GenomeNet

Database: UniProt
Entry: A0A124BVR0_ASPNG
LinkDB: A0A124BVR0_ASPNG
Original site: A0A124BVR0_ASPNG 
ID   A0A124BVR0_ASPNG        Unreviewed;       342 AA.
AC   A0A124BVR0;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Elongation of fatty acids protein {ECO:0000256|RuleBase:RU361115};
DE            EC=2.3.1.- {ECO:0000256|RuleBase:RU361115};
GN   ORFNames=ABL_01885 {ECO:0000313|EMBL:GAQ36846.1};
OS   Aspergillus niger.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=5061 {ECO:0000313|EMBL:GAQ36846.1, ECO:0000313|Proteomes:UP000068243};
RN   [1] {ECO:0000313|Proteomes:UP000068243}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=An76 {ECO:0000313|Proteomes:UP000068243};
RX   PubMed=26893421; DOI=10.1128/genomeA.01700-15;
RA   Gong W., Cheng Z., Zhang H., Liu L., Gao P., Wang L.;
RT   "Draft genome sequence of Aspergillus niger strain An76.";
RL   Genome Announc. 4:E0170015-E0170015(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:GAQ36846.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BCMY01000002; GAQ36846.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A124BVR0; -.
DR   PaxDb; 5061-CADANGAP00002439; -.
DR   VEuPathDB; FungiDB:An02g09910; -.
DR   VEuPathDB; FungiDB:ASPNIDRAFT2_1022934; -.
DR   VEuPathDB; FungiDB:ATCC64974_54690; -.
DR   VEuPathDB; FungiDB:M747DRAFT_338743; -.
DR   OMA; WTYFTST; -.
DR   Proteomes; UP000068243; 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:SF134; ELONGATION OF VERY LONG CHAIN FATTY ACIDS PROTEIN 6; 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   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        54..72
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361115"
FT   TRANSMEM        84..103
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361115"
FT   TRANSMEM        182..202
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361115"
FT   TRANSMEM        222..240
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361115"
FT   TRANSMEM        260..281
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361115"
FT   REGION          313..342
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        321..335
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   342 AA;  39135 MW;  7DBE664C84F2A97B CRC64;
     MDVLQSLPLP SIDRPFGIHL WPIFDKAFEV VVGYPASEFR FEEGVTPMST FKETAVALVA
     YYVIIFGGRE FMKNRPAFKL NTLFMIHNLY LTLISGTLLA LFIEQLLPTV WRHGIFYAIC
     DHDGGWTRPL IVLYYLNYLT KYLELIDTVF LFLKKKPLTF LHTYHHGATA LLCYTQLIGL
     TAVQWVVIDI NLLVHVVMYW YYFQSARGIR IWWKEWITRL QIIQFVIDLG FIYFASYTYF
     SSTYFPWVPN MGKCAGEEFA AFSGMAVISS YLFLFISFYV ATYKKAAKAG RPRRNTGKQA
     VIDMAKFEVS APHADAKGNN KSNGAAVSTG RANGPVTRSR KA
//
DBGET integrated database retrieval system