ID   Y1350_MYCTO             Reviewed;         247 AA.
AC   P9WGR8; L0T9D4; P66781; Q11020;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 41.
DE   RecName: Full=Uncharacterized oxidoreductase MT1393;
DE            EC=1.-.-.-;
GN   Name=fabG2; OrderedLocusNames=MT1393;
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; AAK45656.1; -; Genomic_DNA.
DR   PIR; E70740; E70740.
DR   RefSeq; WP_003406963.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WGR8; -.
DR   SMR; P9WGR8; -.
DR   EnsemblBacteria; AAK45656; AAK45656; MT1393.
DR   GeneID; 45425329; -.
DR   KEGG; mtc:MT1393; -.
DR   PATRIC; fig|83331.31.peg.1500; -.
DR   HOGENOM; CLU_010194_1_3_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   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00061; ADH_SHORT; 1.
PE   3: Inferred from homology;
KW   NAD; Oxidoreductase.
FT   CHAIN           1..247
FT                   /note="Uncharacterized oxidoreductase MT1393"
FT                   /id="PRO_0000428314"
FT   ACT_SITE        155
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT   BINDING         19
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q99714"
FT   BINDING         38
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q99714"
FT   BINDING         63
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q99714"
FT   BINDING         64
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q99714"
FT   BINDING         142
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         155
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q99714"
FT   BINDING         159
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q99714"
FT   BINDING         190
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q99714"
SQ   SEQUENCE   247 AA;  25871 MW;  76CA07892E7BBA73 CRC64;
     MASLLNARTA VITGGAQGLG LAIGQRFVAE GARVVLGDVN LEATEVAAKR LGGDDVALAV
     RCDVTQADDV DILIRTAVER FGGLDVMVNN AGITRDATMR TMTEEQFDQV IAVHLKGTWN
     GTRLAAAIMR ERKRGAIVNM SSVSGKVGMV GQTNYSAAKA GIVGMTKAAA KELAHLGIRV
     NAIAPGLIRS AMTEAMPQRI WDQKLAEVPM GRAGEPSEVA SVAVFLASDL SSYMTGTVLD
     VTGGRFI