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Database: UniProt
Entry: A0A3F2XYM5_DEKBR
LinkDB: A0A3F2XYM5_DEKBR
Original site: A0A3F2XYM5_DEKBR 
ID   A0A3F2XYM5_DEKBR        Unreviewed;       342 AA.
AC   A0A3F2XYM5;
DT   16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT   16-JAN-2019, 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   Name=ELO2 {ECO:0000313|EMBL:VUG16995.1};
GN   ORFNames=DEBR0S1_30834G {ECO:0000313|EMBL:VUG16995.1}, HII12_000491
GN   {ECO:0000313|EMBL:KAF6015928.1};
OS   Dekkera bruxellensis (Brettanomyces custersii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Pichiaceae; Brettanomyces.
OX   NCBI_TaxID=5007 {ECO:0000313|EMBL:VUG16995.1, ECO:0000313|Proteomes:UP000478008};
RN   [1] {ECO:0000313|EMBL:VUG16995.1, ECO:0000313|Proteomes:UP000478008}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Friedrich A., Schacherer J.;
RL   Submitted (JUL-2019) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KAF6015928.1, ECO:0000313|Proteomes:UP000568158}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AWRI1613 {ECO:0000313|EMBL:KAF6015928.1,
RC   ECO:0000313|Proteomes:UP000568158};
RX   PubMed=32592028;
RA   Varela C., Bartel C., Onetto C., Borneman A.;
RT   "Targeted gene deletion in Brettanomyces bruxellensis with an expression-
RT   free CRISPR-Cas9 system.";
RL   Appl. Microbiol. Biotechnol. 104:7105-7115(2020).
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; JABCYN010000005; KAF6015928.1; -; Genomic_DNA.
DR   EMBL; CABFWN010000001; VUG16995.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3F2XYM5; -.
DR   STRING; 5007.A0A3F2XYM5; -.
DR   Proteomes; UP000478008; Unassembled WGS sequence.
DR   Proteomes; UP000568158; 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   Reference proteome {ECO:0000313|Proteomes:UP000478008};
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        52..73
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361115"
FT   TRANSMEM        93..114
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361115"
FT   TRANSMEM        227..247
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361115"
FT   TRANSMEM        259..281
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361115"
FT   REGION          320..342
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   342 AA;  39437 MW;  3FA4E048A22425A0 CRC64;
     MGNSIIPLPT IDRPFGFYLF GVFDKVVTSV TGGRFIPSQF EFVENETFLS DLPHVAIAIA
     MYYILVFGGR FLLKKVGAKP LSLRFQFQIH NMFLTTVSFL LVALMYEQLI PMIAHHGLYF
     SICDGQAWTK EMTTLYYLNY LVKFYEFLDT YYLVLKQKKL TFLHTYHHGA TALLCYTQLI
     GTTSISWVPI TLNLDVHVLM YWYYFLSARG IHVWWKEWVT RFQILQFILD LIFIYYATAI
     KVGHAIAPEY VCKRCAGSPL ATISGCAIIS SYLVLFIAFY IDIYKKSTKK SKVVRRVRGG
     VAAKVNEYVL LDKQTVQDNY DSNTGSPLPT KRRLHRGEKS EL
//
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