ID   B0VPZ1_ACIBS            Unreviewed;       342 AA.
AC   B0VPZ1;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 101.
DE   SubName: Full=Alcohol dehydrogenase {ECO:0000313|EMBL:CAP02882.1};
DE            EC=1.1.1.- {ECO:0000313|EMBL:CAP02882.1};
GN   OrderedLocusNames=ABSDF3625 {ECO:0000313|EMBL:CAP02882.1};
OS   Acinetobacter baumannii (strain SDF).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=509170 {ECO:0000313|EMBL:CAP02882.1, ECO:0000313|Proteomes:UP000001741};
RN   [1] {ECO:0000313|EMBL:CAP02882.1, ECO:0000313|Proteomes:UP000001741}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SDF {ECO:0000313|EMBL:CAP02882.1,
RC   ECO:0000313|Proteomes:UP000001741};
RX   PubMed=18350144; DOI=10.1371/journal.pone.0001805;
RA   Vallenet D., Nordmann P., Barbe V., Poirel L., Mangenot S., Bataille E.,
RA   Dossat C., Gas S., Kreimeyer A., Lenoble P., Oztas S., Poulain J.,
RA   Segurens B., Robert C., Abergel C., Claverie J.-M., Raoult D., Medigue C.,
RA   Weissenbach J., Cruveiller S.;
RT   "Comparative analysis of Acinetobacters: three genomes for three
RT   lifestyles.";
RL   PLoS ONE 3:E1805-E1805(2008).
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}.
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DR   EMBL; CU468230; CAP02882.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0VPZ1; -.
DR   KEGG; abm:ABSDF3625; -.
DR   HOGENOM; CLU_026673_20_2_6; -.
DR   BioCyc; ABAU509170:GCL9-2990-MONOMER; -.
DR   Proteomes; UP000001741; Chromosome.
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   ECO:0000313|EMBL:CAP02882.1}; Zinc {ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          15..336
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   342 AA;  36523 MW;  60ED1632F05FC62F CRC64;
     MSNNTIQAYA AMQAGEKLVP YKFDAGELQP HQVEVKVEYC GLCHSDISVL NNEWRSTVYP
     VVAGHEIIGR IVALGSEAKG LQIGQRVGIG WTAESCQACD ECIGGQQVLC TGENVATIVG
     HAGGFANKVR AGWQWAIPLP EDLDPESAGP LLCGGITVFD PLLKHKIQAT HHVGVIGIGG
     LGHIAIKLLK AWGCEITAFS SNPDKTEELK AMGADHVVNS RDTEAVKAQK GKFDLLLSTV
     NVTLNWRAFI STLAPNGSLH FLGLTLEPVP VSVGSLIDGA KSVTGSPTGS PAALHQLLKF
     AARKKIAPQI ELFPMSQLNE AIERLHSGQA RYRIVLKADF AE
//