3IUP


Conserved Protein Domain Family
ETR_like_1

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cd08291: ETR_like_1 
Click on image for an interactive view with Cn3D
2-enoyl thioester reductase (ETR) like proteins, child 1
2-enoyl thioester reductase (ETR) like proteins. ETR catalyzes the NADPH-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 2-enoyl thioester reductase (ETR) like proteins. 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 has 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. Candida tropicalis enoyl thioester reductase (Etr1p) catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters in mitochondrial fatty acid synthesis. Etr1p forms homodimers, with each subunit containing a nucleotide-binding Rossmann fold domain and a catalytic domain.
Statistics
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PSSM-Id: 176251
View PSSM: cd08291
Aligned: 34 rows
Threshold Bit Score: 354.604
Threshold Setting Gi: 118383415
Created: 28-May-2009
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
 
NADP bindingdimer interface
Conserved site includes 24 residues -Click on image for an interactive view with Cn3D
Feature 1:NADP binding site [chemical binding site]
Evidence:
  • Structure:3IUP: Ralstonia eutropha putative NADPH:quinone oxidoreductase binds NADP, contacts at 4A
    View structure with Cn3D

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1                                                     #                                  
3IUP_A         7 QLRSRIKSSGe------lELSLDSIDTphpgpDEVLIRIEASPLNPSDLGLLfGAADXSTakasgtaerpivtarvpega 80  Ralstonia eutro...
XP_001011144   8 MKALVLEEPKkpi--vfkEIEIPTPKS-----GQVLVKVESAPINPSDLAFLqGHYSSNKg------------------- 61  Tetrahymena the...
XP_001461481   5 MRAVVMEGPGqkp--vvkEIPIPTPQS-----GQVLIKVDSAPINPSDISFLhGAYSSNKq------------------- 58  Paramecium tetr...
XP_001011149   1 MRALIMEQFKqpk--fakNFPIPEPKE-----GQVLIKVEAAPINPSDLSYInGQYGKEAk------------------- 54  Tetrahymena the...
XP_001011148   6 MKALVLEEFGqpl--vlkEIDIPQPNQ-----GEVLVRVESTPINPSDASFMkGSYSSSRk------------------- 59  Tetrahymena the...
XP_001011147   6 MKCLSLEQFGqpl--afkQVDIPQPGQ-----GEVLIKVEASPINPSDLLFLaGKYATLGfv------------------ 60  Tetrahymena the...
XP_001021415   6 MQCLILEQYGk-------PLVLKSVDIpqpteGEVLIQVEAAPINPSDLLFIeGQHSNPSkq------------------ 60  Tetrahymena the...
XP_001453871   6 TMSCLWKESKdakp-yvnRVPIPTVEE-----GQLLIRMDYAPINPSDIKFLlGQSSSNKq------------------- 60  Paramecium tetr...
XP_001011161   9 MKALVLEEFGkpv--qlkEIPVPKPRY-----NEVLIKIEYAPLNPMDLSFLkGSYSSVKk------------------- 62  Tetrahymena the...
XP_001009569   2 YKAVVVKEFKndeaifveEFSLEELRKgl-deKNFIVKVHAAPLNPLDQNKLlGTIFTLKc------------------- 61  Tetrahymena the...
