3IP1


Conserved Protein Domain Family
Zn_ADH3

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cd08265: Zn_ADH3 
Click on image for an interactive view with Cn3D
Alcohol dehydrogenases of the MDR family
This group resembles the zinc-dependent alcohol dehydrogenase and has the catalytic and structural zinc-binding sites characteristic of this group. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines. Other MDR members have only a catalytic zinc, and some contain no coordinated zinc.
Statistics
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PSSM-Id: 176226
View PSSM: cd08265
Aligned: 4 rows
Threshold Bit Score: 648.421
Threshold Setting Gi: 260100166
Created: 13-Jan-2010
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
 
Conserved site includes 24 residues -Click on image for an interactive view with Cn3D
Feature 1:putative NAD(P) binding site [chemical binding site]
Evidence:
  • Comment:MDR family binds NAD(P) as a cofactor
  • Comment:defined by comparison to MDR alcohol dehydrogenase-like family

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1                                                                     ###  #          
3IP1_A      4 RAVRLHAKWDPrpefklgpkdiegkLTWLgskvwRYPEVRVeevpeprieKPTEIIIKVKACGICGSDVHXAQTDEEGYI 83  Thermotoga maritima
YP_920225   2 RAALVTADFAPrpgykitqdeirthKVREgakvwRNPKLVLrtdypvpepKPDEILIRVKAVGICGSDIHFLETDSEGYI 81  Thermofilum penden...
CAJ70959    2 KALIVDGEWNPrknyplsneeqakkRANVgsqvwQHTQFEVkdvs-vpnlQDDEILVRIKSCGICGSDTHLYETDKDGYI 80  Candidatus Kueneni...
EDY40155    5 LAAVLYAKWDPkpeykptpkdiegkLTYLgglvwRYPELRVerrp-ipkiKEDEVLIKVKACGICGSDIHMYESDKDGYI 83  Thermococcus barop...
Feature 1                                                                                     
3IP1_A     84 LYPGLTgfpvTLGHEFSGVVveagpeainRRTNKRFEIGEPVCAEEXLWCGHCRPCAEGFPNHCE--------NLNELGF 155 Thermotoga maritima
YP_920225  82 LYPGLTrfpvVIGHEFSGVVek------vGTNVKTFKPGDMVTSEEMFWCGECDACRSVDFNHCLrlndpadlEFGELGF 155 Thermofilum penden...
CAJ70959   81 IFSGVTelprIIGHELSGIVeq------tGKNVRNVSKGDWIAAESIMWCGMCHACRSGSPNQCK--------YIKLMGL 146 Candidatus Kueneni...
EDY40155   84 LYPGLTafpcVLGHEFSGEIvkvg-ekayNQWGEKFEVGTPVTAEEMVWCGYCRHCRDGYPNHCI--------NLQEIGF 154 Thermococcus barop...
Feature 1                                             #   #                     ######        
3IP1_A    156 NVDGAFAEYVKVDAKYAWSLRELeg-vYEGDRLFLAGSLVEPTSVAYNAVIvrGGGIRPGDNVVILGGGPIGLAAVAILK 234 Thermotoga maritima
YP_920225 156 THDGAMADYVVVKAKYAWKIDSLldryGSEDKAFEAGSLVEPTSVAYHAMFtrAGGFKPGAYVAVWGAGPIGLAAIALAK 235 Thermofilum penden...
CAJ70959  147 SADGAFAEYIAINERYCWEINDFre-iYSEDEAFDIGALIEPVGCAYNGLFivGGGFQPGATVVVYGTGPIGLGAIALAK 225 Candidatus Kueneni...
EDY40155  155 SRDGAFAEYIAVPARVVWEITEIve-rYGEKKGYEAGALVEPTSVAYNGIFerGGGFRPGAYVVVFGAGPIGLAGIALSK 233 Thermococcus barop...
Feature 1               ##   #              #                            ## #                 
3IP1_A    235 HAGASKVILSEPSEvRRNLAKElGADHVIDPtke-----nfVEAVLDYTNGLGAKLFLEATGVpqlVWPQIEEVIwrarg 309 Thermotoga maritima
YP_920225 236 AAGAGKVIAFEVSPtRRELAKKvGADYVFNPvelskngvepWEKIMEVTGGQGADFHVEAAGAprhTIPQMQKSLa---- 311 Thermofilum penden...
CAJ70959  226 IAGASQIIAFDIIDeRANIALEmGADYAFNTnkmr--dclsGEKVMEITKGWGADIQIEAAGAapaTIPEMEKSMa---- 299 Candidatus Kueneni...
EDY40155  234 AAGAAKVIAVEIAEaRQKLAKEmGADVVIDPtki----dsvSGKILEVTHGEGADMYVEAAGAfpkTWPAIEETIwngek 309 Thermococcus barop...
Feature 1            ##                      ###                                              
3IP1_A    310 INATVAIVARAdakiplTGEVFQVRRAQIVGSQGHSGhGTFPRVISLXASGXDXTKIIsKTVsxeeIPEYIKRlqtdksl 389 Thermotoga maritima
YP_920225 312 INGKIVQIGRAaedvpiYLEVFQVRRGQIFGSQGHSGfGNFGNVIRLMAAGKIDMTQIiTARfsldEVYKAFErahqrid 391 Thermofilum penden...
CAJ70959  300 INGKIIYLGRAatttsmHLDHLVSGANKIVGARGHSGyAIFPSIIKLIATGRLKLDKMiTARypfaGIMEAIKassertd 379 Candidatus Kueneni...
EDY40155  310 VNAKVVAIGRAvthvplQFEVLQVRRAQVFGAQGHSGhGIFPSVINLMASGKIDMTKIvTHRfkleDAAEALKfaskqks 389 Thermococcus barop...
Feature 1           
3IP1_A    390 vkVTXL 395 Thermotoga maritima
YP_920225 392 gkITLK 397 Thermofilum pendens Hrk 5
CAJ70959  380 gkILIH 385 Candidatus Kuenenia stuttgartiensis
EDY40155  390 niGKVL 395 Thermococcus barophilus MP

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