Conserved Protein Domain Family
polyketide_synthase

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cd08251: polyketide_synthase 
polyketide synthase
Polyketide synthases produce polyketides in step by step mechanism that is similar to fatty acid synthesis. Enoyl reductase reduces a double to single bond. Erythromycin is one example of a polyketide generated by 3 complex enzymes (megasynthases). 2-enoyl thioester reductase (ETR) catalyzes the NADPH-dependent dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis. 2-enoyl thioester reductase activity has been linked in Candida tropicalis as essential in maintaining mitiochondrial respiratory function. This ETR family is a part of the medium chain dehydrogenase/reductase family, but lack the zinc coordination sites characteristic of the alcohol dehydrogenases in this family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding.
Statistics
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PSSM-Id: 176213
View PSSM: cd08251
Aligned: 7 rows
Threshold Bit Score: 501.572
Threshold Setting Gi: 149924311
Created: 25-Jan-2010
Updated: 2-Oct-2020
Structure
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Aligned Rows:
 
putative NAD(P)
Feature 1:putative NAD(P) binding site [chemical binding site]
Evidence:

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1                               #                                                         
YP_632112    2408 TAQPLEDREVRVAVR--AFSLNFGDLLCIKGLYPTmppYPFTPGFEASGVVVEIGAAVr---sLKPGDAVVAgMGEMLGA 2482 Myxococcus xa...
ABM63528       70 KAANPNPNEVSIQVK--ASAISFTDTLCVQGLYPSh--YPFVPGFEVSGVIRQVGEHIt---dLHVGDEVIAfTGSSMGG 142  Bugula neriti...
ZP_01912681    67 EVGPPGPGQIRVRTR--AFSLNFGDLLSLRGLYPTmppYPFTPGFELAGIVDALGPGVagpgaLEVGDAVIAmLGEAMGA 144  Plesiocystis ...
YP_632113     100 AVAPPSPGDITIQVR--ASALNYPDVMCVRGLYPTmpeYPFVPGFEVAGVVSAVGPGVa---rFAVGDEVIAvTGPLLGG 174  Myxococcus xa...
YP_001421789  549 EVPETKDDEVQIAVR--AFSLNFGDLLCVRGLYPTmppYPFTPGFEASGVVIKTGRHVt---sVIPGDEVIVgMGEEFGS 623  Bacillus amyl...
YP_003124928 3102 DVAAPGPDEVQISVR--SFSLNFADLLCLRGLYPGmppYPFTPGVEASGVVVHVGSNVk---aFRKGDEVIAtIAETMGG 3176 Chitinophaga ...
YP_001613832   84 EDEVGAPEEHAIHVDtvAISLNFGDLLCVQGLYPTmpaYPFTPGFEASGIVRAVGSKVt---rFAAGDEVIVsASVRLGI 160  Sorangium cel...
Feature 1                                         #                   # ####                  ##  
YP_632112    2483 HATSIVCSEsrVFLKPANLSFEEACALPAVSLTMIDAFKKADLQPGERILIQTATGGTGLIAVQLAQLQGAEIFATAGSA 2562 Myxococcus xa...
ABM63528      143 HAAYVTVPQdyVVRKPKDLSFEDACSFPLAFATVYHSFARGKLSHNDHILIQTATGGCGLMALQLARLKQCVCYGTSSRE 222  Bugula neriti...
