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IPDB_MYCTO
ID   IPDB_MYCTO              Reviewed;         250 AA.
AC   P9WPV8; L0TD49; P63652; P71848;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 38.
DE   RecName: Full=Cholesterol ring-cleaving hydrolase IpdB subunit {ECO:0000250|UniProtKB:P9WPV9};
DE            EC=4.1.99.- {ECO:0000250|UniProtKB:P9WPV9};
DE   AltName: Full=(3E)-2-(2-carboxylatoethyl)-3-methyl-6-oxocyclohex-1-ene-1-carboxyl-CoA hydrolase beta subunit {ECO:0000250|UniProtKB:P9WPV9};
DE            Short=COCHEA-CoA hydrolase beta subunit {ECO:0000250|UniProtKB:P9WPV9};
GN   Name=ipdB {ECO:0000250|UniProtKB:P9WPV9}; OrderedLocusNames=MT3656;
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: Involved in the final steps of cholesterol and steroid
CC       degradation. Opens the last steroid ring of cholesterol by catalyzing
CC       the hydrolysis of (3E)-2-(2-carboxylatoethyl)-3-methyl-6-oxocyclohex-1-
CC       ene-1-carboxyl-CoA (COCHEA-CoA) to 6-methyl-3,7-dioxodecanedioyl-CoA
CC       (MeDODA-CoA). {ECO:0000250|UniProtKB:P9WPV9}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(3E)-2-(2-carboxylatoethyl)-3-methyl-6-oxocyclohex-1-ene-1-
CC         carboxyl-CoA + H2O = 6-methyl-3,7-dioxodecanedioyl-CoA;
CC         Xref=Rhea:RHEA:66364, ChEBI:CHEBI:15377, ChEBI:CHEBI:167101,
CC         ChEBI:CHEBI:167102; Evidence={ECO:0000250|UniProtKB:P9WPV9};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66365;
CC         Evidence={ECO:0000250|UniProtKB:P9WPV9};
CC   -!- PATHWAY: Steroid metabolism; cholesterol degradation.
CC       {ECO:0000250|UniProtKB:P9WPV9}.
CC   -!- SUBUNIT: Heterotetramer composed of 2 IpdA subunits and 2 IpdB
CC       subunits. {ECO:0000250|UniProtKB:P9WPV9}.
CC   -!- SIMILARITY: Belongs to the 3-oxoacid CoA-transferase subunit B family.
CC       {ECO:0000305}.
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DR   EMBL; AE000516; AAK48016.1; -; Genomic_DNA.
DR   PIR; A70678; A70678.
DR   RefSeq; WP_003419321.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WPV8; -.
DR   SMR; P9WPV8; -.
DR   EnsemblBacteria; AAK48016; AAK48016; MT3656.
DR   GeneID; 45427536; -.
DR   KEGG; mtc:MT3656; -.
DR   PATRIC; fig|83331.31.peg.3937; -.
DR   HOGENOM; CLU_069088_0_0_11; -.
DR   UniPathway; UPA01058; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0008410; F:CoA-transferase activity; IEA:InterPro.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006707; P:cholesterol catabolic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR004165; CoA_trans_fam_I.
DR   InterPro; IPR037171; NagB/RpiA_transferase-like.
DR   SMART; SM00882; CoA_trans; 1.
DR   SUPFAM; SSF100950; SSF100950; 1.
PE   3: Inferred from homology;
KW   Cholesterol metabolism; Lipid metabolism; Lyase; Steroid metabolism;
KW   Sterol metabolism.
FT   CHAIN           1..250
FT                   /note="Cholesterol ring-cleaving hydrolase IpdB subunit"
FT                   /id="PRO_0000426884"
SQ   SEQUENCE   250 AA;  27393 MW;  4278D0CDCBDCF6DE CRC64;
     MSTRAEVCAV ACAELFRDAG EIMISPMTNM ASVGARLARL TFAPDILLTD GEAQLLADTP
     ALGKTGAPNR IEGWMPFGRV FETLAWGRRH VVMGANQVDR YGNQNISAFG PLQRPTRQMF
     GVRGSPGNTI NHATSYWVGN HCKRVFVEAV DVVSGIGYDK VDPDNPAFRF VNVYRVVSNL
     GVFDFGGPDH SMRAVSLHPG VTPGDVRDAT SFEVHDLDAA EQTRLPTDDE LHLIRAVIDP
     KSLRDREIRS
 
 
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