ID A0A182W1P2_9DIPT Unreviewed; 543 AA.
AC A0A182W1P2;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
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};
OS Anopheles minimus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=112268 {ECO:0000313|EnsemblMetazoa:AMIN004252-PA, ECO:0000313|Proteomes:UP000075920};
RN [1] {ECO:0000313|Proteomes:UP000075920}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MINIMUS1 {ECO:0000313|Proteomes:UP000075920};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Walton C., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Anopheles minimus MINIMUS1.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:AMIN004252-PA}
RP IDENTIFICATION.
RC STRAIN=MINIMUS1 {ECO:0000313|EnsemblMetazoa:AMIN004252-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
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 SPCS3 family.
CC {ECO:0000256|ARBA:ARBA00009289}.
CC -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.
CC {ECO:0000256|ARBA:ARBA00005254, ECO:0000256|RuleBase:RU003707}.
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DR AlphaFoldDB; A0A182W1P2; -.
DR STRING; 112268.A0A182W1P2; -.
DR EnsemblMetazoa; AMIN004252-RA; AMIN004252-PA; AMIN004252.
DR VEuPathDB; VectorBase:AMIN004252; -.
DR OrthoDB; 177540at2759; -.
DR Proteomes; UP000075920; Unassembled WGS sequence.
DR GO; GO:0005787; C:signal peptidase complex; IEA:InterPro.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0006465; P:signal peptide processing; 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 InterPro; IPR007653; SPC3.
DR PANTHER; PTHR11941:SF54; ENOYL-COA HYDRATASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11941; ENOYL-COA HYDRATASE-RELATED; 1.
DR Pfam; PF00378; ECH_1; 1.
DR Pfam; PF04573; SPC22; 1.
DR SUPFAM; SSF52096; ClpP/crotonase; 1.
DR PROSITE; PS00166; ENOYL_COA_HYDRATASE; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 36..58
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 543 AA; 59945 MW; D8D9D776AD7BB2DF CRC64;
MPLIAQWRAV LFLHFKGTER TPPTKMHTVM TRGNAILAYS LSVLSVLTFC CFASTFFYDY
RTDARINTVK VLVKNVPDFS ASREKNDLGF ITFDLATDLN PLFNWNVKQL FLYLTAEYTT
EQNALNQVVL WDKIILRGEN ANLDFKNMNT KYYFWDDGNG LKGHRNVTLT LSWNIIPNAG
LLPSVFSHGE HSFKFPEAYI ESPVYSQITA EDHPVWKSEA YVFKMLKTGT FAARFVKQSL
VGCANGLRTV TVPTHRSLSE DHTKGSVGTA GTDVAPSQEL QLTYLTEEDK QGIAVLGMNR
PKARNSFSKS LVNHLLEAIE VLAHDKNVRV VILRSLVPGI FCAGADLKER ATFTPQEVSR
FVSKLRQMMV NIEQMPTPVV AAIDGAALGG GLEMALACDM RVVATNAKLG LVETKLGIIP
GAGGTQRLPR ILNPAVAKEL IFTARQFSGE EAKALGIVNH AVQPNETGDA AYQRALQLAM
EIVPNGPVGV RMAKKAIDKG LQVDIGTGYA IEEACYAQVI PTKDRLEGLR AFAEKRKPNF
IGE
//
