ID A0A0N1GMR1_9ACTN Unreviewed; 338 AA.
AC A0A0N1GMR1;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Alcohol dehydrogenase {ECO:0000313|EMBL:KPI27770.1};
DE EC=1.1.1.1 {ECO:0000313|EMBL:KPI27770.1};
GN ORFNames=OV320_5818 {ECO:0000313|EMBL:KPI27770.1};
OS Actinobacteria bacterium OV320.
OC Bacteria; Actinomycetota; Actinomycetes.
OX NCBI_TaxID=1592329 {ECO:0000313|EMBL:KPI27770.1, ECO:0000313|Proteomes:UP000037870};
RN [1] {ECO:0000313|EMBL:KPI27770.1, ECO:0000313|Proteomes:UP000037870}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OV320 {ECO:0000313|EMBL:KPI27770.1,
RC ECO:0000313|Proteomes:UP000037870};
RA Brown S.D., Utturkar S.M., Klingeman D.M., Pelletier D.;
RT "Draft genome sequences for four actinobacteria strains OK006 OK074 OV450
RT and OV320.";
RL Submitted (AUG-2015) 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|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:KPI27770.1}.
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DR EMBL; LJCX01000027; KPI27770.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N1GMR1; -.
DR PATRIC; fig|1592329.3.peg.5120; -.
DR Proteomes; UP000037870; Unassembled WGS sequence.
DR GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd08287; FDH_like_ADH3; 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; PTHR42813:SF2; DEHYDROGENASE, ZINC-CONTAINING, PUTATIVE (AFU_ORTHOLOGUE AFUA_2G02810)-RELATED; 1.
DR PANTHER; PTHR42813; ZINC-TYPE ALCOHOL DEHYDROGENASE-LIKE; 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|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU361277};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:KPI27770.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000037870};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 10..336
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 338 AA; 35934 MW; B85BB37F02B4BC82 CRC64;
MRGAVIYAPG DVRFENLDDP KILQPTDAVI RTVATCVCGS DLWPYRGAEP IGDPHPMGHE
YVGIVEEVGS EVANVKPGQF VVGSFATSDN TCANCRNGWQ SSCLHREFMS TCQADYVRIP
NAHGTLVATD EQPDGELVPS LLAVSDVMGT GWYAAVAAEV KPGSTAVVVG DGAVGLCGVI
AAKELGAERI IAMSRHESRQ KLALEFGATD IVSERGDEGV ARVKDLTEGI GADSVLECVG
TAESMRQALH SARPGGNVGF VGVPHDVQVD GQELFFSHVG LRGGPAPVRR YLPDLIDRVL
TGRINPGKVF DLTLPLDQVA EGYQAMDERR AIKALLMP
//