95.67  E-value: 3.29e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387289096 194 DTAFIATTGFTGRELSQIKDGANNFYMVGSLGCASSLALGLSLAKPSQKVVVFDGDSALLMRMGALAVNAYYAPKNFCHI 273
Cdd:PRK06163   29 EEAVIGGIGNTNFDLWAAGQRPQNFYMLGSMGLAFPIALGVALAQPKRRVIALEGDGSLLMQLGALGTIAALAPKNLTII 108

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1387289096 274 VFDNQAHESTGGQFNVSCN-MDYEGLAKSCGYKTVKTVATKDELQSLLADWNANGGMMFIHAKI 336
Cdd:PRK06163  109 VMDNGVYQITGGQPTLTSQtVDVVAIARGAGLENSHWAADEAHFEALVDQALSGPGPSFIAVRI 172
TPP_enzyme_C pfam02775
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
222-334 2.16e-15

Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;


Pssm-ID: 460689 [Multi-domain]  Cd Length: 151  Bit Score: 72.62  E-value: 2.16e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387289096 222 GSLGCASSLALGLSLAKPSQKVVVFDGDSALLMRMGALAVNAYYAPkNFCHIVFDNQAHESTGGQ-------------FN 288
Cdd:pfam02775  28 GTMGYGLPAAIGAKLARPDRPVVAIAGDGGFQMNLQELATAVRYNL-PITVVVLNNGGYGMTRGQqtpfgggrysgpsGK 106

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1387289096 289 VSCNMDYEGLAKSCGYKtVKTVATKDELQSLLADWNANGGMMFIHA 334
Cdd:pfam02775 107 ILPPVDFAKLAEAYGAK-GARVESPEELEEALKEALEHDGPALIDV 151
 
Name Accession Description Interval E-value
Ppyr-DeCO2ase TIGR03297
phosphonopyruvate decarboxylase; This family consists of examples of phosphonopyruvate an ...
 15-362 2.21e-141

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: 405.59  E-value: 2.21e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387289096  15 GYTFYSGVPCSFLKDLINYAINECE---YVMAANEGDAAAICAGASLA-GKKNVLLMQNSGLGNAVSPLTSL--NKVFDI 88
Cdd:TIGR03297   1 GFDFFSGVPDSLLKPFCNYITDNNRdlrHVIAANEGAAVGLAAGAYLAtGKRAAVYMQNSGLGNAVNPLTSLadTEVYDI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387289096  89 PVLGFVSLRGEQGIPDEPQHELMGRITEAMLATMEIDWDYLSADFEEAQKQLEKADDYI-NANKSFFFVVRKNTFSKVLL 167
Cdd:TIGR03297  81 PLLLIVGWRGEPGVHDEPQHVKQGRITLSLLDALEIPWEVLSTDNDEALAQIERALAHAlATSRPYALVVRKGTFASYKL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387289096 168 NKNNE-PNAGLPKRGELIETVLNTCAGDTAFIATTGFTGRELSQIKD-----GANNFYMVGSLGCASSLALGLSLAKPSQ 241
Cdd:TIGR03297 161 KGGPAnPYATLMTREEAIAAILDHLPDNTVIVSTTGKTSRELYELRDrigqgHARDFLTVGSMGHASQIALGLALARPDQ 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387289096 242 KVVVFDGDSALLMRMGALAVNAYYAPKNFCHIVFDNQAHESTGGQFNVSCNMDYEGLAKSCGYKTVKTVATKDELQSLLA 321
Cdd:TIGR03297 241 RVVCLDGDGAALMHMGGLATIGTQGPANLIHVLFNNGAHDSVGGQPTVSQHLDFAQIAKACGYAKVYEVSTLEELETALT 320

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 1387289096 322 DWNANGGMMFIHAKIAQGTLENLERPKTKPREVAKRFSTYI 362
Cdd:TIGR03297 321 AASSANGPRLIEVKVRPGSRADLGRPTTSPPENKRRFMRFL 361
TPP_PpyrDC cd03371
Thiamine pyrophosphate (TPP) family, PpyrDC subfamily, TPP-binding module; composed of ...
 180-361 6.94e-70

