ID A0A2G5VKG7_9PELO Unreviewed; 759 AA.
AC A0A2G5VKG7;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Enoyl-CoA hydratase {ECO:0008006|Google:ProtNLM};
GN Name=Cnig_chr_I.g2388 {ECO:0000313|EMBL:PIC52170.1};
GN ORFNames=B9Z55_002388 {ECO:0000313|EMBL:PIC52170.1};
OS Caenorhabditis nigoni.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=1611254 {ECO:0000313|EMBL:PIC52170.1, ECO:0000313|Proteomes:UP000230233};
RN [1] {ECO:0000313|Proteomes:UP000230233}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JU1422 {ECO:0000313|Proteomes:UP000230233};
RA Yin D., Schwarz E.M., Thomas C.G., Felde R.L., Korf I.F., Cutter A.D.,
RA Schartner C.M., Ralston E.J., Meyer B.J., Haag E.S.;
RT "Rapid genome shrinkage in a self-fertile nematode reveals novel sperm
RT competition proteins.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
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: In the central section; belongs to the 3-hydroxyacyl-CoA
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00007005}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PIC52170.1}.
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DR EMBL; PDUG01000001; PIC52170.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G5VKG7; -.
DR STRING; 1611254.A0A2G5VKG7; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000230233; Chromosome i.
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:InterPro.
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; 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; 2.
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.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000230233}.
FT DOMAIN 358..537
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 539..634
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
FT DOMAIN 672..755
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
FT ACT_SITE 505
FT /note="For hydroxyacyl-coenzyme A dehydrogenase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR612803-1"
FT SITE 147
FT /note="Important for long-chain enoyl-CoA hydratase
FT activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR612803-2"
FT SITE 169
FT /note="Important for long-chain enoyl-CoA hydratase
FT activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR612803-2"
FT SITE 493
FT /note="Important for hydroxyacyl-coenzyme A dehydrogenase
FT activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR612803-2"
SQ SEQUENCE 759 AA; 81852 MW; 216A65734E0D1169 CRC64;
MIREMLSRLV HQSSSTLRTH VSFRLFSQST PAMQSTLRVE KQGEVAVVKI DLPNTKENVL
NKALSADMKA TFDKLQADES VKSIVVMSGK PNSFVAGADI QMLKAEKSAA GIEALSRDGQ
EQFFRIEKSQ KPVVAAIMGS CMGGGLELAL ACHYRIAVND KKTQLAVPEV MLGLLPGAGG
TQRLPKLTTV QNVLDLTLTG KKIKADKAKK IGIVDHVIQP LGDGLGPAAE NTHKYLEEVA
VKTAKDLAEG KLKVNRDKGF IHKATQAVMT NSLFLDNVVL KMAKDKLMKL TAGNYPAPLK
ILDVVRTAYV DPRKGYEAEA KAFGELSQTF QSKALIGLFD GSTDAKKNKY GQGLPVNEVA
VVGAGLMGAG IANVTIDKGV RTVLLDANPA GVERGQNQIA THLNGQVKRR KINKLEKERI
YNHLVPTVDY AAMKNADLVI EAVFEDLQLK HKVIKQIESV VGPNTIIASN TSALPIKDIA
AASSRPDKVI GMHYFSPVEK MQLLEIITHE GTSKETLATA AQLGLKQGKL VVVVKDCPGF
FVVRCLGPMM SEVVRLLQEG VDPAELDKLT TKFGFPVGAA TLADEVGLDV AEHVAQFLGK
ALGPRVRGGS ADLLSELVNA GHKGRKTGKG IFVYGDGKKG SKKVNEEATK LLQKYKLTPN
ATVSSPEDRQ LRLVSRFVNE ALLCLEEGVL ASPSDGDIAS VFGIGFPPFW GGPFRFVDLY
GADKLVASME KFAGAYESAQ FTPCQLLKDH AKSGKKFYN
//
