ID   IPDA_MYCTO              Reviewed;         292 AA.
AC   P9WPW0; L0TCX1; P71850;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 35.
DE   RecName: Full=Cholesterol ring-cleaving hydrolase IpdA subunit {ECO:0000250|UniProtKB:P9WPW1};
DE            EC=4.1.99.- {ECO:0000250|UniProtKB:P9WPW1};
DE   AltName: Full=(3E)-2-(2-carboxylatoethyl)-3-methyl-6-oxocyclohex-1-ene-1-carboxyl-CoA hydrolase alpha subunit {ECO:0000250|UniProtKB:P9WPW1};
DE            Short=COCHEA-CoA hydrolase alpha subunit {ECO:0000250|UniProtKB:P9WPW1};
GN   Name=ipdA {ECO:0000250|UniProtKB:P9WPW1}; OrderedLocusNames=MT3655;
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:P9WPW1}.
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:P9WPW1};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66365;
CC         Evidence={ECO:0000250|UniProtKB:P9WPW1};
CC   -!- PATHWAY: Steroid metabolism; cholesterol degradation.
CC       {ECO:0000250|UniProtKB:P9WPW1}.
CC   -!- SUBUNIT: Heterotetramer composed of 2 IpdA subunits and 2 IpdB
CC       subunits. {ECO:0000250|UniProtKB:P9WPW1}.
CC   -!- SIMILARITY: Belongs to the 3-oxoacid CoA-transferase subunit A family.
CC       {ECO:0000305}.
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DR   EMBL; AE000516; AAK48015.1; -; Genomic_DNA.
DR   PIR; H70677; H70677.
DR   RefSeq; WP_003900094.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WPW0; -.
DR   SMR; P9WPW0; -.
DR   EnsemblBacteria; AAK48015; AAK48015; MT3655.
DR   KEGG; mtc:MT3655; -.
DR   PATRIC; fig|83331.31.peg.3936; -.
DR   HOGENOM; CLU_049557_1_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   Pfam; PF01144; CoA_trans; 1.
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..292
FT                   /note="Cholesterol ring-cleaving hydrolase IpdA subunit"
FT                   /id="PRO_0000426883"
SQ   SEQUENCE   292 AA;  31723 MW;  5C841A83422E4D5D CRC64;
     MPDKRTALDD AVAQLRSGMT IGIAGWGSRR KPMAFVRAIL RSDVTDLTVV TYGGPDLGLL
     CSAGKVKRVY YGFVSLDSPP FYDPWFAHAR TSGAIEAREM DEGMLRCGLQ AAAQRLPFLP
     IRAGLGSSVP QFWAGELQTV TSPYPAPGGG YETLIAMPAL RLDAAFAHLN LGDSHGNAAY
     TGIDPYFDDL FLMAAERRFL SVERIVATEE LVKSVPPQAL LVNRMMVDAI VEAPGGAHFT
     TAAPDYGRDE QFQRHYAEAA STQVGWQQFV HTYLSGTEAD YQAAVHNFGA SR