(data stored in ACNUC10043 zone)

SWISSPROT: B3RUA6_TRIAD

ID   B3RUA6_TRIAD            Unreviewed;       278 AA.
AC   B3RUA6;
DT   02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   02-SEP-2008, sequence version 1.
DT   11-DEC-2019, entry version 47.
DE   RecName: Full=Elongation of very long chain fatty acids protein {ECO:0000256|RuleBase:RU361115};
DE            EC=2.3.1.199 {ECO:0000256|RuleBase:RU361115};
DE   AltName: Full=Very-long-chain 3-oxoacyl-CoA synthase {ECO:0000256|RuleBase:RU361115};
GN   ORFNames=TRIADDRAFT_55215 {ECO:0000313|EMBL:EDV25299.1};
OS   Trichoplax adhaerens (Trichoplax reptans).
OC   Eukaryota; Metazoa; Placozoa; Trichoplacidae; Trichoplax.
OX   NCBI_TaxID=10228 {ECO:0000313|Proteomes:UP000009022};
RN   [1] {ECO:0000313|EMBL:EDV25299.1, ECO:0000313|Proteomes:UP000009022}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Grell-BS-1999 {ECO:0000313|EMBL:EDV25299.1,
RC   ECO:0000313|Proteomes:UP000009022};
RX   PubMed=18719581; DOI=10.1038/nature07191;
RA   Srivastava M., Begovic E., Chapman J., Putnam N.H., Hellsten U.,
RA   Kawashima T., Kuo A., Mitros T., Salamov A., Carpenter M.L.,
RA   Signorovitch A.Y., Moreno M.A., Kamm K., Grimwood J., Schmutz J.,
RA   Shapiro H., Grigoriev I.V., Buss L.W., Schierwater B., Dellaporta S.L.,
RA   Rokhsar D.S.;
RT   "The Trichoplax genome and the nature of placozoans.";
RL   Nature 454:955-960(2008).
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|RuleBase:RU361115};
CC   -!- SIMILARITY: Belongs to the ELO family. {ECO:0000256|RuleBase:RU361115}.
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DR   EMBL; DS985244; EDV25299.1; -; Genomic_DNA.
DR   RefSeq; XP_002111332.1; XM_002111296.1.
DR   STRING; 10228.TriadP55215; -.
DR   EnsemblMetazoa; TriadT55215; TriadP55215; TriadG55215.
DR   GeneID; 6752545; -.
DR   KEGG; tad:TRIADDRAFT_55215; -.
DR   eggNOG; KOG3072; Eukaryota.
DR   eggNOG; ENOG410Z3FZ; LUCA.
DR   HOGENOM; HOG000038943; -.
DR   InParanoid; B3RUA6; -.
DR   KO; K10203; -.
DR   OMA; YMILIFG; -.
DR   OrthoDB; 1094172at2759; -.
DR   Proteomes; UP000009022; Unassembled WGS sequence.
DR   GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
DR   GO; GO:0102336; F:3-oxo-arachidoyl-CoA synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102337; F:3-oxo-cerotoyl-CoA synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102338; F:3-oxo-lignoceronyl-CoA synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009922; F:fatty acid elongase activity; IBA:GO_Central.
DR   GO; GO:0102756; F:very-long-chain 3-ketoacyl-CoA synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0034625; P:fatty acid elongation, monounsaturated fatty acid; IBA:GO_Central.
DR   GO; GO:0034626; P:fatty acid elongation, polyunsaturated fatty acid; IBA:GO_Central.
DR   GO; GO:0019367; P:fatty acid elongation, saturated fatty acid; IBA:GO_Central.
DR   GO; GO:0030148; P:sphingolipid biosynthetic process; IBA:GO_Central.
DR   GO; GO:0042761; P:very long-chain fatty acid biosynthetic process; IBA:GO_Central.
DR   InterPro; IPR030457; ELO_CS.
DR   InterPro; IPR002076; ELO_fam.
DR   PANTHER; PTHR11157; PTHR11157; 1.
DR   Pfam; PF01151; ELO; 1.
DR   PROSITE; PS01188; ELO; 1.
PE   3: Inferred from homology;
DR   PRODOM; B3RUA6.
DR   SWISS-2DPAGE; B3RUA6.
KW   Fatty acid biosynthesis {ECO:0000256|RuleBase:RU361115};
KW   Fatty acid metabolism {ECO:0000256|RuleBase:RU361115};
KW   Lipid biosynthesis {ECO:0000256|RuleBase:RU361115};
KW   Lipid metabolism {ECO:0000256|RuleBase:RU361115};
KW   Membrane {ECO:0000256|RuleBase:RU361115};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009022};
KW   Transferase {ECO:0000256|RuleBase:RU361115};
KW   Transmembrane {ECO:0000256|RuleBase:RU361115};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU361115}.
FT   TRANSMEM        22..40
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361115"
FT   TRANSMEM        61..83
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361115"
FT   TRANSMEM        103..124
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361115"
FT   TRANSMEM        131..148
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361115"
FT   TRANSMEM        154..175
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361115"
FT   TRANSMEM        187..210
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361115"
FT   TRANSMEM        230..250
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361115"
SQ   SEQUENCE   278 AA;  32478 MW;  908A79AC9792CE4C CRC64;
     MAILSVENYF NEKIAADWMN VLAPYSVHIS VLYLVLIYWG KQYMASRKPF NMRRLLFTWS
     LTLAGFSFIG TIALGSYVLS SWYYHGFTYS VCDRTSWKGS GGLWAFLFGL SKLPELGDTF
     FIVVRKTPLP FLHYYHHITV FIYCWYSLRD LIAPGRWFAA INFLVHTVMY TYYAIKSTGM
     YRPPKWINMA ITTLQLSQMI VGCIVNTWAY TVLKSGQRCG TTWSNLRWSL IMYSSYFLLF
     AHFFYQTYFV NANRWKIAQK QKEQKMKAAA SSQSETAK
//

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