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Conserved domains on  [gi|1093259993|emb|SEH77300|]
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2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase [Stutzerimonas xanthomarina]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MenD super family cl34155
2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase [Coenzyme transport ...
 11-557 2.23e-120

2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase [Coenzyme transport and metabolism]; 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase is part of the Pathway/BioSystem: Menaquinone biosynthesis


The actual alignment was detected with superfamily member COG1165:

Pssm-ID: 440779 [Multi-domain]  Cd Length: 567  Bit Score: 367.57  E-value: 2.23e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093259993  11 KNAQVILYLLKAHNIRHVIASPGTTNTALVSSMQQDPHFIMYSSVDERSAAYMACGLAAELNEPVVISCTGATASRNYLP 90
Cdd:COG1165     8 LWARVLVEELVRLGVRHVVISPGSRSTPLTLAFARHPDLRLHSHVDERSAAFFALGLAKASGRPVALVCTSGTAAANYYP 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093259993  91 GMTEAFYRKLPVLAITSMQAFSRVGHHVAQVIDRSSMPKDAVTLSVELPIVKDDED-VWDCEIKVNKAILELKRHGGGPV 169
Cdd:COG1165    88 AVIEAFYSGVPLIVLTADRPPELRDCGANQTIDQVGLFGNHVRWSADLPLPEADPDaLRYLRRTINRALAAALGPPPGPV 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093259993 170 HINLP--------------TTYSKPYdVKQLPDYRVIERISEQDRFPELgtPDHRKIAVFVGAHKTwSKAETEALESFCE 235
Cdd:COG1165   168 HINVPfreplypdpdeedpLAAGGPW-IRVTPPEPAPSPEALAQLADEL--ERAKRGLIVAGPLPP-PEELAEALAALAE 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093259993 236 QYGAVVFCDHSSGYQGKNR-----LLFALAAAQTMLdkspcQPDVLIHIGEVTGDYATLGM----AGRQVWRVSEDGEIR 306
Cdd:COG1165   244 ALGWPVLADPLSNLRHPNVistydLLLRNPEFAELL-----QPDLVIRFGGPPVSKRLKQFlrrhPPAEHWVVDPSGEWR 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093259993 307 DTFRKLRYVFAMPEQAFFAHYAGQAagqAPVNAGYYEQCRQQ----LQAIRDNLPELPLSNAWLASQLAHRIPAGSTIHF 382
Cdd:COG1165   319 DPFHSLTRVIEADPEAFLEALAERL---PPADSAWLARWLAAeqkaRAAIDEYLAEDPLSEGAVARRLLEALPEGSTLFV 395

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093259993 383 GILNSLRCWNFY--ELPASVTAASNVGGFGIDGGLSSLIGASLANPNKLYfAVIGDLAFFYDLNVLGN-RHAGNNLRILL 459
Cdd:COG1165   396 GNSMPVRDLDLFarPLPKGVRVYANRGASGIDGTVSTALGAALASGKPTV-LLTGDLSFLHDLNGLLLlYELPPNLTIVV 474

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093259993 460 VNNGKGTEFRQ--YNHHAAYFgegaEEFvaasghFGCKSPTLVKNFATDLGYEYLAATSKEEFAVHYQRFIAPEvggKSI 537
Cdd:COG1165   475 VNNDGGGIFSMlpGAKFEPEF----ERF------FGTPHGLDFEHLAAMYGLDYARVSSWEELREALAEFLPSD---GPR 541

                         570       580
                  ....*....|....*....|
gi 1093259993 538 IFEVFTDSELESQALESIQN 557
Cdd:COG1165   542 VLEVRTDREENAELLKALFA 561
 
Name Accession Description Interval E-value
MenD COG1165
2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase [Coenzyme transport ...
 11-557 2.23e-120

