ID   P96404_MYCTU            Unreviewed;       262 AA.
AC   P96404; F2GM20; I6XUR1; Q7DA88;
DT   01-MAY-1997, integrated into UniProtKB/TrEMBL.
DT   01-MAY-1997, sequence version 1.
DT   02-SEP-2026, entry version 171.
DE   RecName: Full=Enoyl-CoA hydratase EchA19 {ECO:0000256|ARBA:ARBA00068722};
GN   Name=echA1 {ECO:0000313|EMBL:CCP42950.1};
GN   OrderedLocusNames=Rv0222 {ECO:0000313|EMBL:CCP42950.1};
OS   Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Mycobacteriaceae; Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83332 {ECO:0000313|EMBL:CCP42950.1, ECO:0000313|Proteomes:UP000001584};
RN   [1] {ECO:0000313|EMBL:CCP42950.1, ECO:0000313|Proteomes:UP000001584}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv {ECO:0000313|Proteomes:UP000001584};
RX   PubMed=9634230; DOI=10.1038/31159;
RA   Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C., Harris D.,
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., Devlin K.,
RA   Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA   Krogh A., McLean J., Moule S., Murphy L., Oliver K., Osborne J.,
RA   Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton J.,
RA   Squares R., Squares S., 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] {ECO:0007829|PubMed:21969609}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21969609; DOI=10.1074/mcp.M111.011445;
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] {ECO:0007829|PDB:5KJP}
RP   X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS).
RG   Center for Structural Genomics of Infectious Diseases (CSGID);
RA   Nocek B., Hatzos-Skintges C., Anderson W.F., Joachimiak A.;
RT   "Crystal structure of enoyl-CoA hydratase from Mycobacterium tuberculosis
RT   H37Rv.";
RL   Submitted (JUN-2016) to the PDB data bank.
RN   [4] {ECO:0007829|PDB:6LDZ}
RP   X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS).
RX   PubMed=31942069; DOI=10.1038/s41586-019-1915-7;
RA   Wang L., Wu J., Li J., Yang H., Tang T., Liang H., Zuo M., Wang J., Liu H.,
RA   Liu F., Chen J., Liu Z., Wang Y., Peng C., Wu X., Zheng R., Huang X.,
RA   Ran Y., Rao Z., Ge B.;
RT   "Host-mediated ubiquitination of a mycobacterial protein suppresses
RT   immunity.";
RL   Nature 577:682-688(2020).
CC   -!- FUNCTION: Could possibly oxidize fatty acids using specific components.
CC       {ECO:0000256|ARBA:ARBA00002994}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(22E)-3-oxochola-4,22-dien-24-oyl-CoA + H2O = (22R)-hydroxy-3-
CC         oxo-chol-4-ene-24-oyl-CoA; Xref=Rhea:RHEA:72575, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:136759, ChEBI:CHEBI:192383;
CC         Evidence={ECO:0000256|ARBA:ARBA00050550};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a (3S)-3-hydroxyacyl-CoA = a (2E)-enoyl-CoA + H2O;
CC         Xref=Rhea:RHEA:16105, ChEBI:CHEBI:15377, ChEBI:CHEBI:57318,
CC         ChEBI:CHEBI:58856; EC=4.2.1.17;
CC         Evidence={ECO:0000256|ARBA:ARBA00023709};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 4-saturated-(3S)-3-hydroxyacyl-CoA = a (3E)-enoyl-CoA + H2O;
CC         Xref=Rhea:RHEA:20724, ChEBI:CHEBI:15377, ChEBI:CHEBI:58521,
CC         ChEBI:CHEBI:137480; EC=4.2.1.17;
CC         Evidence={ECO:0000256|ARBA:ARBA00023717};
CC   -!- PATHWAY: Steroid metabolism; cholesterol degradation.
CC       {ECO:0000256|ARBA:ARBA00049645}.
CC   -!- SUBUNIT: Homotrimer; substrate probably binds in elongated tunnels
CC       between the subunits. {ECO:0000256|ARBA:ARBA00063987}.
