ID   Y2750_MYCTO             Reviewed;         272 AA.
AC   P9WGS4; L0TC54; O33292; Q7D6N3;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 36.
DE   RecName: Full=Uncharacterized oxidoreductase MT2820;
DE            EC=1.-.-.-;
GN   OrderedLocusNames=MT2820;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
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DR   EMBL; AE000516; AAK47140.1; -; Genomic_DNA.
DR   PIR; E70879; E70879.
DR   RefSeq; WP_003414045.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WGS4; -.
DR   SMR; P9WGS4; -.
DR   EnsemblBacteria; AAK47140; AAK47140; MT2820.
DR   KEGG; mtc:MT2820; -.
DR   PATRIC; fig|83331.31.peg.3041; -.
DR   HOGENOM; CLU_010194_1_0_11; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR   InterPro; IPR002347; SDR_fam.
DR   InterPro; IPR023985; SDR_subfam_1.
DR   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   TIGRFAMs; TIGR03971; SDR_subfam_1; 1.
DR   PROSITE; PS00061; ADH_SHORT; 1.
PE   3: Inferred from homology;
KW   NAD; Oxidoreductase.
FT   CHAIN           1..272
FT                   /note="Uncharacterized oxidoreductase MT2820"
FT                   /id="PRO_0000428311"
FT   ACT_SITE        170
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT   BINDING         12..34
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         39..40
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         77..78
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         104
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         153
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         174
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         203..205
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   272 AA;  28223 MW;  C662121703EBB3FC CRC64;
     MIDRPLEGKV AFITGAARGL GRAHAVRLAA DGANIIAVDI CEQIASVPYP LSTADDLAAT
     VELVEDAGGG IVARQGDVRD RASLSVALQA GLDEFGRLDI VVANAGIAMM QAGDDGWRDV
     IDVNLTGVFH TVQVAIPTLI EQGTGGSIVL ISSAAGLVGI GSSDPGSLGY AAAKHGVVGL
     MRAYANHLAP QNIRVNSVHP CGVDTPMINN EFFQQWLTTA DMDAPHNLGN ALPVELVQPT
     DIANAVAWLA SEEARYVTGV TLPVDAGFVN KR