2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase [Coenzyme transport and metabolism]; 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440779 [Multi-domain]  Cd Length: 567  Bit Score: 367.57  E-value: 2.23e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093259993  11 KNAQVILYLLKAHNIRHVIASPGTTNTALVSSMQQDPHFIMYSSVDERSAAYMACGLAAELNEPVVISCTGATASRNYLP 90
Cdd:COG1165     8 LWARVLVEELVRLGVRHVVISPGSRSTPLTLAFARHPDLRLHSHVDERSAAFFALGLAKASGRPVALVCTSGTAAANYYP 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093259993  91 GMTEAFYRKLPVLAITSMQAFSRVGHHVAQVIDRSSMPKDAVTLSVELPIVKDDED-VWDCEIKVNKAILELKRHGGGPV 169
Cdd:COG1165    88 AVIEAFYSGVPLIVLTADRPPELRDCGANQTIDQVGLFGNHVRWSADLPLPEADPDaLRYLRRTINRALAAALGPPPGPV 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093259993 170 HINLP--------------TTYSKPYdVKQLPDYRVIERISEQDRFPELgtPDHRKIAVFVGAHKTwSKAETEALESFCE 235
Cdd:COG1165   168 HINVPfreplypdpdeedpLAAGGPW-IRVTPPEPAPSPEALAQLADEL--ERAKRGLIVAGPLPP-PEELAEALAALAE 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093259993 236 QYGAVVFCDHSSGYQGKNR-----LLFALAAAQTMLdkspcQPDVLIHIGEVTGDYATLGM----AGRQVWRVSEDGEIR 306
Cdd:COG1165   244 ALGWPVLADPLSNLRHPNVistydLLLRNPEFAELL-----QPDLVIRFGGPPVSKRLKQFlrrhPPAEHWVVDPSGEWR 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093259993 307 DTFRKLRYVFAMPEQAFFAHYAGQAagqAPVNAGYYEQCRQQ----LQAIRDNLPELPLSNAWLASQLAHRIPAGSTIHF 382
Cdd:COG1165   319 DPFHSLTRVIEADPEAFLEALAERL---PPADSAWLARWLAAeqkaRAAIDEYLAEDPLSEGAVARRLLEALPEGSTLFV 395

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093259993 383 GILNSLRCWNFY--ELPASVTAASNVGGFGIDGGLSSLIGASLANPNKLYfAVIGDLAFFYDLNVLGN-RHAGNNLRILL 459
Cdd:COG1165   396 GNSMPVRDLDLFarPLPKGVRVYANRGASGIDGTVSTALGAALASGKPTV-LLTGDLSFLHDLNGLLLlYELPPNLTIVV 474

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093259993 460 VNNGKGTEFRQ--YNHHAAYFgegaEEFvaasghFGCKSPTLVKNFATDLGYEYLAATSKEEFAVHYQRFIAPEvggKSI 537
Cdd:COG1165   475 VNNDGGGIFSMlpGAKFEPEF----ERF------FGTPHGLDFEHLAAMYGLDYARVSSWEELREALAEFLPSD---GPR 541

                         570       580
                  ....*....|....*....|
gi 1093259993 538 IFEVFTDSELESQALESIQN 557
Cdd:COG1165   542 VLEVRTDREENAELLKALFA 561
TPP_PYR_MenD cd07037
Pyrimidine (PYR) binding domain of ...
 14-175 4.63e-64

Pyrimidine (PYR) binding domain of 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexadiene-1-carboxylate synthase (MenD) and related proteins; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) binding domain of 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexadiene-1-carboxylate (SEPHCHC) synthase (MenD) 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. 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. Escherichia coli MenD (EcMenD) is a homotetramer (dimer-of-homodimers), having two active sites per homodimer lying between PYR and PP domains of different subunits. EcMenD catalyzes a Stetter-like conjugate addition of alpha-ketoglutarate to isochorismate, leading to the formation of SEPHCHC and carbon dioxide, this addition is the first committed step in the biosynthesis of vitamin K2 (menaquinone).


Pssm-ID: 132920 [Multi-domain]  Cd Length: 162  Bit Score: 207.35  E-value: 4.63e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093259993  14 QVILYLLKAHNIRHVIASPGTTNTALVSSMQQDPHFIMYSSVDERSAAYMACGLAAELNEPVVISCTGATASRNYLPGMT 93
Cdd:cd07037     1 QALVEELKRLGVRDVVISPGSRSAPLALAAAEHPEFRLHVRVDERSAAFFALGLAKASGRPVAVVCTSGTAVANLLPAVV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093259993  94 EAFYRKLPVLAITSMQAFSRVGHHVAQVIDRSSMPKDAVTLSVELPIVKDDEDVWDCEIKVNKAILELKRHGGGPVHINL 173
Cdd:cd07037    81 EAYYSGVPLLVLTADRPPELRGTGANQTIDQVGLFGDYVRWSVDLPPPEDDDDLWYLLRLANRAVLEALSAPPGPVHLNL 160


                  ..
gi 1093259993 174 PT 175
Cdd:cd07037   161 PF 162
TPP_enzyme_N pfam02776
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain;
13-174 2.97e-19

