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ECH20_MYCTU
ID   ECH20_MYCTU             Reviewed;         247 AA.
AC   I6Y3U6;
DT   07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2012, sequence version 1.
DT   03-AUG-2022, entry version 65.
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:0000250|UniProtKB:Q0S7P8};
GN   Name=echA20 {ECO:0000303|PubMed:28377529};
GN   OrderedLocusNames=Rv3550 {ECO:0000312|EMBL:CCP46372.1};
OS   Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83332;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=9634230; DOI=10.1038/31159;
RA   Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA   Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA   Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA   Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA   Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA   Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA   Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA   Barrell B.G.;
RT   "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT   genome sequence.";
RL   Nature 393:537-544(1998).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA   Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA   Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA   Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA   Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT   "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT   mass spectrometry.";
RL   Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN   [3]
RP   FUNCTION, AND PATHWAY.
RC   STRAIN=Erdman;
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) (By similarity).
CC       {ECO:0000250|UniProtKB:Q0S7P8, 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:0000250|UniProtKB:Q0S7P8};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66361;
CC         Evidence={ECO:0000250|UniProtKB:Q0S7P8};
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; AL123456; CCP46372.1; -; Genomic_DNA.
DR   RefSeq; NP_218067.1; NC_000962.3.
DR   RefSeq; WP_003419315.1; NZ_NVQJ01000014.1.
DR   AlphaFoldDB; I6Y3U6; -.
DR   SMR; I6Y3U6; -.
DR   STRING; 83332.Rv3550; -.
DR   PaxDb; I6Y3U6; -.
DR   DNASU; 888232; -.
DR   GeneID; 888232; -.
DR   KEGG; mtu:Rv3550; -.
DR   PATRIC; fig|83332.111.peg.3955; -.
DR   TubercuList; Rv3550; -.
DR   eggNOG; COG1024; Bacteria.
DR   OMA; CAGVDIK; -.
DR   PhylomeDB; I6Y3U6; -.
DR   BioCyc; MetaCyc:G185E-7827-MON; -.
DR   UniPathway; UPA01058; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0004300; F:enoyl-CoA hydratase activity; IBA:GO_Central.
DR   GO; GO:0006707; P:cholesterol catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006635; P:fatty acid beta-oxidation; IBA:GO_Central.
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..247
FT                   /note="(7aS)-7a-methyl-1,5-dioxo-2,3,5,6,7,7a-hexahydro-1H-
FT                   indene-carboxyl-CoA hydrolase"
FT                   /id="PRO_0000452310"
SQ   SEQUENCE   247 AA;  26333 MW;  B833E1DA520386CE CRC64;
     MPITSTTPEP GIVAVTVDYP PVNAIPSKAW FDLADAVTAA GANSDTRAVI LRAEGRGFNA
     GVDIKEMQRT EGFTALIDAN RGCFAAFRAV YECAVPVIAA VNGFCVGGGI GLVGNSDVIV
     ASEDATFGLP EVERGALGAA THLSRLVPQH LMRRLFFTAA TVDAATLQHF GSVHEVVSRD
     QLDEAALRVA RDIAAKDTRV IRAAKEALNF IDVQRVNASY RMEQGFTFEL NLAGVADEHR
     DAFVKKS
 
 
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