ID A0A1F7ZMH3_9EURO Unreviewed; 538 AA.
AC A0A1F7ZMH3;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Elongation of fatty acids protein {ECO:0000256|RuleBase:RU361115};
DE EC=2.3.1.- {ECO:0000256|RuleBase:RU361115};
GN ORFNames=ABOM_011720 {ECO:0000313|EMBL:OGM40318.1};
OS Aspergillus bombycis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=109264 {ECO:0000313|EMBL:OGM40318.1, ECO:0000313|Proteomes:UP000179179};
RN [1] {ECO:0000313|EMBL:OGM40318.1, ECO:0000313|Proteomes:UP000179179}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 26010 {ECO:0000313|Proteomes:UP000179179};
RX PubMed=27664179;
RA Moore G.G., Mack B.M., Beltz S.B., Gilbert M.K.;
RT "Draft genome sequence of an aflatoxigenic Aspergillus species, A.
RT bombycis.";
RL Genome Biol. Evol. 0:0-0(2016).
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: 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:OGM40318.1}.
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DR EMBL; LYCR01000149; OGM40318.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F7ZMH3; -.
DR STRING; 109264.A0A1F7ZMH3; -.
DR OrthoDB; 2312411at2759; -.
DR Proteomes; UP000179179; 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:UP000179179};
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 63..81
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 102..126
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 198..218
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 285..306
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 385..406
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361115"
FT REGION 465..538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 465..502
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..522
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 538 AA; 59085 MW; 5D2610CD6BC0A8FE CRC64;
MFDLNLETAS GPAVVRIGLP PSSLLKFPPD ELPTTLPAPQ VSEPTWNQPF NIPPQLYNQL
LDVRVPITIA SVYAVTVCLL NRVNKSRGYK PWGFSQTKLF KAFVILHNVF LAVYSAWTCA
GMFQAFRNSW PDRNDPNGLV GVVDALCKIN GPRGYGNAAT YNPLANQWSI HNPEYKLADG
GVPDPTDVGR MWNQGLAYLG WIFYLSKFYE VLDTAIILAK GKKSSTLQTY HHAGAMMCMW
AGIRYVAPPI WIFTLVNSGI HAMMYTYYTL TALRIRVPTV IKRSLTSMQI TQFLVGTTWA
ASYLFVHYTL PPQSKAAAAA SAVRSTMATA AASGVAPWLK KLGFRAAGAE GIAENVGYAP
EIAGNVSQPH VGPMVTCMDT SGQAFAIWLN VTYLLPLTYL FVRFFIRSYL SRKDPSPQQA
THMHAAEKAG LDALHRVSRE IQKSVEMSGE TSEATEDEAI NKAQALRKKS QQVAADNSPI
RTRASSKQKA RLANQESGQG FSPVKNGAKK LTREEVEAPT DVSGVKDKNP YGVLNRNA
//