CC   -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.
CC       {ECO:0000256|ARBA:ARBA00005254, ECO:0000256|RuleBase:RU003707}.
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DR   EMBL; AL123456; CCP42950.1; -; Genomic_DNA.
DR   RefSeq; NP_214736.1; NC_000962.3.
DR   RefSeq; WP_003899864.1; NC_000962.3.
DR   PDB; 5KJP; X-ray; 1.80 A; A=1-262.
DR   PDB; 6LDZ; X-ray; 2.40 A; A=1-262.
DR   AlphaFoldDB; P96404; -.
DR   SMR; P96404; -.
DR   FunCoup; P96404; 83.
DR   STRING; 83332.Rv0222; -.
DR   PaxDb; 83332-Rv0222; -.
DR   DNASU; 886723; -.
DR   GeneID; 886723; -.
DR   KEGG; mtu:Rv0222; -.
DR   KEGG; mtv:RVBD_0222; -.
DR   PATRIC; fig|83332.111.peg.253; -.
DR   TubercuList; Rv0222; -.
DR   eggNOG; COG1024; Bacteria.
DR   InParanoid; P96404; -.
DR   OrthoDB; 4284283at2; -.
DR   PhylomeDB; P96404; -.
DR   Proteomes; UP000001584; Chromosome.
DR   AbasyAtlas; P96404; -.
DR   GO; GO:0004300; F:enoyl-CoA hydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006635; P:fatty acid beta-oxidation; IBA:GO_Central.
DR   CDD; cd06558; crotonase-like; 1.
DR   FunFam; 3.90.226.10:FF:000042; Enoyl-CoA hydratase EchA1; 1.
DR   Gene3D; 3.90.226.10; 2-enoyl-CoA Hydratase, Chain A, domain 1; 1.
DR   Gene3D; 1.10.12.10; Lyase 2-enoyl-coa Hydratase, Chain A, domain 2; 1.
DR   InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR   InterPro; IPR018376; Enoyl-CoA_hyd/isom_CS.
DR   InterPro; IPR001753; Enoyl-CoA_hydra/iso.
DR   InterPro; IPR014748; Enoyl-CoA_hydra_C.
DR   NCBIfam; NF006100; PRK08252.1; 1.
DR   PANTHER; PTHR43802; ENOYL-COA HYDRATASE; 1.
DR   PANTHER; PTHR43802:SF1; IP11341P-RELATED; 1.
DR   Pfam; PF00378; ECH_1; 1.
DR   SUPFAM; SSF52096; ClpP/crotonase; 1.
DR   PROSITE; PS00166; ENOYL_COA_HYDRATASE; 1.
DR   PDBsum; 5KJP; -.
DR   PDBsum; 6LDZ; -.
PE   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:5KJP, ECO:0007829|PDB:6LDZ};
KW   Cholesterol metabolism {ECO:0000256|ARBA:ARBA00022548};
KW   Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001584};
KW   Steroid metabolism {ECO:0000256|ARBA:ARBA00023221};
KW   Sterol metabolism {ECO:0000256|ARBA:ARBA00023166}.
FT   DOMAIN          19..261
FT                   /note="Enoyl-CoA hydratase/isomerase-like"
FT                   /evidence="ECO:0000259|Pfam:PF00378"
SQ   SEQUENCE   262 AA;  27280 MW;  D58E415D6DAA2772 CRC64;
     MSSESDAANT EPEVLVEQRD RILIITINRP KAKNAVNAAV SRGLADAMDQ LDGDAGLSVA
     ILTGGGGSFC AGMDLKAFAR GENVVVEGRG LGFTERPPTK PLIAAVEGYA LAGGTELALA
     ADLIVAARDS AFGIPEVKRG LVAGGGGLLR LPERIPYAIA MELALTGDNL PAERAHELGL
     VNVLAEPGTA LDAAIALAEK ITANGPLAVV ATKRIITESR GWSPDTMFAE QMKILVPVFT
     SNDAKEGAIA FAERRRPRWT GT
//