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Database: UniProt
Entry: A0A285L567_9ENTR
LinkDB: A0A285L567_9ENTR
Original site: A0A285L567_9ENTR 
ID   A0A285L567_9ENTR        Unreviewed;       335 AA.
AC   A0A285L567;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   RecName: Full=Zinc-type alcohol dehydrogenase-like protein {ECO:0000256|RuleBase:RU364000};
GN   ORFNames=SAMN02744775_04331 {ECO:0000313|EMBL:SNY80075.1};
OS   Enterobacter sp. CC120223-11.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Enterobacter.
OX   NCBI_TaxID=1378073 {ECO:0000313|EMBL:SNY80075.1, ECO:0000313|Proteomes:UP000219512};
RN   [1] {ECO:0000313|EMBL:SNY80075.1, ECO:0000313|Proteomes:UP000219512}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CC120223-11 {ECO:0000313|EMBL:SNY80075.1,
RC   ECO:0000313|Proteomes:UP000219512};
RA   Ehlers B., Leendertz F.H.;
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. Quinone oxidoreductase subfamily.
CC       {ECO:0000256|RuleBase:RU364000}.
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DR   EMBL; OBEF01000028; SNY80075.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A285L567; -.
DR   OrthoDB; 9785812at2; -.
DR   Proteomes; UP000219512; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd08252; AL_MDR; 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; IPR013154; ADH-like_N.
DR   InterPro; IPR014182; ADH_Zn_typ-1.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020843; PKS_ER.
DR   InterPro; IPR002364; Quin_OxRdtase/zeta-crystal_CS.
DR   NCBIfam; TIGR02817; adh_fam_1; 1.
DR   PANTHER; PTHR44154; QUINONE OXIDOREDUCTASE; 1.
DR   PANTHER; PTHR44154:SF1; QUINONE OXIDOREDUCTASE; 1.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF13602; ADH_zinc_N_2; 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; PS01162; QOR_ZETA_CRYSTAL; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|RuleBase:RU364000};
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU364000};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW   Zinc {ECO:0000256|RuleBase:RU364000}.
FT   DOMAIN          13..332
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   335 AA;  36021 MW;  963F1646CD231BC4 CRC64;
     MKAIVITRAA SEGSNIQFLQ DVTLPVPAAQ GHDLLIEVKA VSVNPVDTKV RAGFNADAPR
     VLGWDAVGVV KAVGEKVSLF SPGDEVWYAG ALGRPGSNSE FQLVDERIVA LKPRTLSHAA
     AAALPLTAIT AWELLFDRLG IKENGNEGDT LLIVGAAGGV GSILTQLARK LTKMTVIGTA
     SRPESQQWVM DAGAHHTIDH TRPLAEALAE IGIKNVTHVA SLNHTEHHYA QIIQALAPQG
     KLALIDDPDT LDARPLKAKS LSLHWEFMFT RSMFETSDMI AQHQLLTRVA QLIDEGVLKT
     TLGEHYGAIT AENLQKAHAW IETGRSVGKI VLEGF
//
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