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: 216.80  E-value: 6.94e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387289096 180 RGELIETVLNTCAGDTAFIATTGFTGRELSQIKD-----GANNFYMVGSLGCASSLALGLSLAKPSQKVVVFDGDSALLM 254
Cdd:cd03371     1 REDAIEIVLSRAPATAAVVSTTGMTSRELFELRDrpgggHAQDFLTVGSMGHASQIALGIALARPDRKVVCIDGDGAALM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387289096 255 RMGALAVNAYYAPKNFCHIVFDNQAHESTGGQFNVSCNMDYEGLAKSCGYKTVKTVATKDELQSLLADWNANGGMMFIHA 334
Cdd:cd03371    81 HMGGLATIGGLAPANLIHIVLNNGAHDSVGGQPTVSFDVSLPAIAKACGYRAVYEVPSLEELVAALAKALAADGPAFIEV 160

                         170       180
                  ....*....|....*....|....*..
gi 1387289096 335 KIAQGTLENLERPKTKPREVAKRFSTY 361
Cdd:cd03371   161 KVRPGSRSDLGRPTTSPIENKERFMAF 187
COG4032 COG4032
Sulfopyruvate decarboxylase, TPP-binding subunit (coenzyme M biosynthesis) [Coenzyme transport ...
 11-146 8.59e-53

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


Pssm-ID: 443210  Cd Length: 168  Bit Score: 172.32  E-value: 8.59e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387289096  11 LKQKGYTFYSGVPCSFLKDLINYAINECE--YVMAANEGDAAAICAGASLAGKKNVLLMQNSGLGNAVSPLTSLNKVFDI 88
Cdd:COG4032    11 LKEAGIDFVAYVPCSVLKPLINLLEADPDirHVPVTREEEAVGIAAGAYLGGKRPVVLMQNSGLGNSINALASLNLTYRI 90

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1387289096  89 PVLGFVSLRGEQGiPDEPQHELMGRITEAMLATMEIDWDYLSADfEEAQKQLEKADDY 146
Cdd:COG4032    91 PLLMLVSWRGEPG-EDNPAQVPMGRITPPLLDAMGIPYFVLDTP-EDVEPVIARAIEH 146
TPP_ComE_PpyrDC cd02001
Thiamine pyrophosphate (TPP) family, ComE and PpyrDC subfamily, TPP-binding module; composed ...
 180-339 7.94e-43

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: 146.09  E-value: 7.94e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387289096 180 RGELIEtVLNTCAGDTAFIATTGFTGRELSQIKDGANNFYMVGSLGCASSLALGLSLAKPsQKVVVFDGDSALLMRMGAL 259
Cdd:cd02001     1 RIAAIA-EIIEASGDTPIVSTTGYASRELYDVQDRDGHFYMLGSMGLAGSIGLGLALGLS-RKVIVVDGDGSLLMNPGVL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387289096 260 AVNAYYAPKNFCHIVFDNQAHESTGGQFNVSCNMDYEGLAKSCGYKTVKTvATKDELQSLLADWNANGGMMFIHAKIAQG 339
Cdd:cd02001    79 LTAGEFTPLNLILVVLDNRAYGSTGGQPTPSSNVNLEAWAAACGYLVLSA-PLLGGLGSEFAGLLATTGPTLLHAPIAPG 157
TPP_ComE cd03372
Thiamine pyrophosphate (TPP) family, ComE subfamily, TPP-binding module; composed of proteins ...
 180-358 9.24e-41

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: 141.66  E-value: 9.24e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387289096 180 RGELIETVLnTCAGDTAFIATTGFTGRELSQIKDGANNFYMVGSLGCASSLALGLSLAKPsQKVVVFDGDSALLMRMGAL 259
Cdd:cd03372     1 RRDAIKTLI-ADLKDELVVSNIGFPSKELYAAGDRPLNFYMLGSMGLASSIGLGLALAQP-RKVIVIDGDGSLLMNLGAL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387289096 260 AVNAYYAPKNFCHIVFDNQAHESTGGQFN-VSCNMDYEGLAKSCGYKTVKTVATKDELQSLLADwnANGGMMFIHAKIAQ 338
Cdd:cd03372    79 ATIAAEKPKNLIIVVLDNGAYGSTGNQPThAGKKTDLEAVAKACGLDNVATVASEEAFEKAVEQ--ALDGPSFIHVKIKP 156

