ID A0A158A369_9BURK Unreviewed; 352 AA.
AC A0A158A369;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Alcohol dehydrogenase {ECO:0000313|EMBL:SAK52149.1};
GN ORFNames=AWB77_01374 {ECO:0000313|EMBL:SAK52149.1};
OS Caballeronia fortuita.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Caballeronia.
OX NCBI_TaxID=1777138 {ECO:0000313|EMBL:SAK52149.1, ECO:0000313|Proteomes:UP000054903};
RN [1] {ECO:0000313|Proteomes:UP000054903}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Oliw E.H.;
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; FCNX02000002; SAK52149.1; -; Genomic_DNA.
DR RefSeq; WP_061133605.1; NZ_FCNX02000002.1.
DR AlphaFoldDB; A0A158A369; -.
DR STRING; 1777138.AWB77_01374; -.
DR OrthoDB; 9771084at2; -.
DR Proteomes; UP000054903; 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:SF85; CINNAMYL ALCOHOL DEHYDROGENASE 6-RELATED; 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 11..345
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 352 AA; 38109 MW; 3A2F232B379D73A5 CRC64;
MFEAYSYAAS AADKPLGPHE IQRRDVGPND VRIDILFCGV CHSDLHMARN EWGGTNYPVV
PGHEIVGRVA AVGSDVSKFE VGQLAGVGCM VDSCRVCNAC KEGLEQYCES PESFTQTYNS
PDKKSGGVTF GGYSTSIVVD EAYVLSVPEN LELAAVAPLL CAGITTYSPL RHWNVQQGHK
VGIVGLGGLG HMGVKIAAAM GAHVVLFTTS PGKIEDAKRL GAHEVVISKD LDQMAAHANS
FDFILNTVAA SHDLDQFMAL LKRDGTMTLV GVPEHPHPSP SVMNMIFKRR SLAGSLIGGI
AETQEMLDFC GKHGITSDIE MIRMDEVNQA YERMLKSDVK YRFVIDMATM ER
//