Thiamine pyrophosphate enzyme, N-terminal TPP binding domain;


Pssm-ID: 460690 [Multi-domain]  Cd Length: 169  Bit Score: 85.36  E-value: 2.97e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093259993  13 AQVILYLLKAHNIRHVIASPGTTNTALVSSMQQDPHFIMYSSVDERSAAYMACGLAAELNEPVVISCTGATASRNYLPGM 92
Cdd:pfam02776   2 AEALADVLKALGVDTVFGVPGGHILPLLDALAKSPGIRYVLTRHEQGAAFAADGYARATGKPGVVLVTSGPGATNALTGL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093259993  93 TEAFYRKLPVLAITSMQAFSRVGHHVAQ-VIDRSSMPKDAVTLSVELPIVKDDEDVwdceikVNKAILELKRHGGGPVHI 171
Cdd:pfam02776  82 ANAYVDSVPLLVISGQRPRSLVGRGALQqELDQLALFRPVTKWAVRVTSADEIPEV------LRRAFRAALSGRPGPVYL 155


                  ...
gi 1093259993 172 NLP 174
Cdd:pfam02776 156 EIP 158
PLN02980 PLN02980
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate ...
 31-469 1.51e-05

2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate binding


Pssm-ID: 215530 [Multi-domain]  Cd Length: 1655  Bit Score: 48.31  E-value: 1.51e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093259993   31 SPGTTNTALVSSMQQDPHFIMYSSVDERSAAYMACGLAAELNEPVVISCTGATASRNYLPGMTEAFYRKLPVLAITSMQA 110
Cdd:PLN02980   322 APGSRSSPLAIAASNHPLTTCIACFDERSLAFHALGYARGSLKPAVVITSSGTAVSNLLPAVVEASQDFVPLLLLTADRP 401

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093259993  111 FSRVGHHVAQVIDRSSMPKDAVTLSVELPIVKDDEDVWDCEIKVNKAILELKRHGGGPVHINLP---------------- 174
Cdd:PLN02980   402 PELQDAGANQAINQVNHFGSFVRFFFNLPPPTDLIPARMVLTTLDSAVHWATSSPCGPVHINCPfrepldgsptnwmssc 481

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093259993  175 --------------TTYSKPYDVKQLPDYR-----VIERISEQDR----FPELGTPDHRKIAVFVGAHKTWSKAET---- 227
Cdd:PLN02980   482 lkgldmwmsnaepfTKYIQMQSSKADGDTTgqiteVLEVIQEAKRglllIGAIHTEDDIWAALLLAKHLMWPVVADilsg 561

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093259993  228 ----EALESFCEQYGAVVFCDH----------------------SSGYQGKNRLLF---ALAAAQTMLDKSPCQPD---V 275
Cdd:PLN02980   562 lrlrKLFKSFPEFELNILFVDHldhallsdsvrnwiqfdvviqiGSRITSKRVSQMlekCFPFSYILVDKHPCRHDpshL 641

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093259993  276 LIH-IGEVTGDYATLGMAGRQVWRVSE--------DGEIRDTFRKLRYVFAMPEQAFFAHYAGQA-AGQAPVNAGyyeqc 345
Cdd:PLN02980   642 VTHrVQSNIVQFADCLLKAQFPRRRSKwhghlqalDGMVAQEISFQIHAESSLTEPYVAHVISEAlTSDSALFIG----- 716

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093259993  346 rqQLQAIRDnlpelplSNAWLASQLAHRIPAGSTihfgILNSlrcwnfyELPASVTA-ASNVGGFGIDGGLSSLIGASLA 424
Cdd:PLN02980   717 --NSMAIRD-------ADMYGCSSENYSSRIVDM----MLSA-------ELPCQWIQvAGNRGASGIDGLLSTAIGFAVG 776

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*...
gi 1093259993  425 NpNKLYFAVIGDLAFFYDLN---VLGNRHAGNNLRILLVNNGKGTEFR 469
Cdd:PLN02980   777 C-NKRVLCVVGDISFLHDTNglsILSQRIARKPMTILVINNHGGAIFS 823
 
Name Accession Description Interval E-value
MenD COG1165
2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase [Coenzyme transport ...
 11-557 2.23e-120

