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Database: UniProt
Entry: A0A0N1GMR1_9ACTN
LinkDB: A0A0N1GMR1_9ACTN
Original site: A0A0N1GMR1_9ACTN 
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
//
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