ZP_01912681   145 HASVVLVDAgsVVPKPASVSFAEACAAPVAFLTATHVLARAGLEAGESILIQSAAGGVGLFLVQLARAAGATIFGTASTP 224  Plesiocystis ...
YP_632113     175 HASKVNVPAdnAVRKPATLTFEEACSLPVVFSTVYYAFEMGKLAEGEHVLVQTATGGCGLMALQLAHLKRCICHGSSSRD 254  Myxococcus xa...
YP_001421789  624 QANLITCKEhqVYHKPARLTFEEACALPTVAVTMIDAFRKAGLKKGEKILIQTATGGTGLIAVQMARHIGAEIYATAGSQ 703  Bacillus amyl...
YP_003124928 3177 QATLVTCKQkdVFLKPASLSFEEAAALPAVAMTAIDTLHKAGLKKGERILIQTATGGTGLMLVQLALHYGAEIYATAGSQ 3256 Chitinophaga ...
YP_001613832  161 QSTLIVADEsqLVAKPARLSFEEAASFLTVGLTIVEAFRRLRLAKGETILVQSATGGTGLVAVQLAQRAGATIIATASSD 240  Sorangium cel...
Feature 1          #              ##                      #                     #                 
YP_632112    2563 EKLEYLKRLGVHHCINYLEeDFEAAVKQLTHGEGVDVVINTLSGTAIQKGVRCLRPGGRYIELAMTALKSEKSFDLSVLn 2642 Myxococcus xa...
ABM63528      223 DKLALLKQWALPYVFNYKTcNIDEEIQRVSGHRGVDVVLNMLPGEHIQQGLNSLAKGGRYLELSMHGSLTNEPVSLSSLr 302  Bugula neriti...
ZP_01912681   225 AKLEHLRSLGVQHPINYVEhDFHERVQALTAGRGVDVVVNTLTGEAIQKGLDLLAPGGRYVEIAMSGLKAAPKLDLSGLc 304  Plesiocystis ...
YP_632113     255 DKRKVLERIGVPHVIDYTG-DFAPEIRNQTGGRGVDVVLNMVSGEAIQKGIDSLAPFGRYLEIAVHALKTSPKLDLSRLv 333  Myxococcus xa...
YP_001421789  704 KKIEYLHSLGVRNTICYLEeDFETEIMRMTGGRGVDVVINTLAGDAMQKGMNCLAPGGRYIEIAMTALKSAKSVDLSVLh 783  Bacillus amyl...
YP_003124928 3257 HKLDYLRQLGVQHVINYREnDFQQELMRMTGGQGVHVVVNTLSGDAMQKGLQCLSPGGRYVELAMMALKSARNVDLSVFs 3336 Chitinophaga ...
YP_001613832  241 EKLRYLTAMGVPHVIDYVRrDFEAEVMAITKGKGVDAVINTLAGEAIQKGINCLSPRGRYVEIAMTGLKSARSIDLSRMs 320  Sorangium cel...
Feature 1                ###                                                                 
YP_632112    2643 DNQTFFSLDLRKLas----srPDVIARHQHEFVRlv---eEGKLRATIHrtfpfsdVQSAYKALEDRKNIGKIVV 2710 Myxococcus xanthus...
ABM63528      303 FNQSVQTINLLGLlnk---gdDGFIGSVLAQMVSwi---eSGDLVSTVSriypldqIGEALRYVSEGEHIGKVVV 371  Bugula neritina ba...
ZP_01912681   305 DNQSFISVDLRRLmlrdraltARYVARMVEALEArtalptIGRVFPLES-------IREAYALLEDRGNVGKVVV 372  Plesiocystis pacif...
YP_632113     334 QNQTLHSIDLRRVgfag-rlgAHRLLDEMAAMAS------AGEIVPIVSrvypvrkLQDALQYVSEGKHIGKVVL 401  Myxococcus xanthus...
YP_001421789  784 NNQSFHSVDLRKLsl----qnPDQVKDYQLELQRla---eEGVIQPVISkifsfedIKEAYHCLDDRGNIGKIVI 851  Bacillus amyloliqu...
YP_003124928 3337 NNQAFYSVDVRKLgm----ldHELITSYRKEMLAlv---eKGVLRPTICkqfslesLSAAYAFLDQRENIGKVVV 3404 Chitinophaga pinen...
YP_001613832  321 NNQSFHSLDLRKLll----dvPEHAADLGEELFSlv---eRGELRIVVGktfdfdaIGDAYRYLADRRNIGKVVV 388  Sorangium cellulos...

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