ID   C4LHC3_CORK4            Unreviewed;       286 AA.
AC   C4LHC3;
DT   07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   07-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 73.
DE   SubName: Full=Enoyl-CoA hydratase {ECO:0000313|EMBL:ACR17228.1};
DE            EC=4.2.1.17 {ECO:0000313|EMBL:ACR17228.1};
GN   Name=echA2 {ECO:0000313|EMBL:ACR17228.1};
GN   OrderedLocusNames=ckrop_0451 {ECO:0000313|EMBL:ACR17228.1};
OS   Corynebacterium kroppenstedtii (strain DSM 44385 / JCM 11950 / CIP 105744 /
OS   CCUG 35717).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=645127 {ECO:0000313|EMBL:ACR17228.1, ECO:0000313|Proteomes:UP000001473};
RN   [1] {ECO:0000313|EMBL:ACR17228.1, ECO:0000313|Proteomes:UP000001473}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44385 / JCM 11950 / CIP 105744 / CCUG 35717
RC   {ECO:0000313|Proteomes:UP000001473};
RX   PubMed=18430482; DOI=10.1016/j.jbiotec.2008.03.004;
RA   Tauch A., Schneider J., Szczepanowski R., Tilker A., Viehoever P.,
RA   Gartemann K.-H., Arnold W., Blom J., Brinkrolf K., Brune I., Goetker S.,
RA   Weisshaar B., Goesmann A., Droege M., Puehler A.;
RT   "Ultrafast pyrosequencing of Corynebacterium kroppenstedtii DSM44385
RT   revealed insights into the physiology of a lipophilic corynebacterium that
RT   lacks mycolic acids.";
RL   J. Biotechnol. 136:22-30(2008).
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; CP001620; ACR17228.1; -; Genomic_DNA.
DR   AlphaFoldDB; C4LHC3; -.
DR   STRING; 645127.ckrop_0451; -.
DR   KEGG; ckp:ckrop_0451; -.
DR   eggNOG; COG1024; Bacteria.
DR   HOGENOM; CLU_009834_7_2_11; -.
DR   OrthoDB; 3569436at2; -.
DR   Proteomes; UP000001473; Chromosome.
DR   GO; GO:0004300; F:enoyl-CoA hydratase activity; IEA:UniProtKB-EC.
DR   CDD; cd06558; crotonase-like; 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   PANTHER; PTHR11941:SF54; ENOYL-COA HYDRATASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11941; ENOYL-COA HYDRATASE-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:ACR17228.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001473}.
SQ   SEQUENCE   286 AA;  30399 MW;  E0B97AE2CB2B0CD7 CRC64;
     MTNENNVTSA SPDGEVTLDI LPVDNDTPTD GEPQPRVAVI TIRRDHKRNS LNADVCSQIA
     TYVHEAENTD SVRAILLRGE GKAFCAGADL AGGVYTSAFH HNLDAMLTSI THSPLPVIAD
     VHGPAVGAGT QLAMACDLRV VGESGWFSVP VVRLGIAVDP WTIHRAVELL GGARARSFLY
     TAERLEPDAA ISAGLASSRG NHDDAWQVAV DQATNAPLTL RYLKAVFNQV VPTGVAQGGS
     SEGTGHDDEV LTAVHERLRT ECWDSDDAAE ARAARSEKRS SVFKGK
//