ID A0A1D2NGU6_ORCCI Unreviewed; 374 AA.
AC A0A1D2NGU6;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
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=Ocin01_02224 {ECO:0000313|EMBL:ODN04442.1};
OS Orchesella cincta (Springtail) (Podura cincta).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Collembola;
OC Entomobryomorpha; Entomobryoidea; Orchesellidae; Orchesellinae; Orchesella.
OX NCBI_TaxID=48709 {ECO:0000313|EMBL:ODN04442.1, ECO:0000313|Proteomes:UP000094527};
RN [1] {ECO:0000313|EMBL:ODN04442.1, ECO:0000313|Proteomes:UP000094527}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Mixed pool {ECO:0000313|EMBL:ODN04442.1};
RX PubMed=27289101; DOI=10.1093/gbe/evw134;
RA Faddeeva-Vakhrusheva A., Derks M.F., Anvar S.Y., Agamennone V., Suring W.,
RA Smit S., van Straalen N.M., Roelofs D.;
RT "Gene Family Evolution Reflects Adaptation to Soil Environmental Stressors
RT in the Genome of the Collembolan Orchesella cincta.";
RL Genome Biol. Evol. 8:2106-2117(2016).
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:ODN04442.1}.
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DR EMBL; LJIJ01000043; ODN04442.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1D2NGU6; -.
DR STRING; 48709.A0A1D2NGU6; -.
DR OMA; SYLVMSH; -.
DR OrthoDB; 2881070at2759; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000094527; 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:UP000094527};
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 158..181
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363109"
FT TRANSMEM 252..269
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363109"
FT TRANSMEM 290..312
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363109"
FT TRANSMEM 332..352
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363109"
FT DOMAIN 11..101
FT /note="CS"
FT /evidence="ECO:0000259|PROSITE:PS51203"
SQ SEQUENCE 374 AA; 44121 MW; F8F1367EB2B1BCB3 CRC64;
MSLNSADWVH IRSPFVYWAQ TEKTVSLRVD IRDAQNPRIL IEDSKVVFDS TGYGAQGENE
YHFELALPHN VDSDKSTYRV SDRDVDILLI KKEHGWWSKV TTSVRKPAWL KVDFDRWKSP
DDEEEIPADV MKDFPDIMDR VQREEYGYKV ENLRKVYLFL YNLFQFVGYL FIVGVLSVRY
LRDGQEATHR AFEFVGFAMR YCQIMQALEI IHPLMGFTKT SVPVAFLQIG GRALILFGIV
QAEERLHDES AVFWLFYFWS LAEVFRYPFY MLQIYERKVY FVTWLRYSAW IFLYPLGIAS
ECVVIFSGIT YFVETGRYSV SLPNSWNFSF SFPTIMRLYL LFGVFPVSYA LICNMWRSRT
KALGRSRVMI TKQK
//
