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Database: UniProt
Entry: N1REQ9_FUSC4
LinkDB: N1REQ9_FUSC4
Original site: N1REQ9_FUSC4 
ID   N1REQ9_FUSC4            Unreviewed;       342 AA.
AC   N1REQ9;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=Elongation of fatty acids protein {ECO:0000256|RuleBase:RU361115};
DE            EC=2.3.1.- {ECO:0000256|RuleBase:RU361115};
GN   ORFNames=FOC4_g10011068 {ECO:0000313|EMBL:EMT65093.1};
OS   Fusarium oxysporum f. sp. cubense (strain race 4) (Panama disease fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium oxysporum species complex.
OX   NCBI_TaxID=2502994 {ECO:0000313|EMBL:EMT65093.1, ECO:0000313|Proteomes:UP000016929};
RN   [1] {ECO:0000313|Proteomes:UP000016929}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=race 4 {ECO:0000313|Proteomes:UP000016929};
RA   Fang X., Huang J.;
RT   "Genome sequencing and comparative transcriptomics of race 1 and race 4 of
RT   banana pathogen: Fusarium oxysporum f. sp. cubense.";
RL   Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000016929}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=race 4 {ECO:0000313|Proteomes:UP000016929};
RX   PubMed=24743270;
RA   Guo L., Han L., Yang L., Zeng H., Fan D., Zhu Y., Feng Y., Wang G.,
RA   Peng C., Jiang X., Zhou D., Ni P., Liang C., Liu L., Wang J., Mao C.,
RA   Fang X., Peng M., Huang J.;
RT   "Genome and Transcriptome Analysis of the Fungal Pathogen Fusarium
RT   oxysporum f. sp. cubense Causing Banana Vascular Wilt Disease.";
RL   PLoS ONE 9:E95543-E95543(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|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}.
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DR   EMBL; KB726990; EMT65093.1; -; Genomic_DNA.
DR   AlphaFoldDB; N1REQ9; -.
DR   STRING; 1229665.N1REQ9; -.
DR   HOGENOM; CLU_048483_6_1_1; -.
DR   Proteomes; UP000016929; 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: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.
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:UP000016929};
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        59..77
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361115"
FT   TRANSMEM        89..108
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361115"
FT   TRANSMEM        189..207
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361115"
FT   TRANSMEM        227..245
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361115"
FT   TRANSMEM        265..286
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361115"
FT   REGION          296..342
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        317..336
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   342 AA;  39035 MW;  053E46ABC4A43132 CRC64;
     MSASPATFYE QLPLPTIDRP FGVHLWPIFD KAFTAVVGYS ANDFKFVPFE TPMSTLKSTS
     IFIVIYYAII FGGREWMRNR EPFKLKGLFL IHNLYLTLIS GTLLALFVEQ LLPTVVRGGI
     FHAICDAEGG WTQPLVVLYY LNYLTKYLEL LDTVFLFLKK KPLTFLHCYH HGATAFLCYT
     QLIGSTSVSW VPIVLNLLVH VVMYWYYFQS ARGVRVWWKE WVTRLQIIQF VIDLGFIYFA
     SYTYFTSTYF PWMPNAGKCS GEEFAAFSGI ITISSYLVLF ISFYFATYKK QGKAPTGRQS
     LRRMSQAPLP DPHLVQTTPV KKSNGATATG SKTNGSVRSR KA
//
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