2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase [Coenzyme transport and metabolism]; 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440779 [Multi-domain]  Cd Length: 567  Bit Score: 367.57  E-value: 2.23e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093259993  11 KNAQVILYLLKAHNIRHVIASPGTTNTALVSSMQQDPHFIMYSSVDERSAAYMACGLAAELNEPVVISCTGATASRNYLP 90
Cdd:COG1165     8 LWARVLVEELVRLGVRHVVISPGSRSTPLTLAFARHPDLRLHSHVDERSAAFFALGLAKASGRPVALVCTSGTAAANYYP 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093259993  91 GMTEAFYRKLPVLAITSMQAFSRVGHHVAQVIDRSSMPKDAVTLSVELPIVKDDED-VWDCEIKVNKAILELKRHGGGPV 169
Cdd:COG1165    88 AVIEAFYSGVPLIVLTADRPPELRDCGANQTIDQVGLFGNHVRWSADLPLPEADPDaLRYLRRTINRALAAALGPPPGPV 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093259993 170 HINLP--------------TTYSKPYdVKQLPDYRVIERISEQDRFPELgtPDHRKIAVFVGAHKTwSKAETEALESFCE 235
Cdd:COG1165   168 HINVPfreplypdpdeedpLAAGGPW-IRVTPPEPAPSPEALAQLADEL--ERAKRGLIVAGPLPP-PEELAEALAALAE 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093259993 236 QYGAVVFCDHSSGYQGKNR-----LLFALAAAQTMLdkspcQPDVLIHIGEVTGDYATLGM----AGRQVWRVSEDGEIR 306
Cdd:COG1165   244 ALGWPVLADPLSNLRHPNVistydLLLRNPEFAELL-----QPDLVIRFGGPPVSKRLKQFlrrhPPAEHWVVDPSGEWR 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093259993 307 DTFRKLRYVFAMPEQAFFAHYAGQAagqAPVNAGYYEQCRQQ----LQAIRDNLPELPLSNAWLASQLAHRIPAGSTIHF 382
Cdd:COG1165   319 DPFHSLTRVIEADPEAFLEALAERL---PPADSAWLARWLAAeqkaRAAIDEYLAEDPLSEGAVARRLLEALPEGSTLFV 395

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093259993 383 GILNSLRCWNFY--ELPASVTAASNVGGFGIDGGLSSLIGASLANPNKLYfAVIGDLAFFYDLNVLGN-RHAGNNLRILL 459
Cdd:COG1165   396 GNSMPVRDLDLFarPLPKGVRVYANRGASGIDGTVSTALGAALASGKPTV-LLTGDLSFLHDLNGLLLlYELPPNLTIVV 474

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093259993 460 VNNGKGTEFRQ--YNHHAAYFgegaEEFvaasghFGCKSPTLVKNFATDLGYEYLAATSKEEFAVHYQRFIAPEvggKSI 537
Cdd:COG1165   475 VNNDGGGIFSMlpGAKFEPEF----ERF------FGTPHGLDFEHLAAMYGLDYARVSSWEELREALAEFLPSD---GPR 541

                         570       580
                  ....*....|....*....|
gi 1093259993 538 IFEVFTDSELESQALESIQN 557
Cdd:COG1165   542 VLEVRTDREENAELLKALFA 561
TPP_PYR_MenD cd07037
Pyrimidine (PYR) binding domain of ...
 14-175 4.63e-64

Pyrimidine (PYR) binding domain of 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexadiene-1-carboxylate synthase (MenD) and related proteins; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) binding domain of 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexadiene-1-carboxylate (SEPHCHC) synthase (MenD) 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. 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. Escherichia coli MenD (EcMenD) is a homotetramer (dimer-of-homodimers), having two active sites per homodimer lying between PYR and PP domains of different subunits. EcMenD catalyzes a Stetter-like conjugate addition of alpha-ketoglutarate to isochorismate, leading to the formation of SEPHCHC and carbon dioxide, this addition is the first committed step in the biosynthesis of vitamin K2 (menaquinone).


