ID G8BPI2_TETPH Unreviewed; 362 AA.
AC G8BPI2;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=Elongation of fatty acids protein {ECO:0000256|RuleBase:RU361115};
DE EC=2.3.1.- {ECO:0000256|RuleBase:RU361115};
GN Name=TPHA0B02400 {ECO:0000313|EMBL:CCE61913.1};
GN OrderedLocusNames=TPHA_0B02400 {ECO:0000313|EMBL:CCE61913.1};
OS Tetrapisispora phaffii (strain ATCC 24235 / CBS 4417 / NBRC 1672 / NRRL
OS Y-8282 / UCD 70-5) (Yeast) (Fabospora phaffii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Tetrapisispora.
OX NCBI_TaxID=1071381 {ECO:0000313|EMBL:CCE61913.1, ECO:0000313|Proteomes:UP000005666};
RN [1] {ECO:0000313|EMBL:CCE61913.1, ECO:0000313|Proteomes:UP000005666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24235 / CBS 4417 / NBRC 1672 / NRRL Y-8282 / UCD 70-5
RC {ECO:0000313|Proteomes:UP000005666};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
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; HE612857; CCE61913.1; -; Genomic_DNA.
DR RefSeq; XP_003684347.1; XM_003684299.1.
DR AlphaFoldDB; G8BPI2; -.
DR STRING; 1071381.G8BPI2; -.
DR GeneID; 11535010; -.
DR KEGG; tpf:TPHA_0B02400; -.
DR eggNOG; KOG3071; Eukaryota.
DR HOGENOM; CLU_048483_6_1_1; -.
DR OMA; EWVPISL; -.
DR OrthoDB; 2312411at2759; -.
DR Proteomes; UP000005666; Chromosome 2.
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:SF157; ELONGATION OF FATTY ACIDS PROTEIN 3; 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:UP000005666};
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 93..113
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 125..146
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 199..219
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 225..244
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 264..283
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 303..323
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361115"
FT REGION 329..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 362 AA; 41534 MW; 5CC3072E0C550078 CRC64;
MDTVVEKAAE EVIKQVAGEV GELAEEAIVA QSSNAIVDFL TSCPYVILHT PSVDHPFGIE
LWPIFSKIFE MIAGYPAEEF QFIHNQTFLA NGYHAMGIIA VYYIIIFGGQ ALLRAANAGP
TKLTFLFQLH NLFLTTVSFT LLMLLVEQLL PMIYYHGIFW AICSKEAFAP KLVVLYYLNY
LTKFWELFDT VFLILRRKNL LFLHVYHHGA TALLCYTQIV GQTSVEWVVI SLNLGVHVIM
YWYYFLSSRG IRVWWKEWVT RFQIIQFLID LCFVYFATYT FYANKYFTDI LPHMGTCYGT
QDAAAYGYLI LTSYLFLFIS FYIQSYRKSG KKKQEPAPAK SISTGSKASG AKKNKTKVSR
RA
//
