ID   K5ZJ10_9PROT            Unreviewed;       357 AA.
AC   K5ZJ10;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   SubName: Full=Alcohol dehydrogenase {ECO:0000313|EMBL:EKM99445.1};
GN   ORFNames=MXAZACID_10398 {ECO:0000313|EMBL:EKM99445.1};
OS   Acidocella sp. MX-AZ02.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Acidocella.
OX   NCBI_TaxID=1214225 {ECO:0000313|EMBL:EKM99445.1, ECO:0000313|Proteomes:UP000006217};
RN   [1] {ECO:0000313|EMBL:EKM99445.1, ECO:0000313|Proteomes:UP000006217}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MX-AZ02 {ECO:0000313|EMBL:EKM99445.1,
RC   ECO:0000313|Proteomes:UP000006217};
RX   PubMed=23405365;
RA   Servin-Garciduenas L.E., Garrett R.A., Amils R., Martinez-Romero E.;
RT   "Genome Sequence of the Acidophilic Bacterium Acidocella sp. Strain MX-
RT   AZ02.";
RL   Genome Announc. 1:E00041-12(2013).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947,
CC         ECO:0000256|RuleBase:RU361277};
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. {ECO:0000256|ARBA:ARBA00008072, 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:EKM99445.1}.
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DR   EMBL; AMPS01000160; EKM99445.1; -; Genomic_DNA.
DR   RefSeq; WP_008494281.1; NZ_JH976208.1.
DR   AlphaFoldDB; K5ZJ10; -.
DR   STRING; 1214225.MXAZACID_10398; -.
DR   PATRIC; fig|1214225.3.peg.2016; -.
DR   HOGENOM; CLU_026673_11_0_5; -.
DR   Proteomes; UP000006217; 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; cd08233; butanediol_DH_like; 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; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020843; PKS_ER.
DR   PANTHER; PTHR43161; SORBITOL DEHYDROGENASE; 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.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU361277};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006217};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          7..353
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   357 AA;  37979 MW;  0CB9B5917B962501 CRC64;
     MRALRFHAAR DLRIEEIAAP SAPPPGQILV RNRFVGICGT DLHEYAYGPI FIPTSPHPFT
     KAHGAQILGH EFGGVVEAIG AGVSHVQPGD RVSIQPLIMP RAGDYFADRG LFHLSPELAL
     AGLSWAWGGM AEAALLNDYN VVKIPDSLSD EEAALVEPSA VAVYSCDRGG VRAGASVLVT
     GAGPIGLLTV LAARAAGAGP LFVSDLNDAR LAYAKSIVPE LIVINPKREN VGEMVRAQTE
     GGVGCDVALE CVGNEHALKA CLDAVRKQGV VVQTGLHPHE NPLDWFQVTF KDVDLRGAWA
     YPTHYWPRVI RLIASGALPA SKVVTAKIKL EDAVKEGFDA LLDPSGKHLK ILIDLQA
//