Pssm-ID: 132920 [Multi-domain]  Cd Length: 162  Bit Score: 207.35  E-value: 4.63e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093259993  14 QVILYLLKAHNIRHVIASPGTTNTALVSSMQQDPHFIMYSSVDERSAAYMACGLAAELNEPVVISCTGATASRNYLPGMT 93
Cdd:cd07037     1 QALVEELKRLGVRDVVISPGSRSAPLALAAAEHPEFRLHVRVDERSAAFFALGLAKASGRPVAVVCTSGTAVANLLPAVV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093259993  94 EAFYRKLPVLAITSMQAFSRVGHHVAQVIDRSSMPKDAVTLSVELPIVKDDEDVWDCEIKVNKAILELKRHGGGPVHINL 173
Cdd:cd07037    81 EAYYSGVPLLVLTADRPPELRGTGANQTIDQVGLFGDYVRWSVDLPPPEDDDDLWYLLRLANRAVLEALSAPPGPVHLNL 160


                  ..
gi 1093259993 174 PT 175
Cdd:cd07037   161 PF 162
TPP_SHCHC_synthase cd02009
Thiamine pyrophosphate (TPP) family, SHCHC synthase subfamily, TPP-binding module; composed of ...
 366-544 9.60e-39

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: 140.04  E-value: 9.60e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093259993 366 LASQLAHRIPAGSTIHFGILNSLRCWNFYELPA--SVTAASNVGGFGIDGGLSSLIGASLANpNKLYFAVIGDLAFFYDL 443
Cdd:cd02009     6 LARALPDHLPEGSQLFVGNSMPIRDLDLFALPSdkTVRVFANRGASGIDGTLSTALGIALAT-DKPTVLLTGDLSFLHDL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093259993 444 NVLGNRHA-GNNLRILLVNNGKGTEFRQYNHHaayfgEGAEEFVAasgHFGckSPTLV--KNFATDLGYEYLAATSKEEF 520
Cdd:cd02009    85 NGLLLGKQePLNLTIVVINNNGGGIFSLLPQA-----SFEDEFER---LFG--TPQGLdfEHLAKAYGLEYRRVSSLDEL 154

                         170       180
                  ....*....|....*....|....
gi 1093259993 521 AVHYQRFIApevGGKSIIFEVFTD 544
Cdd:cd02009   155 EQALESALA---QDGPHVIEVKTD 175
TPP_enzyme_N pfam02776
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain;
13-174 2.97e-19

Thiamine pyrophosphate enzyme, N-terminal TPP binding domain;


Pssm-ID: 460690 [Multi-domain]  Cd Length: 169  Bit Score: 85.36  E-value: 2.97e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093259993  13 AQVILYLLKAHNIRHVIASPGTTNTALVSSMQQDPHFIMYSSVDERSAAYMACGLAAELNEPVVISCTGATASRNYLPGM 92
Cdd:pfam02776   2 AEALADVLKALGVDTVFGVPGGHILPLLDALAKSPGIRYVLTRHEQGAAFAADGYARATGKPGVVLVTSGPGATNALTGL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093259993  93 TEAFYRKLPVLAITSMQAFSRVGHHVAQ-VIDRSSMPKDAVTLSVELPIVKDDEDVwdceikVNKAILELKRHGGGPVHI 171
Cdd:pfam02776  82 ANAYVDSVPLLVISGQRPRSLVGRGALQqELDQLALFRPVTKWAVRVTSADEIPEV------LRRAFRAALSGRPGPVYL 155


                  ...
gi 1093259993 172 NLP 174
Cdd:pfam02776 156 EIP 158
IlvB COG0028
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino ...
 13-463 8.07e-17

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: 83.67  E-value: 8.07e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093259993  13 AQVILYLLKAHNIRHVIASPGTTNTALVSSMQQDPHFIMYSSVDERSAAYMACGLAAELNEPVVISCT---GATasrNYL 89
Cdd:COG0028     6 ADALVEALEAEGVETVFGVPGGAILPLYDALRRQSGIRHILVRHEQGAAFMADGYARATGKPGVCLVTsgpGAT---NLV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093259993  90 PGMTEAFYRKLPVLAITSMQAFSRVGHHVAQVIDRSSMPKdavtlsvelPIVKddedvWDCEIK--------VNKAILEL 161
Cdd:COG0028    83 TGLADAYMDSVPVLAITGQVPTSLIGRGAFQEVDQVGLFR---------PITK-----WSYLVTdpedlpevLRRAFRIA 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093259993 162 KRHGGGPVHINLPttyskpYDVkQLPDYRVIERISEQDRFPELGTPDH-------------RKIAVFVGAHKTWSKAeTE 228
Cdd:COG0028   149 TSGRPGPVVLDIP------KDV-QAAEAEEEPAPPELRGYRPRPAPDPeaieeaaellaaaKRPVILAGGGARRAGA-AE 220

