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Database: UniProt
Entry: A1T114_MYCVP
LinkDB: A1T114_MYCVP
Original site: A1T114_MYCVP 
ID   A1T114_MYCVP            Unreviewed;       372 AA.
AC   A1T114;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   24-JAN-2024, entry version 100.
DE   RecName: Full=alcohol dehydrogenase {ECO:0000256|ARBA:ARBA00013190};
DE            EC=1.1.1.1 {ECO:0000256|ARBA:ARBA00013190};
GN   OrderedLocusNames=Mvan_0013 {ECO:0000313|EMBL:ABM10864.1};
OS   Mycolicibacterium vanbaalenii (strain DSM 7251 / JCM 13017 / BCRC 16820 /
OS   KCTC 9966 / NRRL B-24157 / PYR-1) (Mycobacterium vanbaalenii).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=350058 {ECO:0000313|EMBL:ABM10864.1, ECO:0000313|Proteomes:UP000009159};
RN   [1] {ECO:0000313|EMBL:ABM10864.1, ECO:0000313|Proteomes:UP000009159}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 7251 / JCM 13017 / BCRC 16820 / KCTC 9966 / NRRL B-24157 /
RC   PYR-1 {ECO:0000313|Proteomes:UP000009159};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Singan V., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Anderson I.J., Miller C., Richardson P.;
RT   "Complete sequence of Mycobacterium vanbaalenii PYR-1.";
RL   Submitted (DEC-2006) 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|ARBA:ARBA00008072, ECO:0000256|RuleBase:RU361277}.
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DR   EMBL; CP000511; ABM10864.1; -; Genomic_DNA.
DR   RefSeq; WP_011777338.1; NZ_JACKSD010000290.1.
DR   AlphaFoldDB; A1T114; -.
DR   STRING; 350058.Mvan_0013; -.
DR   KEGG; mva:Mvan_0013; -.
DR   eggNOG; COG1062; Bacteria.
DR   HOGENOM; CLU_026673_14_1_11; -.
DR   OMA; CENCLSG; -.
DR   Proteomes; UP000009159; Chromosome.
DR   GO; GO:0004022; F:alcohol dehydrogenase (NAD+) 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; IPR023921; ADH_Zn_actinomycetes.
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   NCBIfam; TIGR03989; Rxyl_3153; 1.
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   Zinc {ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          10..370
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   372 AA;  39262 MW;  8D99222839A2D030 CRC64;
     MKTKAAVLWG LHQKWEVEEL ELDAPRAQEV LVKLTASGLC HSDDHLVTGD MPMNLPVVGG
     HEGAGVVVDV GPGVTEVEAG DHVVLSFIPA CGRCTECARG RSNLCVYGAA IVAGPQLDGT
     FRFHGSSGGR AYDIGQMCVL GTFSEYTVVP IASVVKVDND IPLDKAALVG CGVTTGYGAA
     VRTGEAADGD TVVVMGVGGL GINAIQGAAI AGARNVVALD PVAYKRERSF EFGATHAAAD
     VAEAQALITD LTRGTMADVC VVTTDSAEGA YVAQALSLVG KRGRVVMTAI PHPTDTVVDM
     SLFDLTLYEK QVRGCLFGSS NPRLDIPRLL DLYGSGRLKL DELITREYTL EEINQGYEDM
     HNGRNLRGVI RF
//
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