ID N1JKK7_BLUG1 Unreviewed; 432 AA.
AC N1JKK7;
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=BGHDH14_bgh05957 {ECO:0000313|EMBL:CCU80438.1};
OS Blumeria graminis f. sp. hordei (strain DH14) (Barley powdery mildew)
OS (Oidium monilioides f. sp. hordei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Erysiphales; Erysiphaceae; Blumeria; Blumeria hordei.
OX NCBI_TaxID=546991 {ECO:0000313|EMBL:CCU80438.1, ECO:0000313|Proteomes:UP000015441};
RN [1] {ECO:0000313|EMBL:CCU80438.1, ECO:0000313|Proteomes:UP000015441}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DH14 {ECO:0000313|EMBL:CCU80438.1};
RX PubMed=21148392; DOI=10.1126/science.1194573;
RA Spanu P.D., Abbott J.C., Amselem J., Burgis T.A., Soanes D.M., Stueber K.,
RA Ver Loren van Themaat E., Brown J.K.M., Butcher S.A., Gurr S.J.,
RA Lebrun M.-H., Ridout C.J., Schulze-Lefert P., Talbot N.J., Ahmadinejad N.,
RA Ametz C., Barton G.R., Benjdia M., Bidzinski P., Bindschedler L.V.,
RA Both M., Brewer M.T., Cadle-Davidson L., Cadle-Davidson M.M., Collemare J.,
RA Cramer R., Frenkel O., Godfrey D., Harriman J., Hoede C., King B.C.,
RA Klages S., Kleemann J., Knoll D., Koti P.S., Kreplak J., Lopez-Ruiz F.J.,
RA Lu X., Maekawa T., Mahanil S., Micali C., Milgroom M.G., Montana G.,
RA Noir S., O'Connell R.J., Oberhaensli S., Parlange F., Pedersen C.,
RA Quesneville H., Reinhardt R., Rott M., Sacristan S., Schmidt S.M.,
RA Schoen M., Skamnioti P., Sommer H., Stephens A., Takahara H.,
RA Thordal-Christensen H., Vigouroux M., Wessling R., Wicker T., Panstruga R.;
RT "Genome expansion and gene loss in powdery mildew fungi reveal tradeoffs in
RT extreme parasitism.";
RL Science 330:1543-1546(2010).
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:CCU80438.1}.
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DR EMBL; CAUH01004686; CCU80438.1; -; Genomic_DNA.
DR AlphaFoldDB; N1JKK7; -.
DR STRING; 546991.N1JKK7; -.
DR EnsemblFungi; BLGH_01358-mRNA-1; BLGH_01358-mRNA-1; BLGH_01358.
DR eggNOG; KOG3072; Eukaryota.
DR HOGENOM; CLU_017661_2_0_1; -.
DR InParanoid; N1JKK7; -.
DR OrthoDB; 2312411at2759; -.
DR Proteomes; UP000015441; 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:UP000015441};
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 53..73
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 183..203
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 238..260
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 272..291
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 377..399
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361115"
FT REGION 409..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 409..426
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 432 AA; 48089 MW; 48DB441E3B5C7443 CRC64;
MVNTIYFSRP STDLLQFPPS DFPSTLPPPL SGSAPFTPPI DIPTDIYNAA LDIKIPITIA
IIYAFSALIL NAYNHKCGNR PWKISKTRTF SSFVFLHNIL LAVYSGWTFL GMWGTMQRSV
PIPSDQSNLV HTVDALCKIH GSRGLGESIN FNQSTSLWSP TSSHGNTPDL GAMGRIWNEG
LSFYGWIFYL SKFYEVLDTF IIIVKGKQSG TLQTYHHAGA MFSMWAGIRY MSPPIWMFVF
VNSAIHTIMY TYFTITGIGI KVPRVLKQGI TTLQITQFVV GSLYAAIHLF ISYEIPVQVS
ITESFIEDIP KVIVDQPAQA STFLMSISRG VKNMLVASLG RLSVPPQSSE VLPKITEEVK
FRTEYQNVPC LDTTGQAFAI CLNIIYLTPL TILFVQFFIH SYLRQPTNKS PAVGDLNSSS
TNKKITSGEK SD
//
