ID E0VMB9_PEDHC Unreviewed; 368 AA.
AC E0VMB9;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 24-JAN-2024, entry version 54.
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 Name=8239203 {ECO:0000313|EnsemblMetazoa:PHUM307650-PA};
GN ORFNames=Phum_PHUM307650 {ECO:0000313|EMBL:EEB14525.1};
OS Pediculus humanus subsp. corporis (Body louse).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Paraneoptera; Psocodea; Phthiraptera; Anoplura; Pediculidae;
OC Pediculus.
OX NCBI_TaxID=121224;
RN [1] {ECO:0000313|EMBL:EEB14525.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=USDA {ECO:0000313|EMBL:EEB14525.1};
RA Kirkness E., Hannick L., Hass B., Bruggner R., Lawson D., Bidwell S.,
RA Joardar V., Caler E., Walenz B., Inman J., Schobel S., Galinsky K.,
RA Amedeo P., Strausberg R.;
RT "Annotation of Pediculus humanus corporis strain USDA.";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EEB14525.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=USDA {ECO:0000313|EMBL:EEB14525.1};
RG The Human Body Louse Genome Consortium;
RA Kirkness E., Walenz B., Hass B., Bruggner R., Strausberg R.;
RT "The genome of the human body louse.";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblMetazoa:PHUM307650-PA}
RP IDENTIFICATION.
RC STRAIN=USDA {ECO:0000313|EnsemblMetazoa:PHUM307650-PA};
RG EnsemblMetazoa;
RL Submitted (FEB-2021) to UniProtKB.
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}.
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DR EMBL; AAZO01003571; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DS235306; EEB14525.1; -; Genomic_DNA.
DR RefSeq; XP_002427263.1; XM_002427218.1.
DR AlphaFoldDB; E0VMB9; -.
DR STRING; 121224.E0VMB9; -.
DR EnsemblMetazoa; PHUM307650-RA; PHUM307650-PA; PHUM307650.
DR GeneID; 8239203; -.
DR KEGG; phu:Phum_PHUM307650; -.
DR CTD; 8239203; -.
DR VEuPathDB; VectorBase:PHUM307650; -.
DR eggNOG; KOG3187; Eukaryota.
DR HOGENOM; CLU_046712_0_0_1; -.
DR InParanoid; E0VMB9; -.
DR OMA; SYLVMSH; -.
DR OrthoDB; 2881070at2759; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000009046; 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:UP000009046};
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 247..267
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363109"
FT TRANSMEM 279..301
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363109"
FT TRANSMEM 331..351
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; 43619 MW; AEA36834189F5D82 CRC64;
MAEILSPFVY WAQTEDQLSL KVDLKDASNA DITLESEKLT FSAVGKGAKG EHKYAFSLNF
FSKLNASKSH YRVLDREIEF SLKKAEFGFW PRLTRSPQKP AWLKVDFDKW KVNDPDIDDD
NNRNVLDDYP ELYDKLQKEE KGYKIEEFKK VYLVVYNLFQ LVGFLYILIV IAVKYSKNGF
NSVSETYENT GTIMKLCHLF MWLEVLHPVF GYTKSSILAP FLQVGGRCVI LFLMIEGEPR
MQTKPVVFYL FIIWSLVEVV RYIYYITHLN KFKINFLKWL RYTVWIPLYP LGICCEGVII
LRNIPYFEET FRYTVSLPNS WNFTFHFPTA MRVYLLLLFF PAMYVAMSHM YKIRVKKLKS
KNWKSKYF
//