ID A0A148KKS9_9ALTE Unreviewed; 333 AA.
AC A0A148KKS9;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Alcohol dehydrogenase {ECO:0000313|EMBL:KXI26897.1};
GN ORFNames=AX660_03795 {ECO:0000313|EMBL:KXI26897.1};
OS Paraglaciecola hydrolytica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Paraglaciecola.
OX NCBI_TaxID=1799789 {ECO:0000313|EMBL:KXI26897.1, ECO:0000313|Proteomes:UP000070299};
RN [1] {ECO:0000313|EMBL:KXI26897.1, ECO:0000313|Proteomes:UP000070299}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S66 {ECO:0000313|EMBL:KXI26897.1,
RC ECO:0000313|Proteomes:UP000070299};
RA Wen L., He K., Yang H.;
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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:KXI26897.1}.
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DR EMBL; LSNE01000020; KXI26897.1; -; Genomic_DNA.
DR RefSeq; WP_068382456.1; NZ_LSNE01000020.1.
DR AlphaFoldDB; A0A148KKS9; -.
DR STRING; 1799789.AX660_03795; -.
DR OrthoDB; 9771084at2; -.
DR Proteomes; UP000070299; 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; 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.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|RuleBase:RU361277};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000070299};
KW Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 11..331
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 333 AA; 35561 MW; BC82F95E5CA439D7 CRC64;
MIKAYAAMAP GAKFEAFEYD PGPLGKDEVE LDVESCGICH SDLSMLDNDW GFTQYPFVPG
HEVIGIVNSV GSDVTQIKVG QRVGLGWHSG YCNTCHTCQS GDHNLCASAQ PTIGGRHGGF
ADKVRAQANS VVELPKGVKP DSAGPLFCGG ITVFNPLVQF DVKPTSKVAV IGIGGLGHIA
LQFLNAWGCE VTAFTSSESK KAEALKMGAH HTLNSNNASE LEAAAGRFDF IISTVNVKLD
WNAYVGTLAP KGRLHFVGAT LEPLNIGVFP LIMGQRSVSG SPVGSPATIK KMLDFTALHN
IEPVTEYFSF AQVNEAIDKL RQGKAHYRIV LKD
//
