ID A0A158GI77_9BURK Unreviewed; 352 AA.
AC A0A158GI77;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Alcohol dehydrogenase {ECO:0000313|EMBL:SAL31732.1};
GN ORFNames=AWB64_02887 {ECO:0000313|EMBL:SAL31732.1};
OS Caballeronia sordidicola.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Caballeronia.
OX NCBI_TaxID=196367 {ECO:0000313|EMBL:SAL31732.1, ECO:0000313|Proteomes:UP000054893};
RN [1] {ECO:0000313|EMBL:SAL31732.1, ECO:0000313|Proteomes:UP000054893}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 22029 {ECO:0000313|EMBL:SAL31732.1};
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; FCOC02000007; SAL31732.1; -; Genomic_DNA.
DR RefSeq; WP_060856055.1; NZ_FCOC02000007.1.
DR AlphaFoldDB; A0A158GI77; -.
DR OrthoDB; 9771084at2; -.
DR Proteomes; UP000054893; 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 8..345
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 352 AA; 38104 MW; 575137E86475AD69 CRC64;
MYKTHAYAAR SATTPLSPFE FERRELTAHD VRIDILFCGV CHSDLHTARS EWAGTVYPNV
PGHEIVGRVV EVGSEVSKFK VGQLAGVGCM VDSCRTCPSC QEGLEQYCEG PGGFVGTYNA
PDKHTGGVTY GGYSTQIVVD EAFTLHIPEN LELAAVAPLL CAGITTYSPL RHWNIQPGQK
VGIVGLGGLG HMGVKIAAAL GAHVVLFTTS QSKVEDAKRL GAHDVVISKD ADQMAKHANS
FDYILNTVAA SHDLDAFVTL LKRDGAMTLV GVPEHPHPSP SIGNLIFKRR SLAGSLIGGI
EETQEMLDFC GKHGITSDIE MIRMDEINTA YDRMLKSDVK YRFVIDMSSI KQ
//