ID   Y1938_MYCSS             Reviewed;         283 AA.
AC   Q1BAN7;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Uncharacterized oxidoreductase Mmcs_1938;
DE            EC=1.-.-.-;
GN   OrderedLocusNames=Mmcs_1938;
OS   Mycobacterium sp. (strain MCS).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; unclassified Mycobacterium.
OX   NCBI_TaxID=164756;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCS;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Kim E., Miller C.D., Hughes J.E., Anderson A.J., Sims R.C., Richardson P.;
RT   "Complete sequence of chromosome of Mycobacterium sp. MCS.";
RL   Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the aldo/keto reductase family. {ECO:0000305}.
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DR   EMBL; CP000384; ABG08047.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q1BAN7; -.
DR   SMR; Q1BAN7; -.
DR   KEGG; mmc:Mmcs_1938; -.
DR   HOGENOM; CLU_023205_0_1_11; -.
DR   OMA; KLWPTDQ; -.
DR   BioCyc; MSP164756:G1G6O-1983-MON; -.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.100; -; 1.
DR   InterPro; IPR020471; AKR.
DR   InterPro; IPR018170; Aldo/ket_reductase_CS.
DR   InterPro; IPR023210; NADP_OxRdtase_dom.
DR   InterPro; IPR036812; NADP_OxRdtase_dom_sf.
DR   PANTHER; PTHR43827; PTHR43827; 1.
DR   Pfam; PF00248; Aldo_ket_red; 1.
DR   PIRSF; PIRSF000097; AKR; 1.
DR   PRINTS; PR00069; ALDKETRDTASE.
DR   SUPFAM; SSF51430; SSF51430; 1.
DR   PROSITE; PS00798; ALDOKETO_REDUCTASE_1; 1.
DR   PROSITE; PS00062; ALDOKETO_REDUCTASE_2; 1.
DR   PROSITE; PS00063; ALDOKETO_REDUCTASE_3; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase.
FT   CHAIN           1..283
FT                   /note="Uncharacterized oxidoreductase Mmcs_1938"
FT                   /id="PRO_0000380746"
FT   ACT_SITE        58
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         116
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         196..248
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   283 AA;  30113 MW;  6E03896D577B651F CRC64;
     MTSTRGEAAG IPSVSLNDGH SIPVLGLGVG ELSEAEAERS VAAALEAGYR LIDTAAVYGN
     EAAVGRAVNA SGIPREEIYV TTKLAVADQG FGTSQDAARA SLERLGLDYV DLYLIHWPAG
     DHGKYIDSWG GLMKAKQDGV ARSIGVCNFN AEHLSNIIDL SFFTPAINQI ELHPLLNQAE
     LREVNAGYGI VTEAYGPLGV GRLLDHAAVT GVAQAHGKTP AQVLLRWSIQ LGNVVIARSA
     NPDRITSNLE VFDFELTDDE MATLNGLDEG TRFRPDPETY TGP