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Y0809_MYCTO
ID   Y0809_MYCTO             Reviewed;         566 AA.
AC   Q7D9A2;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=KsdD-like steroid dehydrogenase MT0809;
DE            EC=1.3.99.-;
GN   OrderedLocusNames=MT0809;
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: Able to catalyze the elimination of the C-1 and C-2 hydrogen
CC       atoms of the A-ring from the polycyclic ring structure of 3-
CC       ketosteroids. {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC   -!- PATHWAY: Lipid metabolism; steroid biosynthesis.
CC   -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family.
CC       {ECO:0000305}.
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DR   EMBL; AE000516; AAK45051.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q7D9A2; -.
DR   SMR; Q7D9A2; -.
DR   EnsemblBacteria; AAK45051; AAK45051; MT0809.
DR   KEGG; mtc:MT0809; -.
DR   PATRIC; fig|83331.31.peg.869; -.
DR   HOGENOM; CLU_022946_0_0_11; -.
DR   UniPathway; UPA00062; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0033765; F:steroid dehydrogenase activity, acting on the CH-CH group of donors; IEA:UniProt.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006694; P:steroid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.50.50.60; -; 1.
DR   Gene3D; 3.90.700.10; -; 1.
DR   InterPro; IPR003953; FAD-binding_2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
DR   InterPro; IPR014614; UCP036654.
DR   PANTHER; PTHR43260; PTHR43260; 1.
DR   Pfam; PF00890; FAD_binding_2; 1.
DR   PIRSF; PIRSF036654; UCP036654; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
PE   3: Inferred from homology;
KW   FAD; Flavoprotein; Lipid degradation; Lipid metabolism; Oxidoreductase;
KW   Steroid metabolism.
FT   CHAIN           1..566
FT                   /note="KsdD-like steroid dehydrogenase MT0809"
FT                   /id="PRO_0000403956"
FT   BINDING         23..54
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   566 AA;  61296 MW;  005B476B84ECE128 CRC64;
     MALTCTDMSD AVAGSDAEGL TADAIVVGAG LAGLVAACEL ADRGLRVLIL DQENRANVGG
     QAFWSFGGLF LVNSPEQRRL GIRDSHELAL QDWLGTAAFD RPEDYWPEQW AHAYVDFAAG
     EKRSWLRARG LKIFPLVGWA ERGGYDAQGH GNSVPRFHIT WGTGPALVDI FVRQLRDRPT
     VRFAHRHQVD KLIVEGNAVT GVRGTVLEPS DEPRGAPSSR KSVGKFEFRA SAVIVASGGI
     GGNHELVRKN WPRRMGRIPK QLLSGVPAHV DGRMIGIAQK AGAAVINPDR MWHYTEGITN
     YDPIWPRHGI RIIPGPSSLW LDAAGKRLPV PLFPGFDTLG TLEYITKSGH DYTWFVLNAK
     IIEKEFALSG QEQNPDLTGR RLGQLLRSRA HAGPPGPVQA FIDRGVDFVH ANSLRELVAA
     MNELPDVVPL DYETVAAAVT ARDREVVNKY SKDGQITAIR AARRYRGDRF GRVVAPHRLT
     DPKAGPLIAV KLHILTRKTL GGIETDLDAR VLKADGTPLA GLYAAGEVAG FGGGGVHGYR
     ALEGTFLGGC IFSGRAAGRG AAEDIR
 
 
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