Y1984_MYCSK
ID Y1984_MYCSK Reviewed; 283 AA.
AC A1UEC5;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Uncharacterized oxidoreductase Mkms_1984;
DE EC=1.-.-.-;
GN OrderedLocusNames=Mkms_1984;
OS Mycobacterium sp. (strain KMS).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; unclassified Mycobacterium.
OX NCBI_TaxID=189918;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KMS;
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 Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Miller C.D.,
RA Richardson P.;
RT "Complete sequence of chromosome of Mycobacterium sp. KMS.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the aldo/keto reductase family. {ECO:0000305}.
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DR EMBL; CP000518; ABL91183.1; -; Genomic_DNA.
DR RefSeq; WP_011559338.1; NC_008705.1.
DR AlphaFoldDB; A1UEC5; -.
DR SMR; A1UEC5; -.
DR STRING; 189918.Mkms_1984; -.
DR EnsemblBacteria; ABL91183; ABL91183; Mkms_1984.
DR KEGG; mkm:Mkms_1984; -.
DR HOGENOM; CLU_023205_0_1_11; -.
DR OMA; KLWPTDQ; -.
DR OrthoDB; 1035565at2; -.
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 Mkms_1984"
FT /id="PRO_0000380744"
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