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ECH20_RHOJR
ID   ECH20_RHOJR             Reviewed;         258 AA.
AC   Q0S7P8;
DT   07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   25-MAY-2022, entry version 93.
DE   RecName: Full=(7aS)-7a-methyl-1,5-dioxo-2,3,5,6,7,7a-hexahydro-1H-indene-carboxyl-CoA hydrolase {ECO:0000305};
DE            Short=HIEC-CoA hydrolase {ECO:0000305};
DE            EC=4.1.99.- {ECO:0000269|PubMed:28377529};
GN   Name=echA20 {ECO:0000303|PubMed:28377529};
GN   OrderedLocusNames=RHA1_ro04652 {ECO:0000312|EMBL:ABG96438.1};
OS   Rhodococcus jostii (strain RHA1).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX   NCBI_TaxID=101510;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RHA1;
RX   PubMed=17030794; DOI=10.1073/pnas.0607048103;
RA   McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M., Fernandes C.,
RA   Miyazawa D., Wong W., Lillquist A.L., Wang D., Dosanjh M., Hara H.,
RA   Petrescu A., Morin R.D., Yang G., Stott J.M., Schein J.E., Shin H.,
RA   Smailus D., Siddiqui A.S., Marra M.A., Jones S.J.M., Holt R.,
RA   Brinkman F.S.L., Miyauchi K., Fukuda M., Davies J.E., Mohn W.W.,
RA   Eltis L.D.;
RT   "The complete genome of Rhodococcus sp. RHA1 provides insights into a
RT   catabolic powerhouse.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(2006).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RC   STRAIN=RHA1;
RX   PubMed=28377529; DOI=10.1128/mbio.00321-17;
RA   Crowe A.M., Casabon I., Brown K.L., Liu J., Lian J., Rogalski J.C.,
RA   Hurst T.E., Snieckus V., Foster L.J., Eltis L.D.;
RT   "Catabolism of the last two steroid rings in Mycobacterium tuberculosis and
RT   other bacteria.";
RL   MBio 8:e00321-e00321(2017).
CC   -!- FUNCTION: Involved in the final steps of cholesterol and steroid
CC       degradation (PubMed:28377529). Catalyzes the hydrolytic ring D opening
CC       of (7aS)-7a-methyl-1,5-dioxo-2,3,5,6,7,7a-hexahydro-1H-indene-carboxyl-
CC       CoA (HIEC-CoA) to (3E)-2-(2-carboxylatoethyl)-3-methyl-6-oxocyclohex-1-
CC       ene-1-carboxyl-CoA (COCHEA-CoA) (PubMed:28377529).
CC       {ECO:0000269|PubMed:28377529}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(7aS)-7a-methyl-1,5-dioxo-2,3,5,6,7,7a-hexahydro-1H-indene-
CC         carboxyl-CoA + H2O = (3E)-2-(2-carboxylatoethyl)-3-methyl-6-
CC         oxocyclohex-1-ene-1-carboxyl-CoA + H(+); Xref=Rhea:RHEA:66360,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:167100,
CC         ChEBI:CHEBI:167101; Evidence={ECO:0000269|PubMed:28377529};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66361;
CC         Evidence={ECO:0000269|PubMed:28377529};
CC   -!- PATHWAY: Steroid metabolism; cholesterol degradation.
CC       {ECO:0000269|PubMed:28377529}.
CC   -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.
CC       {ECO:0000305}.
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DR   EMBL; CP000431; ABG96438.1; -; Genomic_DNA.
DR   RefSeq; WP_007300903.1; NC_008268.1.
DR   AlphaFoldDB; Q0S7P8; -.
DR   SMR; Q0S7P8; -.
DR   STRING; 101510.RHA1_ro04652; -.
DR   EnsemblBacteria; ABG96438; ABG96438; RHA1_ro04652.
DR   KEGG; rha:RHA1_ro04652; -.
DR   PATRIC; fig|101510.16.peg.4695; -.
DR   eggNOG; COG1024; Bacteria.
DR   HOGENOM; CLU_009834_7_6_11; -.
DR   OMA; CAGVDIK; -.
DR   UniPathway; UPA01058; -.
DR   Proteomes; UP000008710; Chromosome.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006707; P:cholesterol catabolic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR   InterPro; IPR001753; Enoyl-CoA_hydra/iso.
DR   Pfam; PF00378; ECH_1; 1.
DR   SUPFAM; SSF52096; SSF52096; 1.
PE   1: Evidence at protein level;
KW   Cholesterol metabolism; Lipid metabolism; Lyase; Reference proteome;
KW   Steroid metabolism; Sterol metabolism.
FT   CHAIN           1..258
FT                   /note="(7aS)-7a-methyl-1,5-dioxo-2,3,5,6,7,7a-hexahydro-1H-
FT                   indene-carboxyl-CoA hydrolase"
FT                   /id="PRO_0000452311"
SQ   SEQUENCE   258 AA;  27450 MW;  636AFADBD0D0F6CE CRC64;
     MGITSTTDGD GITTVTVDYP PVNAIPSRGW FELADAVLDA GRNPDTHVVI LRAEGRGFNA
     GVDIKEMQAT DGYGALVDAN RGCAAAFAAV YDCAVPVVVA VNGFCVGGGI GLVGNADVIV
     ASDDAVFGLP EVDRGALGAA THLARLVPQH MMRTLYYTAQ NVTAQQLQHF GSVYEVVPRE
     KLDDTARDIA AKIAAKDTRV IRCAKEAING IDPVDVKTSY RLEQGYTFEL NLAGVSDEHR
     DEFVETGKPR SHSNNRKG
 
 
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