                         170       180
                  ....*....|....*....|..
gi 1387289096 339 GtleNLERPKTK--PREVAKRF 358
Cdd:cd03372   157 G---NTDVPNIPrdPVEIKNRF 175
sulfopyru_alph TIGR03845
sulfopyruvate decarboxylase, alpha subunit; This model represents the alpha subunit, or the ...
 9-146 3.24e-29

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: 110.44  E-value: 3.24e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387289096   9 NFLKQKGYTFYSGVPCSFLKDLINYAINECEYVMAANEGDAAAICAGASLAGKKNVLLMQNSGLGNAVSPLTSLNKVFDI 88
Cdd:TIGR03845   6 NILKDAGIDLVASVPCDNLKNLLPLIEKDFRHIPLTREEEGVGICAGAYLAGKKPAILMQSSGLGNSINALASLNKTYGI 85

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1387289096  89 PVLGFVSLRGEQG------IPdepqhelMGRITEAMLATMEIdwDYLSADFEEAQKQLEKADDY 146
Cdd:TIGR03845  86 PLPILASWRGVYKekipaqIP-------MGRATPKLLDTLGI--PYTIPREPEEAKLIEKAISD 140
PRK06163 PRK06163
hypothetical protein; Provisional
 194-336 3.29e-23

hypothetical protein; Provisional


Pssm-ID: 235721 [Multi-domain]  Cd Length: 202  Bit Score: 95.67  E-value: 3.29e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387289096 194 DTAFIATTGFTGRELSQIKDGANNFYMVGSLGCASSLALGLSLAKPSQKVVVFDGDSALLMRMGALAVNAYYAPKNFCHI 273
Cdd:PRK06163   29 EEAVIGGIGNTNFDLWAAGQRPQNFYMLGSMGLAFPIALGVALAQPKRRVIALEGDGSLLMQLGALGTIAALAPKNLTII 108

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1387289096 274 VFDNQAHESTGGQFNVSCN-MDYEGLAKSCGYKTVKTVATKDELQSLLADWNANGGMMFIHAKI 336
Cdd:PRK06163  109 VMDNGVYQITGGQPTLTSQtVDVVAIARGAGLENSHWAADEAHFEALVDQALSGPGPSFIAVRI 172
TPP_PYR_POX_like cd07035
Pyrimidine (PYR) binding domain of POX and related proteins; Thiamine pyrophosphate (TPP ...
 10-143 1.25e-16

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: 76.03  E-value: 1.25e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387289096  10 FLKQKGYTFYSGVPCSFLKDLINYAIN-ECEYVMAANEGDAAAICAGASLA-GKKNVLLMQ-NSGLGNAVSPLTSLNKvf 86
Cdd:cd07035     6 ALKAEGVDHVFGVPGGAILPLLDALARsGIRYILVRHEQGAVGMADGYARAtGKPGVVLVTsGPGLTNAVTGLANAYL-- 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1387289096  87 D-IPVLGFVSLRGEQGIP-----DEPQHELMGRITeamLATMEIDwdylsaDFEEAQKQLEKA 143
Cdd:cd07035    84 DsIPLLVITGQRPTAGEGrgafqEIDQVALFRPIT---KWAYRVT------SPEEIPEALRRA 137
TPP_enzyme_C pfam02775
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
222-334 2.16e-15

Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;


Pssm-ID: 460689 [Multi-domain]  Cd Length: 151  Bit Score: 72.62  E-value: 2.16e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387289096 222 GSLGCASSLALGLSLAKPSQKVVVFDGDSALLMRMGALAVNAYYAPkNFCHIVFDNQAHESTGGQ-------------FN 288
Cdd:pfam02775  28 GTMGYGLPAAIGAKLARPDRPVVAIAGDGGFQMNLQELATAVRYNL-PITVVVLNNGGYGMTRGQqtpfgggrysgpsGK 106

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1387289096 289 VSCNMDYEGLAKSCGYKtVKTVATKDELQSLLADWNANGGMMFIHA 334
Cdd:pfam02775 107 ILPPVDFAKLAEAYGAK-GARVESPEELEEALKEALEHDGPALIDV 151
TPP_enzymes cd00568
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ...
 216-336 1.09e-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: 68.44  E-value: 1.09e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387289096 216 NNFYMVGSLGCASSLALGLSLAKPSQKVVVFDGDSALLMRMGALAVnAYYAPKNFCHIVFDNQAHESTGGQFNVSC---- 291
Cdd:cd00568    40 LTSTGFGAMGYGLPAAIGAALAAPDRPVVCIAGDGGFMMTGQELAT-AVRYGLPVIVVVFNNGGYGTIRMHQEAFYggrv 118

