ID A0A0N0U6R7_9HYME Unreviewed; 315 AA.
AC A0A0N0U6R7;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Elongation of very long chain fatty acids protein {ECO:0000256|RuleBase:RU361115};
DE EC=2.3.1.199 {ECO:0000256|RuleBase:RU361115};
DE AltName: Full=Very-long-chain 3-oxoacyl-CoA synthase {ECO:0000256|RuleBase:RU361115};
GN ORFNames=WN51_07512 {ECO:0000313|EMBL:KOX78651.1};
OS Melipona quadrifasciata.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC Anthophila; Apidae; Melipona.
OX NCBI_TaxID=166423 {ECO:0000313|EMBL:KOX78651.1, ECO:0000313|Proteomes:UP000053105};
RN [1] {ECO:0000313|EMBL:KOX78651.1, ECO:0000313|Proteomes:UP000053105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0111107301 {ECO:0000313|EMBL:KOX78651.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KOX78651.1};
RA Pan H., Kapheim K.;
RT "The genome of Melipona quadrifasciata.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a very-long-chain acyl-CoA + H(+) + malonyl-CoA = a very-long-
CC chain 3-oxoacyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:32727,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57384, ChEBI:CHEBI:90725, ChEBI:CHEBI:90736;
CC EC=2.3.1.199; Evidence={ECO:0000256|RuleBase:RU361115};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the ELO family. {ECO:0000256|RuleBase:RU361115}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU361115}.
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DR EMBL; KQ435720; KOX78651.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N0U6R7; -.
DR STRING; 166423.A0A0N0U6R7; -.
DR OrthoDB; 168669at2759; -.
DR Proteomes; UP000053105; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009922; F:fatty acid elongase activity; IEA:UniProtKB-EC.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR InterPro; IPR030457; ELO_CS.
DR InterPro; IPR002076; ELO_fam.
DR PANTHER; PTHR11157:SF103; ELONGATION OF VERY LONG CHAIN FATTY ACIDS PROTEIN; 1.
DR PANTHER; PTHR11157; FATTY ACID ACYL TRANSFERASE-RELATED; 1.
DR Pfam; PF01151; ELO; 1.
DR PROSITE; PS01188; ELO; 1.
PE 3: Inferred from homology;
KW Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160,
KW ECO:0000256|RuleBase:RU361115};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832,
KW ECO:0000256|RuleBase:RU361115};
KW Lipid biosynthesis {ECO:0000256|RuleBase:RU361115};
KW Lipid metabolism {ECO:0000256|RuleBase:RU361115};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU361115};
KW Reference proteome {ECO:0000313|Proteomes:UP000053105};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361115};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU361115};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU361115}.
FT TRANSMEM 101..121
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 192..215
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361115"
SQ SEQUENCE 315 AA; 37121 MW; F68B7A47B9A0EFE7 CRC64;
MKKKTKKEEM KLEISLVKSS FNSKTTIFVR KKRARFGSMS NLIRLVVNNY NEILEVNKEI
MVDSWPMMSS PGPMLCIVGT YLAFVLKVGP KMMEKRPAFQ LNNLLILYNA VQVLFSIWLT
LQFFEMRVAF LIFSPKCNNE NPSPTDLQTR ATVFFVLRKK QNQVTFLHVY HHTITSIFSW
GYLKFLPGEQ GALIGFLNTF VHIVMYSYYL IAALGPEYKK YLWWKKYMTW IQLSLRDDDR
KMEFEFQFRV PNRTLKKNKE NAKGVLRQAN YFQIPPDLNM KFLNDAICVL FRYRTRSHRA
DFLIFIEICS GVVAP
//
