ID A0A1C5E3Z7_9ACTN Unreviewed; 346 AA.
AC A0A1C5E3Z7;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Alcohol dehydrogenase {ECO:0000313|EMBL:SCF89716.1};
GN ORFNames=GA0115259_104414 {ECO:0000313|EMBL:SCF89716.1};
OS Streptomyces sp. MnatMP-M17.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1839780 {ECO:0000313|EMBL:SCF89716.1, ECO:0000313|Proteomes:UP000198886};
RN [1] {ECO:0000313|EMBL:SCF89716.1, ECO:0000313|Proteomes:UP000198886}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MnatMP-M17 {ECO:0000313|EMBL:SCF89716.1,
RC ECO:0000313|Proteomes:UP000198886};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-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; FMDK01000424; SCF89716.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C5E3Z7; -.
DR OrthoDB; 3567264at2; -.
DR Proteomes; UP000198886; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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; PTHR42940; ALCOHOL DEHYDROGENASE 1-RELATED; 1.
DR PANTHER; PTHR42940:SF7; ALCOHOL DEHYDROGENASE N-TERMINAL DOMAIN-CONTAINING PROTEIN; 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000198886};
KW Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 18..340
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 346 AA; 36089 MW; C1CCF2933FDCF0F6 CRC64;
MTSTKTRTYR AMQVDRPGAA PHLVEKEFRE PGPGQVRVAV EACGVCHTDA VMIEGGFPGA
PFPMVPGHEI AGRIDAIGDG VEEFEKGQRV AVGWFGGNCG HCVACRDGDA INCATLQTPG
LAYPGGYADT VVVPASALAR IPDGFSFVDA APMGCAGVTV CGALSRSAAR PGDLVAIIGV
GGLGHLGVQF ADKMGFETVA IARGKDKEPL ARELGARHYI DNRSQDVAAE LRALGGAKVV
LNTATNSKAA TDTLDGLGHR GELIVIALHP EPLQISTMQL ITGTRKVYGH ASGTSREVEE
TLRFAALTGI RPMTEEVPLT EAGPALDKML ASKARFRMVL TSGPGH
//