Feature 1                                                                                      ##
3IUP_A        81 xrsxagrldaSXPVGNEGAGVVVEAGSSPaaqalXGKTVAAIGG----AXYSQYRCIPADQCLVLPEGATpADGASSFVN 156 Ralstonia eutro...
XP_001011144  62 ---------yPCVPGFEGSGVVISSGGGIlgwslVGKRVAIAAQtq-wGTYAEYCVADANSVLPLPDEVSfNQGACTFVN 131 Tetrahymena the...
XP_001461481  59 ---------fPCVPGFEGSGTVIANGGGIigwrlVGKRVAFYSQsq-fGTFGEYSVADALGCLELENDITlQEACCSFVN 128 Paramecium tetr...
XP_001011149  55 ---------fPVVLGFEGSGTIVKSGGGAyadslVNKRVAFSAEt---GSYAEFCLAKATSVVPISDNLTfSQASCSFVN 122 Tetrahymena the...
XP_001011148  60 ---------aPCVPGFEGSGVVVKSGGGEvadslLNKRVAFTAGgq-nGTFAQYATANANFVLPIEDDVTfNQAASSFVN 129 Tetrahymena the...
XP_001011147  61 ---------pPYIPGFEGSGLVIKSGGGQeadylLNKRVAFFRCr---GAYAQYTISNSQTCLIIDDDITfNQAASSFIN 128 Tetrahymena the...
XP_001021415  61 ---------pPCIPGFEGSGIIVKSGGGEladslINKRVAFYRSk---GSFAQYTVSKAEWCLVFDKQITfNQAASSFIN 128 Tetrahymena the...
XP_001453871  61 ---------fPCVAGFEGSGTVVLTGGGIaswgmSGKRVAFYTNhe-yGTYGEYCIADTNLCIELDNDIEsSQAACSFVN 130 Paramecium tetr...
XP_001011161  63 ---------lPVTPGFEGSGTVVASGGGLygwslIGKRVAVYVQrsphGCYAEYAVTNAFQCITVPETVSfENAASGLVN 133 Tetrahymena the...
XP_001009569  62 ----------PFTPGSEASGIIVESHNKDl----IGKKVAVSVQt---GTWKEYILATEENSIFLNDDVDlDSASCGFVN 124 Tetrahymena the...
Feature 1          #                   # ####                   ##    #                          
3IUP_A       157 PLTALGXVETXRlEGHSALVHTAAASNLGQXLNQICLKDGIKLVNIVRKq--EQADLLKAQ-GAVHVCNAAsp--tFXQD 231 Ralstonia eutro...
XP_001011144 132 PLTVIAMLQIVQeANVKTVVHSAAASALGKMMVRYFQDNGVQVINVVRRa--EQVEILKKE-GAQHILDSTqe--dFDEK 206 Tetrahymena the...
XP_001461481 129 PLTVISMLEVAKeHKTQAVVHTAAASQLGRMMVRHFQANGVRVINIVRRd--AQVEMLKKE-GADIILNSSds--dFLEK 203 Paramecium tetr...
XP_001011149 123 PLTCVAFLEIVKeAGVKAIVHSAAASALGKMVVRYFQQNGIKVINLVRRq--EQVDTLKAI-GAEYVLNQTdp--nFNQE 197 Tetrahymena the...
XP_001011148 130 PLTVIAMLETVQqANAKAVVQSAAASALGRMMVRYFKQHGIEVINIVRRp--EQIQILKNE-GANIVLNSNqe--dFLPT 204 Tetrahymena the...
XP_001011147 129 PLTVVGMLETVKeAKVKTVVHSAAASALGRMMVRYFKNNGIEVINIVRRq--DQVEILKKE-GATIILNQNdq--dFYPQ 203 Tetrahymena the...
XP_001021415 129 PLTVINMLEIVKeAKVKAIVNSAASSALGRMIVRYFKKNGIDVINIVRRp--EQIDILKQE-GATYILNQNdk--dFLNQ 203 Tetrahymena the...
XP_001453871 131 PLSAIGMLDICKkNNAKAVINNPGASQLGKMMNRLFNERNIKVINIVRRe--EQVYELRYEcGAELIINQNdp--dFLKQ 206 Paramecium tetr...
XP_001011161 134 PLTVVMMHKKTLkKKAKAIISNPGASAVGRMIYRYFTANGIKVINIVRRq--EQVDLLKKEeNAEYVLNSSdp--nFQKD 209 Tetrahymena the...
XP_001009569 125 PLTAVGLIYQAQkYNAKAVVNLAAQSALGKMINYLAKDSGLNCLNVIRGdenRIQSIIKEY-QNENVISTDqdpqsFQKQ 203 Tetrahymena the...
