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Database: UniProt
Entry: A0A397SD98_9GLOM
LinkDB: A0A397SD98_9GLOM
Original site: A0A397SD98_9GLOM 
ID   A0A397SD98_9GLOM        Unreviewed;       278 AA.
AC   A0A397SD98;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=Elongation of fatty acids protein {ECO:0000256|RuleBase:RU361115};
DE            EC=2.3.1.- {ECO:0000256|RuleBase:RU361115};
GN   ORFNames=C1645_784510 {ECO:0000313|EMBL:RIA84250.1};
OS   Glomus cerebriforme.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC   Glomeromycetes; Glomerales; Glomeraceae; Glomus.
OX   NCBI_TaxID=658196 {ECO:0000313|EMBL:RIA84250.1, ECO:0000313|Proteomes:UP000265703};
RN   [1] {ECO:0000313|EMBL:RIA84250.1, ECO:0000313|Proteomes:UP000265703}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DAOM 227022 {ECO:0000313|EMBL:RIA84250.1,
RC   ECO:0000313|Proteomes:UP000265703};
RA   Morin E., San Clemente H., Chen E.C.H., De La Providencia I., Hainaut M.,
RA   Kuo A., Kohler A., Murat C., Tang N., Roy S., Loubradou J., Henrissat B.,
RA   Grigoriev I.V., Corradi N., Roux C., Martin F.M.;
RT   "Comparative genomics reveals the genomic features of Rhizophagus
RT   irregularis, R. cerebriforme, R. diaphanum and Gigaspora rosea, and their
RT   symbiotic lifestyle signature.";
RL   Submitted (JUN-2018) 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}.
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:RIA84250.1}.
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DR   EMBL; QKYT01000506; RIA84250.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A397SD98; -.
DR   STRING; 658196.A0A397SD98; -.
DR   Proteomes; UP000265703; 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:UP000265703};
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        47..68
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361115"
FT   TRANSMEM        80..100
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361115"
FT   TRANSMEM        155..174
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361115"
FT   TRANSMEM        180..199
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361115"
FT   TRANSMEM        219..237
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361115"
FT   TRANSMEM        243..266
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361115"
SQ   SEQUENCE   278 AA;  32903 MW;  ECE60A2FF2F019F9 CRC64;
     MNDTKNLIFR AEEIFSIPYN TSNWDYYQFI NPNEFQWKVG ITPFSNWQFI VGAWATYFVT
     IISLKSIMSS TSPFSMRYIS AIHNLILCIL SAVMFGYATL DFIYRYQERG IGECFCTSDS
     SSAKGRLFYV TYIYYLSKFD ELLDTVILAL KKRPIIFLHW YHHAIVILMV WSWLEDSNMY
     ASIGMMANTL IHVFMYYYYF STSLGRKVWF KKYITTGQII QFAISFILAI PYLYFHFTKN
     CQLGFNAFVF SMVCNGSFLI LFIRFYRKTY SRDVGKNK
//
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