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Database: UniProt
Entry: A0A0L0HTH2_SPIPD
LinkDB: A0A0L0HTH2_SPIPD
Original site: A0A0L0HTH2_SPIPD 
ID   A0A0L0HTH2_SPIPD        Unreviewed;       324 AA.
AC   A0A0L0HTH2;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=Elongation of fatty acids protein {ECO:0000256|RuleBase:RU361115};
DE            EC=2.3.1.- {ECO:0000256|RuleBase:RU361115};
GN   ORFNames=SPPG_01628 {ECO:0000313|EMBL:KND04195.1};
OS   Spizellomyces punctatus (strain DAOM BR117).
OC   Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC   Chytridiomycota incertae sedis; Chytridiomycetes; Spizellomycetales;
OC   Spizellomycetaceae; Spizellomyces.
OX   NCBI_TaxID=645134 {ECO:0000313|EMBL:KND04195.1, ECO:0000313|Proteomes:UP000053201};
RN   [1] {ECO:0000313|EMBL:KND04195.1, ECO:0000313|Proteomes:UP000053201}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DAOM BR117 {ECO:0000313|EMBL:KND04195.1,
RC   ECO:0000313|Proteomes:UP000053201};
RG   The Broad Institute Genome Sequencing Platform;
RA   Russ C., Cuomo C., Shea T., Young S.K., Zeng Q., Koehrsen M., Haas B.,
RA   Borodovsky M., Guigo R., Alvarado L., Berlin A., Bochicchio J.,
RA   Borenstein D., Chapman S., Chen Z., Engels R., Freedman E., Gellesch M.,
RA   Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., Howarth C.,
RA   Jen D., Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A.,
RA   Saif S., Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., Walk T.,
RA   White J., Yandava C., Burger G., Gray M.W., Holland P.W.H., King N.,
RA   Lang F.B.F., Roger A.J., Ruiz-Trillo I., Lander E., Nusbaum C.;
RT   "The Genome Sequence of Spizellomyces punctatus strain DAOM BR117.";
RL   Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
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; KQ257451; KND04195.1; -; Genomic_DNA.
DR   RefSeq; XP_016612234.1; XM_016749947.1.
DR   AlphaFoldDB; A0A0L0HTH2; -.
DR   STRING; 645134.A0A0L0HTH2; -.
DR   GeneID; 27685279; -.
DR   VEuPathDB; FungiDB:SPPG_01628; -.
DR   eggNOG; KOG3071; Eukaryota.
DR   InParanoid; A0A0L0HTH2; -.
DR   OMA; LQCQNLN; -.
DR   OrthoDB; 2312411at2759; -.
DR   Proteomes; UP000053201; 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:UP000053201};
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        42..59
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361115"
FT   TRANSMEM        79..100
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361115"
FT   TRANSMEM        120..141
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361115"
FT   TRANSMEM        171..190
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361115"
FT   TRANSMEM        211..229
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361115"
FT   TRANSMEM        249..272
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361115"
SQ   SEQUENCE   324 AA;  37154 MW;  991912FE8E512E5A CRC64;
     MKPLALSLFH PLFTNTSLDL LGLHPDEFKF ENAPLSTRSE VAKWFLVYLT VVLGGQAFMR
     RFVKEPIAVK PLFFLHNAFL SASSLALLVL FLEIIVPNIW NHGLLWAVCH EKSYSPRMEL
     LYYINYLIKY YEFIDTIFLV VKKKKLEFLH VYHHSMTMAL CFFELEGRPS VAWVPVTLNL
     FVHVIMYYYY ARTAVSSKPI WWKKYLTTLQ IVQFIIDLFA IYTATYIYLS SDPLAGVLPN
     FGLGKCSGTP VAAGVGCFIL TSYLGLFIQF FFKTYSGRKG GKGGKVGKVA DDTVERFEKE
     IGQEKVLSAV RKEGSTRRRL KRVD
//
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