Feature 1                       ##                                     ## ##                    #
3IUP_A       232 LTEALVStgatIAFDATGGGKLGGQILTCXeaalnksareysrYGSTTHKQVYLYGGLDtspTEFNRNFGXa--WGXGGW 309 Ralstonia eutro...
XP_001011144 207 LKALCTSlnatIFFDAVAGELTGRVLRCMP-------------NKSTVYVYGGLSLSGSv--LDPSDLIFRk-qTVTGFW 270 Tetrahymena the...
XP_001461481 204 LKNVLQTlratVFFDAVGGEQSGKILEVMP-------------SHSTCYVYGGLSLKPVg-nVSIMDLIFKd-kKVVGFW 268 Paramecium tetr...
XP_001011149 198 LSKLSEElqatIFFDAVAGTTTADVVFQMP-------------RGSTVYVYGGLSGQESl--IGPRVLIFKd-aTVKGFW 261 Tetrahymena the...
XP_001011148 205 LKAHAIElnatVFFDAVAGPLTGQVLSSMP-------------NGSTAYVYGALSLQEAs--ISPTQLIFRd-qSIKGLW 268 Tetrahymena the...
XP_001011147 204 LKKLTTDlnakIFFDAIAGSFTGEILSQMP-------------NNSTAYVYGLLSGENSs--VSPTELIFRd-qSVKGFS 267 Tetrahymena the...
XP_001021415 204 LNKITNQlnatIFFDAVAGSFTGEVLTQMP-------------IYSTAYVYGFLSGKNF---SIPTYEFIYnkqNIQGFS 267 Tetrahymena the...
XP_001453871 207 LKIMCETtqasIYFDAVGGEQSGQILNIMP-------------KGSTLMMYGTLDSWQIg-gIQANDLLSDk-kSIQGFF 271 Paramecium tetr...
XP_001011161 210 LNQLSKKlgatVSFDAVGGSLCAVILNNMP-------------DGSSTYVYGNLSMKNSe--ASQNDLIFKh-kKIKGFW 273 Tetrahymena the...
XP_001009569 204 FKELAEKlsatVAFDPVGGSLTGQIFNNLP-------------QNSILIVYGSLSQKDIe-gINGVQVRWAn-kRLEGFT 268 Tetrahymena the...
Feature 1        ##                                                                    ##  #   
3IUP_A       310 LLFPFLqk-------igRERANALKQRVV-------AELKTTFAshyskeislaevldLDXIAVYNk--rATGEKYLI 371 Ralstonia eutroph...
XP_001011144 271 LTEWLKnkni----vslLFLLKKLKGLLL-------SQLKTDIQreac------leegINAVKFYTsn-mSKGKVVFK 330 Tetrahymena therm...
XP_001461481 269 LTQYVKskni----isqALLLNQLKGLIK-------TNLKTIVAktvd------vsefKEGLDFYKkn-mSEGKVLIR 328 Paramecium tetrau...
XP_001011149 262 LSPWLGklkl----eqiVSLVKKVQTLLT-------SDLKTDIAgeekle---nfsqaLEKYAKNM----SAGKILFR 321 Tetrahymena therm...
XP_001011148 269 LTKWLTtisk----eqlKTAILKLQKLIK-------TELRTEIAqecs------lqegSQAVRQYIkn-mSSGKILFK 328 Tetrahymena therm...
XP_001011147 268 LNTWLQsitp----elkRQSLEKLQKLIK-------TDLKSEISkeyp------lqdgQQAIEYYSkn-mSSGKVLIK 327 Tetrahymena therm...
XP_001021415 268 ITSRLLtlsp----ekrKKQLEIVQEFIQ-------TDFKTDIAnefp------ikniEKAINYYSqn-mSEGKVLLK 327 Tetrahymena therm...
XP_001453871 272 LNVWLKeqnk----lelIMTLKKLKNFIK-------TSLKTKIAkefp------ldqfQQAIDYYKth-mTEGKTLIC 331 Paramecium tetrau...
XP_001011161 274 LVDWMK-----------KTSVLENYFLSKklgsmynNIMATSFArkyp-------lnqIEEACRFYlknmTEGKILLS 333 Tetrahymena therm...
XP_001009569 269 FYGWIQsipeqdrkkskELVQQKMNTLFK-------TQIHTSYGln----------qhKEAISLFRk--vQGGQKIIF 327 Tetrahymena therm...

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