ID F5Z3Q0_MYCSD Unreviewed; 335 AA.
AC F5Z3Q0;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=alcohol dehydrogenase {ECO:0000256|ARBA:ARBA00013190};
DE EC=1.1.1.1 {ECO:0000256|ARBA:ARBA00013190};
GN Name=adhA {ECO:0000313|EMBL:AEF35950.1};
GN OrderedLocusNames=JDM601_1950 {ECO:0000313|EMBL:AEF35950.1};
OS Mycolicibacter sinensis (strain JDM601) (Mycobacterium sinense).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacter.
OX NCBI_TaxID=875328 {ECO:0000313|EMBL:AEF35950.1, ECO:0000313|Proteomes:UP000009224};
RN [1] {ECO:0000313|EMBL:AEF35950.1, ECO:0000313|Proteomes:UP000009224}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JDM601 {ECO:0000313|EMBL:AEF35950.1,
RC ECO:0000313|Proteomes:UP000009224};
RX PubMed=21685274; DOI=10.1128/JB.05291-11;
RA Zhang Z.Y., Sun Z.Q., Wang Z.L., Wen Z.L., Sun Q.W., Zhu Z.Q., Song Y.Z.,
RA Zhao J.W., Wang H.H., Zhang S.L., Guo X.K.;
RT "Complete genome sequence of a novel clinical isolate, the nontuberculous
RT Mycobacterium strain JDM601.";
RL J. Bacteriol. 193:4300-4301(2011).
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; CP002329; AEF35950.1; -; Genomic_DNA.
DR AlphaFoldDB; F5Z3Q0; -.
DR STRING; 875328.JDM601_1950; -.
DR KEGG; mjd:JDM601_1950; -.
DR eggNOG; COG1064; Bacteria.
DR HOGENOM; CLU_026673_20_7_11; -.
DR Proteomes; UP000009224; Chromosome.
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; IPR014187; ADH_Zn_typ-2.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR NCBIfam; TIGR02822; adh_fam_2; 1.
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:UP000009224};
KW Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 16..333
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 335 AA; 35262 MW; A77D831C01789509 CRC64;
MTMTAWRVDR PGPIAGGPLH RVSTAVPRPQ PSELLVAVRA CGVCRTDLHV TEGDLPVHRA
GVTPGHEVVG EVVEVGAEAG GGFAVGDRVG IAWLRHTCGS CRYCRRGDEN LCPRSRYTGW
DDDGGYAEFA TVPAAFAHHL PGGYSDSELA PLLCAGIIGY RSLQLADLPP GGRLGIYGFG
GSAHITAQVA LARGAEVHVM TRDPQARELA LQLGAASVQG AADPPPVRLD SAILFAPVGE
LVPPACQALD RGGTCAIAGI HLSDIPSLNY QRDLFYERRI RSVTSNTRAD AREFLEFAAA
HHITVTTPEY SLGDADRALA DLAADRIAGA AVLVV
//
