ID   Y1919_MYCSJ             Reviewed;         276 AA.
AC   A3PXT0;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Uncharacterized oxidoreductase Mjls_1919;
DE            EC=1.-.-.-;
GN   OrderedLocusNames=Mjls_1919;
OS   Mycobacterium sp. (strain JLS).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; unclassified Mycobacterium.
OX   NCBI_TaxID=164757;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JLS;
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   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Miller C.D., Anderson A.J.,
RA   Sims R.C., Richardson P.;
RT   "Complete sequence of Mycobacterium sp. JLS.";
RL   Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the aldo/keto reductase family. {ECO:0000305}.
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DR   EMBL; CP000580; ABN97707.1; -; Genomic_DNA.
DR   AlphaFoldDB; A3PXT0; -.
DR   SMR; A3PXT0; -.
DR   STRING; 164757.Mjls_1919; -.
DR   KEGG; mjl:Mjls_1919; -.
DR   HOGENOM; CLU_023205_0_1_11; -.
DR   OMA; AEMYANE; -.
DR   BioCyc; MSP164757:G1G8C-1939-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; PS00062; ALDOKETO_REDUCTASE_2; 1.
DR   PROSITE; PS00063; ALDOKETO_REDUCTASE_3; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase.
FT   CHAIN           1..276
FT                   /note="Uncharacterized oxidoreductase Mjls_1919"
FT                   /id="PRO_0000380743"
FT   ACT_SITE        50
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         108
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         188..240
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   276 AA;  30203 MW;  954F7333C9043EB6 CRC64;
     MGAPLVALND GNSIPQVGLG VWQTPPEDTE RAVAAALAAG YRHVDTAAAY GNEEQTGRAI
     AQSGLDRSQV YLVTKLWNSE QGYDATLAAF EASVDRLGVD YLDLYLIHWP VPEKNLFVDT
     FRAFARLRED GRIRSIGVSN FEPEHLRVLI DSTGIVPAVN QIELHPLLPQ RELRELHAQL
     GIATEAWSPL GQGSLLAHPT VTGVAESHGK TAAQALIRWH MQLGNIVIPK SVNPQRIESN
     FDVFDFELSE QDMASISSLE DASRLGPDPK TFNFTG