ID K1QGC5_CRAGI Unreviewed; 246 AA.
AC K1QGC5;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Enoyl-CoA hydratase, mitochondrial {ECO:0000256|ARBA:ARBA00041110};
DE EC=4.2.1.17 {ECO:0000256|ARBA:ARBA00012076};
DE EC=5.3.3.8 {ECO:0000256|ARBA:ARBA00012064};
DE AltName: Full=Enoyl-CoA hydratase 1 {ECO:0000256|ARBA:ARBA00042381};
DE AltName: Full=Short-chain enoyl-CoA hydratase {ECO:0000256|ARBA:ARBA00041421};
GN ORFNames=CGI_10006089 {ECO:0000313|EMBL:EKC32958.1};
OS Crassostrea gigas (Pacific oyster) (Crassostrea angulata).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC Autobranchia; Pteriomorphia; Ostreida; Ostreoidea; Ostreidae; Crassostrea.
OX NCBI_TaxID=29159 {ECO:0000313|EMBL:EKC32958.1};
RN [1] {ECO:0000313|EMBL:EKC32958.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=05x7-T-G4-1.051#20 {ECO:0000313|EMBL:EKC32958.1};
RX PubMed=22992520; DOI=10.1038/nature11413;
RA Zhang G., Fang X., Guo X., Li L., Luo R., Xu F., Yang P., Zhang L.,
RA Wang X., Qi H., Xiong Z., Que H., Xie Y., Holland P.W., Paps J., Zhu Y.,
RA Wu F., Chen Y., Wang J., Peng C., Meng J., Yang L., Liu J., Wen B.,
RA Zhang N., Huang Z., Zhu Q., Feng Y., Mount A., Hedgecock D., Xu Z., Liu Y.,
RA Domazet-Loso T., Du Y., Sun X., Zhang S., Liu B., Cheng P., Jiang X.,
RA Li J., Fan D., Wang W., Fu W., Wang T., Wang B., Zhang J., Peng Z., Li Y.,
RA Li N., Wang J., Chen M., He Y., Tan F., Song X., Zheng Q., Huang R.,
RA Yang H., Du X., Chen L., Yang M., Gaffney P.M., Wang S., Luo L., She Z.,
RA Ming Y., Huang W., Zhang S., Huang B., Zhang Y., Qu T., Ni P., Miao G.,
RA Wang J., Wang Q., Steinberg C.E., Wang H., Li N., Qian L., Zhang G., Li Y.,
RA Yang H., Liu X., Wang J., Yin Y., Wang J.;
RT "The oyster genome reveals stress adaptation and complexity of shell
RT formation.";
RL Nature 490:49-54(2012).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-2-methylpropenoyl-CoA + H2O = (S)-3-hydroxyisobutanoyl-
CC CoA; Xref=Rhea:RHEA:31175, ChEBI:CHEBI:15377, ChEBI:CHEBI:62500,
CC ChEBI:CHEBI:62611; Evidence={ECO:0000256|ARBA:ARBA00036655};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31176;
CC Evidence={ECO:0000256|ARBA:ARBA00036655};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3S)-3-hydroxybutanoyl-CoA = (2E)-butenoyl-CoA + H2O;
CC Xref=Rhea:RHEA:26558, ChEBI:CHEBI:15377, ChEBI:CHEBI:57316,
CC ChEBI:CHEBI:57332; Evidence={ECO:0000256|ARBA:ARBA00036765};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:26560;
CC Evidence={ECO:0000256|ARBA:ARBA00036765};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-hydroxybutanoyl-CoA = (2E)-butenoyl-CoA + H2O;
CC Xref=Rhea:RHEA:45584, ChEBI:CHEBI:15377, ChEBI:CHEBI:57332,
CC ChEBI:CHEBI:78611; Evidence={ECO:0000256|ARBA:ARBA00036643};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:45586;
CC Evidence={ECO:0000256|ARBA:ARBA00036643};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-hydroxyisovaleryl-CoA = 3-methyl-(2E)-butenoyl-CoA + H2O;
CC Xref=Rhea:RHEA:31079, ChEBI:CHEBI:15377, ChEBI:CHEBI:57344,
CC ChEBI:CHEBI:62555; Evidence={ECO:0000256|ARBA:ARBA00035855};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31081;
CC Evidence={ECO:0000256|ARBA:ARBA00035855};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-hydroxypropanoyl-CoA = acryloyl-CoA + H2O;
CC Xref=Rhea:RHEA:26518, ChEBI:CHEBI:15377, ChEBI:CHEBI:57367,
CC ChEBI:CHEBI:58528; Evidence={ECO:0000256|ARBA:ARBA00036137};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:26520;
CC Evidence={ECO:0000256|ARBA:ARBA00036137};
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:ARBA00035854};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:16107;
CC Evidence={ECO:0000256|ARBA:ARBA00035854};
CC -!- SUBUNIT: Homohexamer; dimer of trimers.
CC {ECO:0000256|ARBA:ARBA00038629}.
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; JH817508; EKC32958.1; -; Genomic_DNA.
DR AlphaFoldDB; K1QGC5; -.
DR HOGENOM; CLU_009834_7_6_1; -.
DR InParanoid; K1QGC5; -.
DR OMA; KEMQAMD; -.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
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; 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;
SQ SEQUENCE 246 AA; 26174 MW; 549C15D686F052AD CRC64;
MNRPEARNAL GKQFLREFAD CTNVVKFDKN LRVVILRSLV KGVFCAGADL KERAKMTNEE
TGPFVAGLRA SVSEVANLPM PVVAAIDGFA LGGGLEVALA CDIRVSSDDA KMGLVETRLA
IIPGGGGTQR LARAIGPAKA KELIFAARVF TGKEAAEMGV VNHSVEQNSD GDAAYQRALK
LGQEILPQGP VALRAAKFAI NRGSEVDIAS GLSFEEAGYS QVINTKDRLE GLSAFKEKRP
PRFSGE
//