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1387289096 292 ------NMDYEGLAKSCGYKTVkTVATKDELQSLLADWNANGGMMFIHAKI 336
Cdd:cd00568   119 sgtdlsNPDFAALAEAYGAKGV-RVEDPEDLEAALAEALAAGGPALIEVKT 168
IlvB COG0028
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino ...
 222-336 2.52e-10

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: 61.71  E-value: 2.52e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387289096 222 GSLGCASSLALGLSLAKPSQKVVVFDGDSALLMRMGALAVNAYYAPkNFCHIVFDNQA------HESTGGQFNVSC---- 291
Cdd:COG0028   412 GTMGYGLPAAIGAKLARPDRPVVAITGDGGFQMNLQELATAVRYGL-PVKVVVLNNGGlgmvrqWQELFYGGRYSGtdlp 490

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1387289096 292 NMDYEGLAKSCGYKTVkTVATKDELQSLLADWNANGGMMFIHAKI 336
Cdd:COG0028   491 NPDFAKLAEAFGAKGE-RVETPEELEAALEEALASDGPALIDVRV 534
TPP_IOR_alpha cd02008
Thiamine pyrophosphate (TPP) family, IOR-alpha subfamily, TPP-binding module; composed of ...
 223-321 6.25e-09

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: 54.98  E-value: 6.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387289096 223 SLGCASSLALGLSLAKPSQKVVVFDGDSALLmRMGALAV-NAYYAPKNFCHIVFDNQAHESTGGQFNVSC---------N 292
Cdd:cd02008    52 CMGASIGVAIGMAKASEDKKVVAVIGDSTFF-HSGILGLiNAVYNKANITVVILDNRTTAMTGGQPHPGTgktltepttV 130

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1387289096 293 MDYEGLAKSCGYKTVKTV------ATKDELQSLLA 321
Cdd:cd02008   131 IDIEALVRAIGVKRVVVVdpydlkAIREELKEALA 165
TPP_AHAS cd02015
Thiamine pyrophosphate (TPP) family, Acetohydroxyacid synthase (AHAS) subfamily, TPP-binding ...
 222-337 1.39e-07

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: 50.96  E-value: 1.39e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387289096 222 GSLGCASSLALGLSLAKPSQKVVVFDGDSALLMRMGALAVNAYY-AP-KNfchIVFDNQA-----------HESTGGQFN 288
Cdd:cd02015    50 GTMGFGLPAAIGAKVARPDKTVICIDGDGSFQMNIQELATAAQYnLPvKI---VILNNGSlgmvrqwqelfYEGRYSHTT 126

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1387289096 289 VSCNMDYEGLAKSCGYKTVkTVATKDELQSLLADWNANGGMMFIHAKIA 337
Cdd:cd02015   127 LDSNPDFVKLAEAYGIKGL-RVEKPEELEAALKEALASDGPVLLDVLVD 174
TPP_POX cd02014
Thiamine pyrophosphate (TPP) family, Pyruvate oxidase (POX) subfamily, TPP-binding module; ...
 222-336 1.99e-06

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: 47.53  E-value: 1.99e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387289096 222 GSLGCASSLALGLSLAKPSQKVVVFDGDSALLMRMGALAVNAYYAP--KNfchIVFDNQA-------HESTG-GQFNVSC 291
Cdd:cd02014    51 ATMGNGLPGAIAAKLAYPDRQVIALSGDGGFAMLMGDLITAVKYNLpvIV---VVFNNSDlgfikweQEVMGqPEFGVDL 127

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1387289096 292 -NMDYEGLAKSCGYKTVkTVATKDELQSLLADWNANGGMMFIHAKI 336
Cdd:cd02014   128 pNPDFAKIAEAMGIKGI-RVEDPDELEAALDEALAADGPVVIDVVT 172
TPP_BZL_OCoD_HPCL cd02004
Thiamine pyrophosphate (TPP) family, BZL_OCoD_HPCL subfamily, TPP-binding module; composed of ...
 192-337 4.96e-05

