ID A0A0G3V2Q7_9ACTN Unreviewed; 368 AA.
AC A0A0G3V2Q7;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Zn-dependent alcohol dehydrogenase, class III {ECO:0000313|EMBL:AKL74058.1};
DE EC=1.1.1.1 {ECO:0000313|EMBL:AKL74058.1};
DE EC=1.1.1.284 {ECO:0000313|EMBL:AKL74058.1};
GN ORFNames=IMCC26256_111789 {ECO:0000313|EMBL:AKL74058.1};
OS Actinobacteria bacterium IMCC26256.
OC Bacteria; Actinomycetota; Actinomycetes.
OX NCBI_TaxID=1650658 {ECO:0000313|EMBL:AKL74058.1, ECO:0000313|Proteomes:UP000035517};
RN [1] {ECO:0000313|EMBL:AKL74058.1, ECO:0000313|Proteomes:UP000035517}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMCC26256 {ECO:0000313|EMBL:AKL74058.1,
RC ECO:0000313|Proteomes:UP000035517};
RA Kim S.;
RT "Genome sequencing of freshwater Actinobacteria.";
RL Submitted (MAY-2015) 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}.
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DR EMBL; CP011489; AKL74058.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G3V2Q7; -.
DR STRING; 1650658.IMCC26256_111789; -.
DR KEGG; abai:IMCC26256_111789; -.
DR PATRIC; fig|1650658.3.peg.1782; -.
DR OrthoDB; 334894at2; -.
DR Proteomes; UP000035517; Chromosome.
DR GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR GO; GO:0106322; F:S-(hydroxymethyl)glutathione dehydrogenase NAD activity; IEA:UniProtKB-EC.
DR GO; GO:0106321; F:S-(hydroxymethyl)glutathione dehydrogenase NADP activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd08279; Zn_ADH_class_III; 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; PTHR43880; ALCOHOL DEHYDROGENASE; 1.
DR PANTHER; PTHR43880:SF12; ALCOHOL DEHYDROGENASE CLASS-3; 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; 2.
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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:AKL74058.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000035517};
KW Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 9..366
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 368 AA; 38414 MW; B2302E13D7ACF0BD CRC64;
MTKAAVYATL NQPLEIMELN LMDPQVGEVR IALGASGVCH SDLSVINGTL PIPPPAVLGH
EGAGTVVAVG LGVTNVKVGD HVVISWVPQC GTCYTCSRDQ GELCETGATA SMFGTMLDYT
SRFSMKDGTA VAQMSASGTF AEETVVPAIS CIKIPDDVPF QIAALIGCGV LTGFGAAVNT
ANIREGDNVV VVGAGGVGLN TIQGAKHKGA GKIIAVDMVD GKLETAASVG ATHTINASNG
DAIEQVMALT DGRGADVAFE VIGFPATIRQ SFDMTRKGGE TVIVGVPRLD QTMEFNPGMD
FVIAEKTLKG CWYGGANVHR DVPMLISQYK NGSLKLDELI SREIKLEEVN SAMDEMHGGH
IARSVIVY
//
