ID A0A182PJP5_9DIPT Unreviewed; 771 AA.
AC A0A182PJP5;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=enoyl-CoA hydratase {ECO:0000256|ARBA:ARBA00012076};
DE EC=4.2.1.17 {ECO:0000256|ARBA:ARBA00012076};
OS Anopheles epiroticus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=199890 {ECO:0000313|EnsemblMetazoa:AEPI007159-PA, ECO:0000313|Proteomes:UP000075885};
RN [1] {ECO:0000313|Proteomes:UP000075885}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Epiroticus2 {ECO:0000313|Proteomes:UP000075885};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Howell P., 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 epiroticus epiroticus2.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:AEPI007159-PA}
RP IDENTIFICATION.
RC STRAIN=Epiroticus2 {ECO:0000313|EnsemblMetazoa:AEPI007159-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3S)-hydroxydecanoyl-CoA + NAD(+) = 3-oxodecanoyl-CoA + H(+) +
CC NADH; Xref=Rhea:RHEA:31187, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:62548, ChEBI:CHEBI:62616;
CC Evidence={ECO:0000256|ARBA:ARBA00001391};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31188;
CC Evidence={ECO:0000256|ARBA:ARBA00001391};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3S)-hydroxyhexadecanoyl-CoA + NAD(+) = 3-oxohexadecanoyl-CoA
CC + H(+) + NADH; Xref=Rhea:RHEA:31159, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57349, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:62613; Evidence={ECO:0000256|ARBA:ARBA00000193};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31160;
CC Evidence={ECO:0000256|ARBA:ARBA00000193};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3S)-hydroxyhexadecanoyl-CoA = (2E)-hexadecenoyl-CoA + H2O;
CC Xref=Rhea:RHEA:31163, ChEBI:CHEBI:15377, ChEBI:CHEBI:61526,
CC ChEBI:CHEBI:62613; Evidence={ECO:0000256|ARBA:ARBA00000469};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31165;
CC Evidence={ECO:0000256|ARBA:ARBA00000469};
CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC {ECO:0000256|ARBA:ARBA00005005}.
CC -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.
CC {ECO:0000256|RuleBase:RU003707}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the enoyl-CoA
CC hydratase/isomerase family. {ECO:0000256|ARBA:ARBA00008750}.
CC -!- SIMILARITY: In the central section; belongs to the 3-hydroxyacyl-CoA
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00007005}.
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DR AlphaFoldDB; A0A182PJP5; -.
DR STRING; 199890.A0A182PJP5; -.
DR EnsemblMetazoa; AEPI007159-RA; AEPI007159-PA; AEPI007159.
DR VEuPathDB; VectorBase:AEPI007159; -.
DR OrthoDB; 622692at2759; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000075885; Unassembled WGS sequence.
DR GO; GO:0016507; C:mitochondrial fatty acid beta-oxidation multienzyme complex; IEA:InterPro.
DR GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IEA:InterPro.
DR GO; GO:0004300; F:enoyl-CoA hydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IEA:UniProtKB-UniPathway.
DR CDD; cd06558; crotonase-like; 1.
DR Gene3D; 1.10.1040.50; -; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR006176; 3-OHacyl-CoA_DH_NAD-bd.
DR InterPro; IPR006108; 3HC_DH_C.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
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; IPR012803; Fa_ox_alpha_mit.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR NCBIfam; TIGR02441; fa_ox_alpha_mit; 1.
DR PANTHER; PTHR43612; TRIFUNCTIONAL ENZYME SUBUNIT ALPHA; 1.
DR PANTHER; PTHR43612:SF3; TRIFUNCTIONAL ENZYME SUBUNIT ALPHA, MITOCHONDRIAL; 1.
DR Pfam; PF00725; 3HCDH; 1.
DR Pfam; PF02737; 3HCDH_N; 1.
DR Pfam; PF00378; ECH_1; 1.
DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 2.
DR SUPFAM; SSF52096; ClpP/crotonase; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00166; ENOYL_COA_HYDRATASE; 1.
PE 3: Inferred from homology;
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NAD {ECO:0000256|ARBA:ARBA00023027}.
FT DOMAIN 368..546
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 549..644
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
FT ACT_SITE 515
FT /note="For hydroxyacyl-coenzyme A dehydrogenase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR612803-1"
FT SITE 155
FT /note="Important for long-chain enoyl-CoA hydratase
FT activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR612803-2"
FT SITE 177
FT /note="Important for long-chain enoyl-CoA hydratase
FT activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR612803-2"
FT SITE 503
FT /note="Important for hydroxyacyl-coenzyme A dehydrogenase
FT activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR612803-2"
SQ SEQUENCE 771 AA; 82832 MW; 672FB6E2619372E6 CRC64;
MASVRLIGAA MQRNVTFGRA LRLSELQSQM TMRCLATAAP AGKHMKTRIV DNVMVITLDS
PGAKVNSLNA EVQSEFDAVL REVETNPAVS SAVLISGKPG CFVAGADITM LEQCKTVEAA
TKISHEGQIQ FSKLEKSRKP VVAAINGVCL GGGLELALAC HYRVALKDKK TVVGLPEVML
GLLPGAGGTQ RLPKLTSIPT ALDLALTGKS VKADKAKKLG IVDLLVNPLG PGLKPADQNT
LEYLEQVAIQ VAKDLASEKL KVNRQKTGIV AKVTEFAFGI EWVKNKVFEK AREQVMKLSG
GLYPAPLKIL DVIRVGVDKG QEAGYEAERK GFGELSQTPQ SKGLIGLFRG QTECKKNRFG
KPANPPKTIG VLGAGLMGAG IVQVSIDKGY QVIMKDTTEA GLGRGVGQIQ NGLQGAIKRK
RISAIERDQI LSNLTSTLSY EPFRKTDIVI EAVFENIDIK HRVIKELEQV VPKHCIIATN
TSAIPITKIA AGSSRPENVV GMHYFSPVDK MQLLEIITHP GTSKETAAAA VEVGLRQGKV
VITVGDGPGF YTTRILSTML SEAIRLLQEG VDPKDLDKMT KTFGFPVGAA TLADEVGIDV
GAHIAVDLAK AFGDRFSGGN LGVMEDMVKA GFMGRKSGKG VFVYSGGRSK NREVNQDAMA
IMKQKYALQS RGANSVEDMQ LRMVSRFVNE AVLCLEEKIL DSPLEGDVGA VFGLGFPPFT
GGPFRWVDQY GAERLVSKMR SYADLYGAPF VPAQTLLDMA KDSSKKFYPS K
//
