ID   ADHC_MYCBO              Reviewed;         346 AA.
AC   P0A4X1; A0A1R3Y3Q1; P31975; X2BMX0;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=NADP-dependent alcohol dehydrogenase C;
DE            EC=1.1.1.2;
GN   Name=adhC; Synonyms=adh; OrderedLocusNames=BQ2027_MB3071;
OS   Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=233413;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=BCG;
RX   PubMed=1427101; DOI=10.1016/0378-1119(92)90164-k;
RA   Stelandre M., Bosseloir Y., de Bruyn J., Maes P., Content J.;
RT   "Cloning and sequence analysis of the gene encoding an NADP-dependent
RT   alcohol dehydrogenase in Mycobacterium bovis BCG.";
RL   Gene 121:79-86(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA   Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA   Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA   Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA   Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT   "The complete genome sequence of Mycobacterium bovis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA   Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA   Robbe-Austerman S., Gordon S.V.;
RT   "Updated reference genome sequence and annotation of Mycobacterium bovis
RT   AF2122/97.";
RL   Genome Announc. 5:E00157-E00157(2017).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a primary alcohol + NADP(+) = an aldehyde + H(+) + NADPH;
CC         Xref=Rhea:RHEA:15937, ChEBI:CHEBI:15378, ChEBI:CHEBI:15734,
CC         ChEBI:CHEBI:17478, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.2;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. {ECO:0000305}.
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DR   EMBL; X63450; CAA45049.1; -; Genomic_DNA.
DR   EMBL; LT708304; SIU01696.1; -; Genomic_DNA.
DR   PIR; JC1376; JC1376.
DR   RefSeq; NP_856716.1; NC_002945.3.
DR   RefSeq; WP_003415965.1; NC_002945.4.
DR   AlphaFoldDB; P0A4X1; -.
DR   SMR; P0A4X1; -.
DR   EnsemblBacteria; SIU01696; SIU01696; BQ2027_MB3071.
DR   GeneID; 45427038; -.
DR   PATRIC; fig|233413.5.peg.3374; -.
DR   OMA; YRFSIDM; -.
DR   SABIO-RK; P0A4X1; -.
DR   Proteomes; UP000001419; Chromosome.
DR   GO; GO:0008106; F:alcohol dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR013149; ADH-like_C.
DR   InterPro; IPR013154; ADH_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   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   SMART; SM00829; PKS_ER; 1.
DR   SUPFAM; SSF50129; SSF50129; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00059; ADH_ZINC; 1.
PE   3: Inferred from homology;
KW   Metal-binding; NADP; Oxidoreductase; Zinc.
FT   CHAIN           1..346
FT                   /note="NADP-dependent alcohol dehydrogenase C"
FT                   /id="PRO_0000160744"
FT   BINDING         41
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         63
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         94
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         97
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         100
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         108
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         158
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   346 AA;  37075 MW;  969179113DBA27C1 CRC64;
     MSTVAAYAAM SATEPLTKTT ITRRDPGPHD VAIDIKFAGI CHSDIHTVKA EWGQPNYPVV
     PGHEIAGVVT AVGSEVTKYR QGDRVGVGCF VDSCRECNSC TRGIEQYCKP GANFTYNSIG
     KDGQPTQGGY SEAIVVDENY VLRIPDVLPL DVAAPLLCAG ITLYSPLRHW NAGANTRVAI
     IGLGGLGHMG VKLGAAMGAD VTVLSQSLKK MEDGLRLGAK SYYATADPDT FRKLRGGFDL
     ILNTVSANLD LGQYLNLLDV DGTLVELGIP EHPMAVPAFA LALMRRSLAG SNIGGIAETQ
     EMLNFCAEHG VTPEIELIEP DYINDAYERV LASDVRYRFV IDISAL