ID A0A0N9NFU1_9ACTN Unreviewed; 268 AA.
AC A0A0N9NFU1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE SubName: Full=Enoyl-CoA hydratase {ECO:0000313|EMBL:ALG86550.1};
DE EC=4.2.1.17 {ECO:0000313|EMBL:ALG86550.1};
GN ORFNames=ACH46_02740 {ECO:0000313|EMBL:ALG86550.1};
OS Gordonia phthalatica.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Gordonia.
OX NCBI_TaxID=1136941 {ECO:0000313|EMBL:ALG86550.1, ECO:0000313|Proteomes:UP000063789};
RN [1] {ECO:0000313|Proteomes:UP000063789}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QH-11 {ECO:0000313|Proteomes:UP000063789};
RA Jin D., Kong X., Bai Z.;
RT "Complete genome sequence and metabolic analysis of phthalate degradation
RT pathway in Gordonia sp. QH-11.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ALG86550.1, ECO:0000313|Proteomes:UP000063789}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QH-11 {ECO:0000313|EMBL:ALG86550.1,
RC ECO:0000313|Proteomes:UP000063789};
RX PubMed=29068282; DOI=10.1099/ijsem.0.002430;
RA Jin D., Kong X., Jia M., Yu X., Wang X., Zhuang X., Deng Y., Bai Z.;
RT "Gordonia phthalatica sp. nov., a di-n-butyl phthalate-degrading bacterium
RT isolated from activated sludge.";
RL Int. J. Syst. Evol. Microbiol. 67:5128-5133(2017).
CC -!- FUNCTION: Could possibly oxidize fatty acids using specific components.
CC {ECO:0000256|ARBA:ARBA00002994}.
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 -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.
CC {ECO:0000256|ARBA:ARBA00005254, ECO:0000256|RuleBase:RU003707}.
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DR EMBL; CP011853; ALG86550.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N9NFU1; -.
DR STRING; 1136941.ACH46_02740; -.
DR KEGG; goq:ACH46_02740; -.
DR PATRIC; fig|1136941.3.peg.551; -.
DR OrthoDB; 4699757at2; -.
DR Proteomes; UP000063789; Chromosome.
DR GO; GO:0004300; F:enoyl-CoA hydratase activity; IEA:UniProtKB-EC.
DR CDD; cd06558; crotonase-like; 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 PANTHER; PTHR43459; ENOYL-COA HYDRATASE; 1.
DR PANTHER; PTHR43459:SF3; ENOYL-COA HYDRATASE ECHA15 (ENOYL HYDRASE) (UNSATURATED ACYL-COA HYDRATASE) (CROTONASE)-RELATED; 1.
DR Pfam; PF00378; ECH_1; 1.
DR SUPFAM; SSF52096; ClpP/crotonase; 1.
DR PROSITE; PS00166; ENOYL_COA_HYDRATASE; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000313|EMBL:ALG86550.1}.
SQ SEQUENCE 268 AA; 28754 MW; 0712C2E2986A6524 CRC64;
MNFSDYQHLL FERRDNGVLL LTLNRPDKYN ATNEVMHAEL ARVFPEISAD PETRVVVVTG
AGKAFSAGGD LSMVEAMAGD HQRVADMLDE MSRLVYGIID CAKPVVSAVN GVAVGAGTVV
ALLSDISVCA EDAKLGDGHV KLGVAAGDHA AIIWPLLAGM AKAKYYLMTG EMITGAEAER
IGLVTKALPR DEVLDEALRI ADVMATGSQN AIRWTKKALN NWLRNAGPIF DQSAAYEMLC
FMAPDVVEGY TSLREKRAPQ FPSAAPTA
//