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Database: UniProt
Entry: A0A101AXG7_9MYCO
LinkDB: A0A101AXG7_9MYCO
Original site: A0A101AXG7_9MYCO 
ID   A0A101AXG7_9MYCO        Unreviewed;       354 AA.
AC   A0A101AXG7;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=alcohol dehydrogenase {ECO:0000256|ARBA:ARBA00013190};
DE            EC=1.1.1.1 {ECO:0000256|ARBA:ARBA00013190};
GN   ORFNames=AU194_15750 {ECO:0000313|EMBL:KUI30772.1};
OS   Mycobacterium sp. GA-2829.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=1772283 {ECO:0000313|EMBL:KUI30772.1, ECO:0000313|Proteomes:UP000053444};
RN   [1] {ECO:0000313|EMBL:KUI30772.1, ECO:0000313|Proteomes:UP000053444}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GA-2829 {ECO:0000313|EMBL:KUI30772.1,
RC   ECO:0000313|Proteomes:UP000053444};
RG   TB Trials Study Group;
RA   Sutton G., Brinkac L., Sanka R., Adams M., Lau E.L., Macaden R.,
RA   Grewal H.M.S.;
RL   Submitted (JAN-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}.
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:KUI30772.1}.
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DR   EMBL; LQIT01000029; KUI30772.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A101AXG7; -.
DR   STRING; 1772283.AU194_15750; -.
DR   Proteomes; UP000053444; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd05284; arabinose_DH_like; 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; PTHR42940; ALCOHOL DEHYDROGENASE 1-RELATED; 1.
DR   PANTHER; PTHR42940:SF8; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 11; 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:UP000053444};
KW   Zinc {ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          8..351
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   354 AA;  37960 MW;  0B3CABA27D9E911C CRC64;
     MRAARMYGYK QPLRLEEIDV PAIEPHEVLV KVGGAGMCRT DFQLIDGYFD TGLQMDFPIT
     PGHEVAGWVD TVGAQVPRSA ALSEGDQVVV FGSWGDGACR QCHEGNEQLC AHGVWAGFGL
     HGGYQEYLPV DYRYLIKMPG RDDLSPETLA PLTDAGLTPY RGLKKLRAAG HLGAGRTLAV
     SGIGGLGSYG TQYAKLLGGG ADVVAFARSD EKLKIALDNG ADHAINVGGK TTEAIRQELE
     SLTGRSELDA VIECAGSEEA IRLAFSLLAA EGAVASVGLI GNRVDIPLFP LVAREYTYFG
     SFWGNYNDLT EVLALAEAGR IRHTVTRVRF DEVNETLDAI ARGDVLGRAV IVYD
//
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