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093259993 229 ALESFCEQYGAVVFC----------DH-----SSGYQGKNRLLFALAAAqtmldkspcqpDVLIHIG-----EVTGDYAT 288
Cdd:COG0028   221 ELRALAERLGAPVVTtlmgkgafpeDHplylgMLGMHGTPAANEALAEA-----------DLVLAVGarfddRVTGNWDE 289

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093259993 289 LGmAGRQVWRVSED---------------GEIRDTFRKLryvfampeqaffahyAGQAAGQAPVNAGYYEQCRQQLQAIR 353
Cdd:COG0028   290 FA-PDAKIIHIDIDpaeigknypvdlpivGDAKAVLAAL---------------LEALEPRADDRAAWLARIAAWRAEYL 353

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093259993 354 DNLPEL--PLSNAWLASQLAHRIPAGSTIHFGILN----SLRCWNFYElPASVTAASNVGGFGIdgGLSSLIGASLANPN 427
Cdd:COG0028   354 AAYAADdgPIKPQRVIAALREALPDDAIVVTDVGQhqmwAARYLRFRR-PRRFLTSGGLGTMGY--GLPAAIGAKLARPD 430

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*..
gi 1093259993 428 KLYFAVIGDLAFF-----------YDLNVLgnrhagnnlrILLVNNG 463
Cdd:COG0028   431 RPVVAITGDGGFQmnlqelatavrYGLPVK----------VVVLNNG 467
TPP_PYR_POX_like cd07035
Pyrimidine (PYR) binding domain of POX and related proteins; Thiamine pyrophosphate (TPP ...
 14-174 1.82e-15

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: 74.11  E-value: 1.82e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093259993  14 QVILYLLKAHNIRHVIASPGTTNTALVSSMQQ-DPHFIMysSVDERSAAYMACGLAAELNEP---VVISCTGATasrNYL 89
Cdd:cd07035     1 DALVEALKAEGVDHVFGVPGGAILPLLDALARsGIRYIL--VRHEQGAVGMADGYARATGKPgvvLVTSGPGLT---NAV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093259993  90 PGMTEAFYRKLPVLAITSMQAFSRVGHHVAQVIDRSSMPKdAVTLSVELpiVKDDEDVwdcEIKVNKAILELKRHGGGPV 169
Cdd:cd07035    76 TGLANAYLDSIPLLVITGQRPTAGEGRGAFQEIDQVALFR-PITKWAYR--VTSPEEI---PEALRRAFRIALSGRPGPV 149


                  ....*
gi 1093259993 170 HINLP 174
Cdd:cd07035   150 ALDLP 154
TPP_enzyme_PYR cd06586
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine ...
 14-174 1.45e-10

Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine pyrophosphate (TPP) family, pyrimidine (PYR) binding domain; 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. The PYR and PP domains have a common fold, but do not share strong sequence conservation. The PP domain is not included in this group. 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. In the case of 2-oxoisovalerate dehydrogenase (2OXO), sulfopyruvate decarboxylase (ComDE), and the E1 component of human pyruvate dehydrogenase complex (E1- PDHc) the PYR and PP domains appear on different subunits. TPP-dependent enzymes are multisubunit proteins, the smallest catalytic unit being a dimer-of-active sites. For many of these enzymes the active sites lie between PP and PYR domains on different subunits. However, for the homodimeric enzymes 1-deoxy-D-xylulose 5-phosphate synthase (DXS) and Desulfovibrio africanus pyruvate:ferredoxin oxidoreductase (PFOR), each active site lies at the interface of the PYR and PP domains from the same subunit.


Pssm-ID: 132915 [Multi-domain]  Cd Length: 154  Bit Score: 59.67  E-value: 1.45e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093259993  14 QVILYLLKAHNIRHVIASPGTTNTALVSSMQQDPHFIMYSSVDERSAAYMACGLAAeLNEPVVISCTGATASRNYLPGMT 93
Cdd:cd06586     1 AAFAEVLTAWGVRHVFGYPGDEISSLLDALREGDKRIIDTVIHELGAAGAAAGYAR-AGGPPVVIVTSGTGLLNAINGLA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093259993  94 EAFYRKLPVLAITSmqAFSRVGHHVA--QVIDRSSMPKDAVTLSVELPivkddEDVWDCEiKVNKAILELKRHgGGPVHI 171
Cdd:cd06586    80 DAAAEHLPVVFLIG--ARGISAQAKQtfQSMFDLGMYRSIPEANISSP-----SPAELPA-GIDHAIRTAYAS-QGPVVV 150


                  ...
gi 1093259993 172 NLP 174
Cdd:cd06586   151 RLP 153
TPP_PYR_POX cd07039
Pyrimidine (PYR) binding domain of POX; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) ...
 13-187 3.49e-07

Pyrimidine (PYR) binding domain of POX; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) binding domain of pyruvate oxidase (POX) 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. 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. Lactobacillus plantarum POX is a homotetramer (dimer-of-homodimers), having two active sites per homodimer lying between PYR and PP domains of different subunits. POX decarboxylates pyruvate, producing hydrogen peroxide and the energy-storage metabolite acetylphosphate.


