Y0687_MYCTO
ID Y0687_MYCTO Reviewed; 275 AA.
AC P9WGS6; L0T4F2; P95033; Q7D9F4;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 37.
DE RecName: Full=Uncharacterized NAD-dependent oxidoreductase MT0715;
DE EC=1.-.-.-;
GN OrderedLocusNames=MT0715;
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; AAK44941.1; -; Genomic_DNA.
DR PIR; B70640; B70640.
DR RefSeq; WP_003403468.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WGS6; -.
DR SMR; P9WGS6; -.
DR EnsemblBacteria; AAK44941; AAK44941; MT0715.
DR GeneID; 45424649; -.
DR KEGG; mtc:MT0715; -.
DR PATRIC; fig|83331.31.peg.763; -.
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..275
FT /note="Uncharacterized NAD-dependent oxidoreductase MT0715"
FT /id="PRO_0000428310"
FT ACT_SITE 173
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 20..22
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 41..42
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 80..81
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 107
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 160
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 177
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 206..208
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
SQ SEQUENCE 275 AA; 29028 MW; 43E9EB57986474C3 CRC64;
MSARGGSLHG RVAFVTGAAR AQGRSHAVRL AREGADIVAL DICAPVSGSV TYPPATSEDL
GETVRAVEAE GRKVLAREVD IRDDAELRRL VADGVEQFGR LDIVVANAGV LGWGRLWELT
DEQWETVIGV NLTGTWRTLR ATVPAMIDAG NGGSIVVVSS SAGLKATPGN GHYAASKHAL
VALTNTLAIE LGEFGIRVNS IHPYSVDTPM IEPEAMIQTF AKHPGYVHSF PPMPLQPKGF
MTPDEISDVV VWLAGDGSGA LSGNQIPVDK GALKY