ID A0A1L9RCL2_ASPWE Unreviewed; 365 AA.
AC A0A1L9RCL2;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Elongation of fatty acids protein {ECO:0000256|RuleBase:RU361115};
DE EC=2.3.1.- {ECO:0000256|RuleBase:RU361115};
GN ORFNames=ASPWEDRAFT_114706 {ECO:0000313|EMBL:OJJ32652.1};
OS Aspergillus wentii DTO 134E9.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Cremei.
OX NCBI_TaxID=1073089 {ECO:0000313|EMBL:OJJ32652.1, ECO:0000313|Proteomes:UP000184383};
RN [1] {ECO:0000313|Proteomes:UP000184383}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DTO 134E9 {ECO:0000313|Proteomes:UP000184383};
RX PubMed=28196534; DOI=10.1186/s13059-017-1151-0;
RA de Vries R.P., Riley R., Wiebenga A., Aguilar-Osorio G., Amillis S.,
RA Uchima C.A., Anderluh G., Asadollahi M., Askin M., Barry K., Battaglia E.,
RA Bayram O., Benocci T., Braus-Stromeyer S.A., Caldana C., Canovas D.,
RA Cerqueira G.C., Chen F., Chen W., Choi C., Clum A., Dos Santos R.A.,
RA Damasio A.R., Diallinas G., Emri T., Fekete E., Flipphi M., Freyberg S.,
RA Gallo A., Gournas C., Habgood R., Hainaut M., Harispe M.L., Henrissat B.,
RA Hilden K.S., Hope R., Hossain A., Karabika E., Karaffa L., Karanyi Z.,
RA Krasevec N., Kuo A., Kusch H., LaButti K., Lagendijk E.L., Lapidus A.,
RA Levasseur A., Lindquist E., Lipzen A., Logrieco A.F., MacCabe A.,
RA Maekelae M.R., Malavazi I., Melin P., Meyer V., Mielnichuk N., Miskei M.,
RA Molnar A.P., Mule G., Ngan C.Y., Orejas M., Orosz E., Ouedraogo J.P.,
RA Overkamp K.M., Park H.-S., Perrone G., Piumi F., Punt P.J., Ram A.F.,
RA Ramon A., Rauscher S., Record E., Riano-Pachon D.M., Robert V., Roehrig J.,
RA Ruller R., Salamov A., Salih N.S., Samson R.A., Sandor E., Sanguinetti M.,
RA Schuetze T., Sepcic K., Shelest E., Sherlock G., Sophianopoulou V.,
RA Squina F.M., Sun H., Susca A., Todd R.B., Tsang A., Unkles S.E.,
RA van de Wiele N., van Rossen-Uffink D., Oliveira J.V., Vesth T.C.,
RA Visser J., Yu J.-H., Zhou M., Andersen M.R., Archer D.B., Baker S.E.,
RA Benoit I., Brakhage A.A., Braus G.H., Fischer R., Frisvad J.C.,
RA Goldman G.H., Houbraken J., Oakley B., Pocsi I., Scazzocchio C.,
RA Seiboth B., vanKuyk P.A., Wortman J., Dyer P.S., Grigoriev I.V.;
RT "Comparative genomics reveals high biological diversity and specific
RT adaptations in the industrially and medically important fungal genus
RT Aspergillus.";
RL Genome Biol. 18:RESEARCH28.1-RESEARCH28.45(2017).
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|ARBA:ARBA00001906};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an acyl-CoA + H(+) + malonyl-CoA = a 3-oxoacyl-CoA + CO2 +
CC CoA; Xref=Rhea:RHEA:50252, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:58342,
CC ChEBI:CHEBI:90726; Evidence={ECO:0000256|RuleBase:RU361115};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50253;
CC 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; KV878214; OJJ32652.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1L9RCL2; -.
DR STRING; 1073089.A0A1L9RCL2; -.
DR VEuPathDB; FungiDB:ASPWEDRAFT_114706; -.
DR OrthoDB; 2312411at2759; -.
DR Proteomes; UP000184383; 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; IPR002076; ELO_fam.
DR PANTHER; PTHR11157:SF126; ELONGATION OF VERY LONG CHAIN FATTY ACIDS PROTEIN 4; 1.
DR PANTHER; PTHR11157; FATTY ACID ACYL TRANSFERASE-RELATED; 1.
DR Pfam; PF01151; 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|ARBA:ARBA00022516,
KW ECO:0000256|RuleBase:RU361115};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098,
KW ECO:0000256|RuleBase:RU361115};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU361115};
KW Reference proteome {ECO:0000313|Proteomes:UP000184383};
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 58..76
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 97..115
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 331..353
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361115"
SQ SEQUENCE 365 AA; 40663 MW; CA1105B084BA7633 CRC64;
MDFITVPSIQ FGLPPRELFS FPPSQRKTPI PAYPDSSTRS LLRPFTINPH IFHASLDLKS
TLTFIAIYVT AVLSLNQLNA SRRYQPWAFS KTSTFRALVI LHNALLALFS AWTLFTTCQA
LKGCWPAGEP NYYAHVAEML CETDSSALRS ESISAKSLWE EGSGYIGWVF YISKFYEVLD
TMIILARGKK SSTLQTYHHA GVIICGWATM KYESPASLVG IVLNSAVHTL MYSYFTIHSL
GVSVPMSIKR SLTTIQIAQF LTGFVWGYSY LFVKYHVPLD ITAQPVDHSN SWESGSYSRM
EYNPPSTRGS DSVTRVVATA ATPCLSDSGE ALTVVLTTVY VLPLLLLFVR FFIESYTKGG
IKAKD
//