Pssm-ID: 132922 [Multi-domain]  Cd Length: 164  Bit Score: 50.24  E-value: 3.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093259993  13 AQVILYLLKAHNIRHVIASPGTTNTALVSSM--QQDPHFImySSVDERSAAYMACGLAAELNEPVV---ISCTGATasrN 87
Cdd:cd07039     3 ADVIVETLENWGVKRVYGIPGDSINGLMDALrrEGKIEFI--QVRHEEAAAFAASAEAKLTGKLGVclgSSGPGAI---H 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093259993  88 YLPGMTEAFYRKLPVLAITSMQAFSRVGHHVAQVIDRSSMPKDavtLSVELPIVKDDE---DVWDCEIKvnKAILElkrh 164
Cdd:cd07039    78 LLNGLYDAKRDRAPVLAIAGQVPTDELGTDYFQEVDLLALFKD---VAVYNETVTSPEqlpELLDRAIR--TAIAK---- 148

                         170       180
                  ....*....|....*....|...
gi 1093259993 165 gGGPVHINLPTtyskpyDVKQLP 187
Cdd:cd07039   149 -RGVAVLILPG------DVQDAP 164
TPP_enzymes cd00568
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ...
 366-529 7.66e-07

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: 49.18  E-value: 7.66e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093259993 366 LASQLAHRIPAGSTIHFGILNSLRCWNFY---ELPASVTAASNVGGFGIdgGLSSLIGASLANPNKLYFAVIGDLAFFYD 442
Cdd:cd00568     2 VLAALRAALPEDAIVVNDAGNSAYWAYRYlplRRGRRFLTSTGFGAMGY--GLPAAIGAALAAPDRPVVCIAGDGGFMMT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093259993 443 LNVLGN-RHAGNNLRILLVNNG-----KGTEFRQYNHHAAYFGEGAEEFVAasghfgcksptlvknFATDLGYEYLAATS 516
Cdd:cd00568    80 GQELATaVRYGLPVIVVVFNNGgygtiRMHQEAFYGGRVSGTDLSNPDFAA---------------LAEAYGAKGVRVED 144

                         170
                  ....*....|...
gi 1093259993 517 KEEFAVHYQRFIA 529
Cdd:cd00568   145 PEDLEAALAEALA 157
PLN02980 PLN02980
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate ...
 31-469 1.51e-05

2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate binding


Pssm-ID: 215530 [Multi-domain]  Cd Length: 1655  Bit Score: 48.31  E-value: 1.51e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093259993   31 SPGTTNTALVSSMQQDPHFIMYSSVDERSAAYMACGLAAELNEPVVISCTGATASRNYLPGMTEAFYRKLPVLAITSMQA 110
Cdd:PLN02980   322 APGSRSSPLAIAASNHPLTTCIACFDERSLAFHALGYARGSLKPAVVITSSGTAVSNLLPAVVEASQDFVPLLLLTADRP 401

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093259993  111 FSRVGHHVAQVIDRSSMPKDAVTLSVELPIVKDDEDVWDCEIKVNKAILELKRHGGGPVHINLP---------------- 174
Cdd:PLN02980   402 PELQDAGANQAINQVNHFGSFVRFFFNLPPPTDLIPARMVLTTLDSAVHWATSSPCGPVHINCPfrepldgsptnwmssc 481

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093259993  175 --------------TTYSKPYDVKQLPDYR-----VIERISEQDR----FPELGTPDHRKIAVFVGAHKTWSKAET---- 227
Cdd:PLN02980   482 lkgldmwmsnaepfTKYIQMQSSKADGDTTgqiteVLEVIQEAKRglllIGAIHTEDDIWAALLLAKHLMWPVVADilsg 561

