ID   Q1YQ87_9GAMM            Unreviewed;       339 AA.
AC   Q1YQ87;
DT   02-MAY-2006, integrated into UniProtKB/TrEMBL.
DT   02-MAY-2006, sequence version 1.
DT   24-JAN-2024, entry version 88.
DE   SubName: Full=Zinc-containing alcohol dehydrogenase family protein {ECO:0000313|EMBL:EAS46356.1};
GN   ORFNames=GB2207_00245 {ECO:0000313|EMBL:EAS46356.1};
OS   gamma proteobacterium HTCC2207.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC   Porticoccaceae; SAR92 clade.
OX   NCBI_TaxID=314287 {ECO:0000313|EMBL:EAS46356.1, ECO:0000313|Proteomes:UP000005555};
RN   [1] {ECO:0000313|EMBL:EAS46356.1, ECO:0000313|Proteomes:UP000005555}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC2207 {ECO:0000313|EMBL:EAS46356.1,
RC   ECO:0000313|Proteomes:UP000005555};
RA   Giovannoni S.J., Cho J.-C., Ferriera S., Johnson J., Kravitz S.,
RA   Halpern A., Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R.,
RA   Venter J.C.;
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU361277};
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. {ECO:0000256|RuleBase:RU361277}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EAS46356.1}.
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DR   EMBL; AAPI01000007; EAS46356.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q1YQ87; -.
DR   STRING; 314287.GB2207_00245; -.
DR   eggNOG; COG1064; Bacteria.
DR   HOGENOM; CLU_026673_20_2_6; -.
DR   OrthoDB; 9771084at2; -.
DR   Proteomes; UP000005555; Unassembled WGS sequence.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd05283; CAD1; 1.
DR   Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR013149; ADH-like_C.
DR   InterPro; IPR013154; ADH-like_N.
DR   InterPro; IPR002328; ADH_Zn_CS.
DR   InterPro; IPR047109; CAD-like.
DR   InterPro; IPR029752; D-isomer_DH_CS1.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020843; PKS_ER.
DR   PANTHER; PTHR42683; ALDEHYDE REDUCTASE; 1.
DR   PANTHER; PTHR42683:SF38; ALDEHYDE REDUCTASE AHR; 1.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   SMART; SM00829; PKS_ER; 1.
DR   SUPFAM; SSF50129; GroES-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00059; ADH_ZINC; 1.
DR   PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|RuleBase:RU361277};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Zinc {ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          17..336
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   339 AA;  36291 MW;  8F405029B3DDAE5F CRC64;
     MSTAKSINAY AILEPGGQFE SYSYPVDDLK NNEVEMDVLH SGICHSDLSM VENEWGLTKY
     PLVAGHEIIG KITAKGADVH GLKPGTVVGL GWHSGYCGHC HPCKTGDQNL CPSAVRTIIG
     HNGGFAEKVR AQASSVVVIP EGMDPVSAGP LLCAGITVFN PIVQFGIKST DKVAVIGIGG
     LGHLALQFLN AWGCEVTAFT SSDSKHQEAL DLGAHKTLNS RDPDALKNAA SSFDFIISTV
     NVKLEWNLYL NALKPKGRLH FVGAITAPLD ISMFPLMLGQ REVSGSPVGS PATIETMLDF
     ANLHNIKPQV ECFPMTEINQ AFAHLKTGDA RYRIVLSND
//