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: 43.29  E-value: 4.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387289096 192 AGDTAFIATTGFTGRELSQIKDGANNfymvGSLGCASSLALGLSLAKPSQKVVVFDGDSALLM-----------RMGALA 260
Cdd:cd02004    22 GGNTMDWARYILRPRKPRHRLDAGTF----GTLGVGLGYAIAAALARPDKRVVLVEGDGAFGFsgmeletavryNLPIVV 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387289096 261 V--NayyapkNFC--HIVFDNQahESTGGQFNVSCNM---DYEGLAKSCGYKTVKtVATKDELQSLLADWNANGGMMFIH 333
Cdd:cd02004    98 VvgN------NGGwyQGLDGQQ--LSYGLGLPVTTLLpdtRYDLVAEAFGGKGEL-VTTPEELKPALKRALASGKPALIN 168


                  ....
gi 1387289096 334 AKIA 337
Cdd:cd02004   169 VIID 172
TPP_BFDC cd02002
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins ...
 222-316 5.35e-04

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: 40.27  E-value: 5.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387289096 222 GSLGCASSLALGLSLAKPSQKVVVFDGDSALLMRMGAL--AVnAYYAPKNFchIVFDN----------QAHESTGGQFNV 289
Cdd:cd02002    49 GGLGWGLPAAVGAALANPDRKVVAIIGDGSFMYTIQALwtAA-RYGLPVTV--VILNNrgygalrsflKRVGPEGPGENA 125

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1387289096 290 -------SCNMDYEGLAKSCGYkTVKTVATKDEL 316
Cdd:cd02002   126 pdgldllDPGIDFAAIAKAFGV-EAERVETPEEL 158
PRK07418 PRK07418
acetolactate synthase large subunit;
222-343 9.97e-04

acetolactate synthase large subunit;


Pssm-ID: 236014 [Multi-domain]  Cd Length: 616  Bit Score: 41.19  E-value: 9.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387289096 222 GSLGCASSLALGLSLAKPSQKVVVFDGDSALLMRMGALAVNAYYApKNFCHIVFDN-------QAHESTGGQFNVSCNM- 293
Cdd:PRK07418  434 GTMGFGMPAAMGVKVALPDEEVICIAGDASFLMNIQELGTLAQYG-INVKTVIINNgwqgmvrQWQESFYGERYSASNMe 512

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1387289096 294 ----DYEGLAKSCGYKTVkTVATKDELQSLLADWNANGGMMFIHAKIAQGtlEN 343
Cdd:PRK07418  513 pgmpDFVKLAEAFGVKGM-VISERDQLKDAIAEALAHDGPVLIDVHVRRD--EN 563
PRK06456 PRK06456
acetolactate synthase large subunit;
221-278 6.11e-03

acetolactate synthase large subunit;


Pssm-ID: 180569 [Multi-domain]  Cd Length: 572  Bit Score: 38.67  E-value: 6.11e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1387289096 221 VGSLGCASSLALGLSLAKPSQKVVVFDGDSALLMRMGALAVNA-YYAPknFCHIVFDNQ 278
Cdd:PRK06456  420 MGTMGFGLPAAMGAKLARPDKVVVDLDGDGSFLMTGTNLATAVdEHIP--VISVIFDNR 476
PRK08527 PRK08527
acetolactate synthase large subunit;
222-336 6.34e-03

acetolactate synthase large subunit;


Pssm-ID: 181458 [Multi-domain]  Cd Length: 563  Bit Score: 38.54  E-value: 6.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387289096 222 GSLGCASSLALGLSLAKPSQKVVVFDGDSALLMRMGALaVNAYYAPKNFCHIVFDNQA-----------HESTGGQFNVS 290
Cdd:PRK08527  414 GTMGYGLPAALGAKLAVPDKVVINFTGDGSILMNIQEL-MTAVEYKIPVINIILNNNFlgmvrqwqtffYEERYSETDLS 492

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1387289096 291 CNMDYEGLAKSCGYKTVKtVATKDELQSLLADWNANGGMMFIHAKI 336
Cdd:PRK08527  493 TQPDFVKLAESFGGIGFR-VTTKEEFDKALKEALESDKVALIDVKI 537
 
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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