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Database: UniProt
Entry: A0A132PL99_9MYCO
LinkDB: A0A132PL99_9MYCO
Original site: A0A132PL99_9MYCO 
ID   A0A132PL99_9MYCO        Unreviewed;       348 AA.
AC   A0A132PL99;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=Dehydrogenase {ECO:0000313|EMBL:KWX23119.1};
GN   ORFNames=AFM11_17325 {ECO:0000313|EMBL:KWX23119.1};
OS   Mycolicibacterium wolinskyi.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=59750 {ECO:0000313|EMBL:KWX23119.1, ECO:0000313|Proteomes:UP000070612};
RN   [1] {ECO:0000313|EMBL:KWX23119.1, ECO:0000313|Proteomes:UP000070612}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC_01 {ECO:0000313|EMBL:KWX23119.1,
RC   ECO:0000313|Proteomes:UP000070612};
RA   de Man T.J., Perry K.A., Coulliette A.D., Jensen B., Toney N.C.,
RA   Limbago B.M., Noble-Wang J.;
RT   "A draft genome sequence of Mycobacterium wolinskyi.";
RL   Submitted (JUL-2015) 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:KWX23119.1}.
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DR   EMBL; LGTW01000010; KWX23119.1; -; Genomic_DNA.
DR   RefSeq; WP_067850949.1; NZ_LGTW01000010.1.
DR   AlphaFoldDB; A0A132PL99; -.
DR   STRING; 59750.AWC31_01905; -.
DR   PATRIC; fig|59750.3.peg.818; -.
DR   Proteomes; UP000070612; 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; cd08233; butanediol_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   PANTHER; PTHR43161:SF23; (R,R)-BUTANEDIOL DEHYDROGENASE-RELATED; 1.
DR   PANTHER; PTHR43161; SORBITOL DEHYDROGENASE; 1.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF00107; ADH_zinc_N; 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|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU361277};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070612};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          24..140
FT                   /note="Alcohol dehydrogenase-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08240"
FT   DOMAIN          181..308
FT                   /note="Alcohol dehydrogenase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00107"
SQ   SEQUENCE   348 AA;  36630 MW;  D085A8BB215BE1A4 CRC64;
     MKAAVYYGPN KVEVADVPEP QPRPGTVKLK VGFNGICGTD LHEYYAGPIF VPTEPHPLTG
     QQLPLTMGHE FSGTVTDVGP GVTDFVPGDR VAVEPIYRCG KCAPCRAGTY NICQQIGFHG
     LMSDGGMAEY TVVPTNMLHR LPDNVSLELG ALVEPMSVAY HAATLGEVGP LHTAVIFGAG
     PIGIGLWFAL RGKGLDSVFV SEPSPTRRAA IEALGAKTLD PTQIDVPAFI ADHTEGRGAD
     AAFDAAGVAP AIEAATASVG ARKPTISVAI YEKPLTTPLL NLVMNESRIQ GSLCYTSADF
     EAVIELMSQG VYDTTGWVTP IGIDDVIDEG FEALHAGTKM KVLVDPAN
//
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