SADH_MYCTO
ID SADH_MYCTO Reviewed; 276 AA.
AC P9WGP8; F2GNY3; L0TEA6; O53302; Q7D656;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 44.
DE RecName: Full=Putative oxidoreductase SadH;
DE EC=1.-.-.-;
GN Name=sadH; OrderedLocusNames=MT3170;
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 -!- FUNCTION: Required for maintaining the appropriate mycolic acid
CC composition and permeability of the envelope on its exposure to acidic
CC pH. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; AE000516; AAK47506.1; -; Genomic_DNA.
DR PIR; A70853; A70853.
DR RefSeq; WP_003416074.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WGP8; -.
DR SMR; P9WGP8; -.
DR EnsemblBacteria; AAK47506; AAK47506; MT3170.
DR KEGG; mtc:MT3170; -.
DR PATRIC; fig|83331.31.peg.3416; -.
DR HOGENOM; CLU_010194_2_1_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 Pfam; PF00106; adh_short; 1.
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 Oxidoreductase.
FT CHAIN 1..276
FT /note="Putative oxidoreductase SadH"
FT /id="PRO_0000428324"
FT ACT_SITE 155
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 142
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 276 AA; 29217 MW; 4721366EEBE3E270 CRC64;
MSSFEGKVAV ITGAGSGIGR ALALNLSEKR AKLALSDVDT DGLAKTVRLA QALGAQVKSD
RLDVAEREAV LAHADAVVAH FGTVHQVYNN AGIAYNGNVD KSEFKDIERI IDVDFWGVVN
GTKAFLPHVI ASGDGHIVNI SSLFGLIAVP GQSAYNAAKF AVRGFTEALR QEMLVARHPV
KVTCVHPGGI KTAVARNATV ADGEDQQTFA EFFDRRLALH SPEMAAKTIV NGVAKGQARV
VVGLEAKAVD VLARIMGSSY QRLVAAGVAK FFPWAK