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093259993  228 ----EALESFCEQYGAVVFCDH----------------------SSGYQGKNRLLF---ALAAAQTMLDKSPCQPD---V 275
Cdd:PLN02980   562 lrlrKLFKSFPEFELNILFVDHldhallsdsvrnwiqfdvviqiGSRITSKRVSQMlekCFPFSYILVDKHPCRHDpshL 641

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093259993  276 LIH-IGEVTGDYATLGMAGRQVWRVSE--------DGEIRDTFRKLRYVFAMPEQAFFAHYAGQA-AGQAPVNAGyyeqc 345
Cdd:PLN02980   642 VTHrVQSNIVQFADCLLKAQFPRRRSKwhghlqalDGMVAQEISFQIHAESSLTEPYVAHVISEAlTSDSALFIG----- 716

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093259993  346 rqQLQAIRDnlpelplSNAWLASQLAHRIPAGSTihfgILNSlrcwnfyELPASVTA-ASNVGGFGIDGGLSSLIGASLA 424
Cdd:PLN02980   717 --NSMAIRD-------ADMYGCSSENYSSRIVDM----MLSA-------ELPCQWIQvAGNRGASGIDGLLSTAIGFAVG 776

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*...
gi 1093259993  425 NpNKLYFAVIGDLAFFYDLN---VLGNRHAGNNLRILLVNNGKGTEFR 469
Cdd:PLN02980   777 C-NKRVLCVVGDISFLHDTNglsILSQRIARKPMTILVINNHGGAIFS 823
PRK08273 PRK08273
thiamine pyrophosphate protein; Provisional
 13-130 9.00e-05

thiamine pyrophosphate protein; Provisional


Pssm-ID: 181344 [Multi-domain]  Cd Length: 597  Bit Score: 45.29  E-value: 9.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093259993  13 AQVILYLLKAHNIRHVIASPGTTNTALVSSM---QQDPHFImySSVDERSAAYMACGLAAELNEP-VVISCTGATASrNY 88
Cdd:PRK08273    6 ADFILERLREWGVRRVFGYPGDGINGLLGALgraDDKPEFV--QARHEEMAAFMAVAHAKFTGEVgVCLATSGPGAI-HL 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1093259993  89 LPGMTEAFYRKLPVLAITSMQAFSRVGHHVAQVIDRSSMPKD 130
Cdd:PRK08273   83 LNGLYDAKLDHVPVVAIVGQQARAALGGHYQQEVDLQSLFKD 124
TPP_BFDC cd02002
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins ...
 361-441 1.66e-03

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: 39.89  E-value: 1.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093259993 361 LSNAWLASQLAHRIPAGSTI-HFGILNSLRCWNFYELPASVTAASNVGGfGIDGGLSSLIGASLANPNKLYFAVIGDLAF 439
Cdd:cd02002     1 LTPEYLAAALAAALPEDAIIvDEAVTNGLPLRDQLPLTRPGSYFTLRGG-GLGWGLPAAVGAALANPDRKVVAIIGDGSF 79


                  ..
gi 1093259993 440 FY 441
Cdd:cd02002    80 MY 81
TPP_enzyme_C pfam02775
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
407-463 1.77e-03

Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;


Pssm-ID: 460689 [Multi-domain]  Cd Length: 151  Bit Score: 39.11  E-value: 1.77e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093259993 407 GGFGIDG-GLSSLIGASLANPNKLYFAVIGDLAFFYDLNVLGN--RHaGNNLRILLVNNG 463
Cdd:pfam02775  25 GGLGTMGyGLPAAIGAKLARPDRPVVAIAGDGGFQMNLQELATavRY-NLPITVVVLNNG 83
ilvB CHL00099
acetohydroxyacid synthase large subunit
 408-496 5.52e-03

acetohydroxyacid synthase large subunit


Pssm-ID: 214363 [Multi-domain]  Cd Length: 585  Bit Score: 39.68  E-value: 5.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093259993 408 GFGIDG-GLSSLIGASLANPNKLYFAVIGDLAFFYDLNVLGNRhAGNNLR--ILLVNNGKGTEFRQ---------YNHha 475
Cdd:CHL00099  428 GLGTMGyGLPAAIGAQIAHPNELVICISGDASFQMNLQELGTI-AQYNLPikIIIINNKWQGMVRQwqqafygerYSH-- 504

                          90       100
                  ....*....|....*....|.
gi 1093259993 476 AYFGEGAEEFVAASGHFGCKS 496
Cdd:CHL00099  505 SNMEEGAPDFVKLAEAYGIKG 525
 
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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