ID E2BIT0_HARSA Unreviewed; 368 AA.
AC E2BIT0;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 24-JAN-2024, entry version 42.
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=EAI_13542 {ECO:0000313|EMBL:EFN84362.1};
OS Harpegnathos saltator (Jerdon's jumping ant).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Ponerinae; Ponerini; Harpegnathos.
OX NCBI_TaxID=610380 {ECO:0000313|Proteomes:UP000008237};
RN [1] {ECO:0000313|EMBL:EFN84362.1, ECO:0000313|Proteomes:UP000008237}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R22 G/1 {ECO:0000313|EMBL:EFN84362.1,
RC ECO:0000313|Proteomes:UP000008237};
RX PubMed=20798317; DOI=10.1126/science.1192428;
RA Bonasio R., Zhang G., Ye C., Mutti N.S., Fang X., Qin N., Donahue G.,
RA Yang P., Li Q., Li C., Zhang P., Huang Z., Berger S.L., Reinberg D.,
RA Wang J., Liebig J.;
RT "Genomic comparison of the ants Camponotus floridanus and Harpegnathos
RT saltator.";
RL Science 329:1068-1071(2010).
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}.
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DR EMBL; GL448535; EFN84362.1; -; Genomic_DNA.
DR RefSeq; XP_011139650.1; XM_011141348.2.
DR AlphaFoldDB; E2BIT0; -.
DR STRING; 610380.E2BIT0; -.
DR EnsemblMetazoa; XM_011141348.3; XP_011139650.1; LOC105183312.
DR GeneID; 105183312; -.
DR KEGG; hst:105183312; -.
DR InParanoid; E2BIT0; -.
DR OMA; SYLVMSH; -.
DR OrthoDB; 2881070at2759; -.
DR PhylomeDB; E2BIT0; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000008237; 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:UP000008237};
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 151..173
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363109"
FT TRANSMEM 216..234
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363109"
FT TRANSMEM 246..264
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363109"
FT TRANSMEM 284..304
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363109"
FT TRANSMEM 325..347
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363109"
FT DOMAIN 4..94
FT /note="CS"
FT /evidence="ECO:0000259|PROSITE:PS51203"
SQ SEQUENCE 368 AA; 43867 MW; F20A7C1AE6C6EA45 CRC64;
MSNTLTPFVY WAQTESQVTL KVDLTDVKDL NVDIQNNLLK VTAYGQGARG WNNYSFSLNL
HSPINPNESN YKVIDRQVDF MLKKKSNGWW PRLISYPQKP SWLKIDFDKW KNEDMDDNED
EKRDICYDYP DTFEKLLTEE FGYKKEEYAK AYLVIYNIFQ FVGFFYVIAV MGIRFSRDGP
DSMTDTYMVV GNLFKSIQLL QFLEVMHPLF GYTKNSSLIS FMQIGGRIFI LFCMIDAEPR
IQNKPIIFYL FLIWSMVEIV RYPYYITQLL NIKVSFLTWL RYTLWIPLYP LGFLCEGIII
FRNIPYFEET KKFSIFLPNA YNFTFYLPSF LRIYLLLFFL PSLYTVMSHM LQMRSSKLRN
SNIKRAYT
//
