ID A0A026VWZ7_OOCBI Unreviewed; 266 AA.
AC A0A026VWZ7;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 24-JAN-2024, entry version 34.
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=X777_14035 {ECO:0000313|EMBL:EZA48150.1};
OS Ooceraea biroi (Clonal raider ant) (Cerapachys biroi).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Dorylinae; Ooceraea.
OX NCBI_TaxID=2015173 {ECO:0000313|EMBL:EZA48150.1, ECO:0000313|Proteomes:UP000053097};
RN [1] {ECO:0000313|EMBL:EZA48150.1, ECO:0000313|Proteomes:UP000053097}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24508170; DOI=10.1016/j.cub.2014.01.018;
RA Oxley P.R., Ji L., Fetter-Pruneda I., McKenzie S.K., Li C., Hu H.,
RA Zhang G., Kronauer D.J.;
RT "The genome of the clonal raider ant Cerapachys biroi.";
RL Curr. Biol. 24:451-458(2014).
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}.
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DR EMBL; KK107672; EZA48150.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A026VWZ7; -.
DR STRING; 2015173.A0A026VWZ7; -.
DR OMA; MTTYMKI; -.
DR Proteomes; UP000053097; 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:UP000053097};
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 27..48
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 60..81
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 119..138
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 150..167
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 173..196
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 208..226
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 238..257
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361115"
SQ SEQUENCE 266 AA; 31095 MW; 9921FA1FE56D2E43 CRC64;
MANLIRHVVS NYNEVLQNIK DPNVDSWPLM GSPGPMLCIV GTYLIFVLKA GPKMMEKRPA
FQLNTVMILY NAFQVLFSIW LTSLALDIDI RHLIFSNGCS FQNHGSKAND LQTALSRGAW
WYFFAKIIEL LDTVFFVLRK KQNQVTFLHV YHHTVTAVFS WCYLKLLPGE QGVVVGFLNS
VVHIIMYSYY LIAALGSKYR KYLWWKKYMT WIQLLQFGIM LFYLILTLAM DCRMPKALTY
MFLTNVIIFI YLFSDFYRKA YKTKAT
//
