ID A0A3S1I1A9_ELYCH Unreviewed; 374 AA.
AC A0A3S1I1A9;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase {ECO:0000256|ARBA:ARBA00013122, ECO:0000256|RuleBase:RU363109};
DE EC=4.2.1.134 {ECO:0000256|ARBA:ARBA00013122, ECO:0000256|RuleBase:RU363109};
GN ORFNames=EGW08_002020 {ECO:0000313|EMBL:RUS90239.1};
OS Elysia chlorotica (Eastern emerald elysia) (Sea slug).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Heterobranchia; Euthyneura; Panpulmonata; Sacoglossa; Placobranchoidea;
OC Plakobranchidae; Elysia.
OX NCBI_TaxID=188477 {ECO:0000313|EMBL:RUS90239.1, ECO:0000313|Proteomes:UP000271974};
RN [1] {ECO:0000313|EMBL:RUS90239.1, ECO:0000313|Proteomes:UP000271974}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EC2010 {ECO:0000313|EMBL:RUS90239.1};
RC TISSUE=Whole organism of an adult {ECO:0000313|EMBL:RUS90239.1};
RA Cai H., Li Q., Fang X., Li J., Curtis N.E., Altenburger A., Shibata T.,
RA Feng M., Maeda T., Schwartz J.A., Shigenobu S., Lundholm N., Nishiyama T.,
RA Yang H., Hasebe M., Li S., Pierce S.K., Wang J.;
RT "A draft genome assembly of the solar-powered sea slug Elysia chlorotica.";
RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the third of the four reactions of the long-chain
CC fatty acids elongation cycle. This endoplasmic reticulum-bound
CC enzymatic process, allows the addition of two carbons to the chain of
CC long- and very long-chain fatty acids/VLCFAs per cycle. This enzyme
CC catalyzes the dehydration of the 3-hydroxyacyl-CoA intermediate into
CC trans-2,3-enoyl-CoA, within each cycle of fatty acid elongation.
CC Thereby, it participates to the production of VLCFAs of different chain
CC lengths that are involved in multiple biological processes as
CC precursors of membrane lipids and lipid mediators.
CC {ECO:0000256|RuleBase:RU363109}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a very-long-chain (3R)-3-hydroxyacyl-CoA = a very-long-chain
CC (2E)-enoyl-CoA + H2O; Xref=Rhea:RHEA:45812, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:83728, ChEBI:CHEBI:85440; EC=4.2.1.134;
CC Evidence={ECO:0000256|RuleBase:RU363109};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005194, ECO:0000256|RuleBase:RU363109}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|RuleBase:RU363109}; Multi-pass membrane protein
CC {ECO:0000256|RuleBase:RU363109}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the very long-chain fatty acids dehydratase HACD
CC family. {ECO:0000256|ARBA:ARBA00007811, ECO:0000256|RuleBase:RU363109}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU363109}.
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:RUS90239.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; RQTK01000037; RUS90239.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3S1I1A9; -.
DR STRING; 188477.A0A3S1I1A9; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000271974; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0102158; F:very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd06465; p23_hB-ind1_like; 1.
DR Gene3D; 2.60.40.790; -; 1.
DR InterPro; IPR007052; CS_dom.
DR InterPro; IPR008978; HSP20-like_chaperone.
DR InterPro; IPR007482; Tyr_Pase-like_PTPLA.
DR PANTHER; PTHR11035; VERY-LONG-CHAIN (3R)-3-HYDROXYACYL-COA DEHYDRATASE; 1.
DR PANTHER; PTHR11035:SF35; VERY-LONG-CHAIN (3R)-3-HYDROXYACYL-COA DEHYDRATASE; 1.
DR Pfam; PF04969; CS; 1.
DR Pfam; PF04387; PTPLA; 1.
DR SUPFAM; SSF49764; HSP20-like chaperones; 1.
DR PROSITE; PS51203; CS; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW Endoplasmic reticulum {ECO:0000256|RuleBase:RU363109};
KW Fatty acid biosynthesis {ECO:0000256|RuleBase:RU363109};
KW Fatty acid metabolism {ECO:0000256|RuleBase:RU363109};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516,
KW ECO:0000256|RuleBase:RU363109};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098,
KW ECO:0000256|RuleBase:RU363109};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU363109};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU363109};
KW Reference proteome {ECO:0000313|Proteomes:UP000271974};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU363109};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU363109}.
FT TRANSMEM 157..182
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363109"
FT TRANSMEM 221..240
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363109"
FT TRANSMEM 283..308
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363109"
FT TRANSMEM 328..350
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363109"
FT DOMAIN 4..94
FT /note="CS"
FT /evidence="ECO:0000259|PROSITE:PS51203"
SQ SEQUENCE 374 AA; 42822 MW; 7D08A82399EB7F96 CRC64;
MASSLSPFVY WGQSNDTVSL KVDLRNVEDV NVSLTEEGLD FDALGLGVKG VHQYGFHLDF
YLPVDPEKSR YRKTDIAVEF QIQKAGSETW PRLTSERLKL PWLKIDFDKF PLDESDIDED
MEFENGKSAQ KDMLDKISVE MASKPSKDGI TATQAYLFFY NLFQFVGYTF IFAKLIYIYG
VYGQAGMERA FEAVGSQMVL CQAVAVMEAL HPLFGLVKSS VIIAMAQMIG RNLILFLLVL
QEPRLQLSSV CWLLFTVWSS VEVIRYPFYL LQLMGLKVRI LTWLRYTVWI PLYPLGILVE
GAIVFKSITY FEETGFYSFS LPNSANFAFY FPYFLMVHLL LMALGGSNNL KHMYAQRKKQ
LSNSNSRTRK NKSS
//