ID   ADH_MYCPN               Reviewed;         351 AA.
AC   P75214;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=Probable NADP-dependent isopropanol dehydrogenase;
DE            EC=1.1.1.80;
GN   Name=adh; OrderedLocusNames=MPN_564; ORFNames=MP278;
OS   Mycoplasma pneumoniae (strain ATCC 29342 / M129) (Mycoplasmoides
OS   pneumoniae).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=272634;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29342 / M129;
RX   PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA   Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT   "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT   pneumoniae.";
RL   Nucleic Acids Res. 24:4420-4449(1996).
CC   -!- FUNCTION: Alcohol dehydrogenase with a preference for medium chain
CC       secondary alcohols, such as 2-butanol and isopropanol. Has very low
CC       activity with primary alcohols, such as ethanol. Under physiological
CC       conditions, the enzyme reduces aldehydes and 2-ketones to produce
CC       secondary alcohols. Is also active with acetaldehyde and
CC       propionaldehyde (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NADP(+) + propan-2-ol = acetone + H(+) + NADPH;
CC         Xref=Rhea:RHEA:21792, ChEBI:CHEBI:15347, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17824, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.80;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. {ECO:0000305}.
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DR   EMBL; U00089; AAB95926.1; -; Genomic_DNA.
DR   PIR; S73604; S73604.
DR   RefSeq; NP_110253.1; NC_000912.1.
DR   RefSeq; WP_010874921.1; NC_000912.1.
DR   AlphaFoldDB; P75214; -.
DR   SMR; P75214; -.
DR   IntAct; P75214; 1.
DR   STRING; 272634.MPN_564; -.
DR   PRIDE; P75214; -.
DR   EnsemblBacteria; AAB95926; AAB95926; MPN_564.
DR   KEGG; mpn:MPN_564; -.
DR   PATRIC; fig|272634.6.peg.626; -.
DR   HOGENOM; CLU_026673_11_3_14; -.
DR   OMA; TGWFGAV; -.
DR   BioCyc; MPNE272634:G1GJ3-925-MON; -.
DR   Proteomes; UP000000808; Chromosome.
DR   GO; GO:0050009; F:isopropanol 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; Reference proteome; Zinc.
FT   CHAIN           1..351
FT                   /note="Probable NADP-dependent isopropanol dehydrogenase"
FT                   /id="PRO_0000160746"
FT   BINDING         37
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         59
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         60
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         150
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         175..178
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         198..200
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         265..267
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         340
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   351 AA;  37812 MW;  3153B93BFFE64D2C CRC64;
     MKAYAMLKIG ATGWIEKPRP VCGPNDAIIR PLAVAPCTSD VHTVWEGGIG ERHNMVLGHE
     GCGVVDEVGS EVKSFKVGDR VLVAAITPEW NSVNAQAGYP MHSGGMLGGW KFSNVKDGMF
     AEYFHVNDAE GNLALMPEGM DLADACMLSD MIPTGFHANE LADIQYGVAL SFFCAGPVGL
     MAIAGAALKG AGRIIVVDSR PDIVEIAKAY GATDYIDFKK VSVVDEILKW TNNEGVEKVL
     ISGGGSTILE TAIKVLRPGG KIGNVNYFGA GEFLTIPRVE WGVGMAHKAI HGGLMLGGRL
     RLEKLARLIM TKKLDPSKMI THRFKGFEHI EEALFLMKDK PKDLIKSVVI F