ID K7ZQ10_THRS2 Unreviewed; 276 AA. AC K7ZQ10; DT 06-FEB-2013, integrated into UniProtKB/TrEMBL. DT 06-FEB-2013, sequence version 1. DT 24-JAN-2024, entry version 26. DE RecName: Full=Elongation of 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}; OS Thraustochytrium sp. (strain ATCC 26185 / S-3). OC Eukaryota; Sar; Stramenopiles; Bigyra; Labyrinthulomycetes; OC Thraustochytrida; Thraustochytriaceae; Thraustochytrium. OX NCBI_TaxID=672127 {ECO:0000313|EMBL:BAM66614.1}; RN [1] {ECO:0000313|EMBL:BAM66614.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 26185 {ECO:0000313|EMBL:BAM66614.1}; RA Ohara J., Sakaguchi K., Okita Y., Okino N., Ito M.; RT "Two fatty acid elongases in thraustochytrid."; RL Submitted (NOV-2012) 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|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 --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB762292; BAM66614.1; -; Genomic_DNA. DR AlphaFoldDB; K7ZQ10; -. 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:SF126; ELONGATION OF VERY LONG CHAIN FATTY ACIDS PROTEIN; 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 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 43..61 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361115" FT TRANSMEM 73..90 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361115" FT TRANSMEM 123..143 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361115" FT TRANSMEM 155..172 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361115" FT TRANSMEM 178..196 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361115" FT TRANSMEM 208..225 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361115" FT TRANSMEM 245..265 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361115" SQ SEQUENCE 276 AA; 31919 MW; 3EEEA8BCBFD3FEA9 CRC64; MDVVEQQWRR FVDAVDNGIV EFMEHEKPNK LNEGKLFTST EEMMALIVGY LAFVVLGSAF MKAFVDKPFE LKFLKLVHNI FLTGLSMYMA TECARQAYLG GYKLFGNPME KGTESHAPGM ANIIYIFYVS KFLEFLDTVF MILGKKWKQL SFLHVYHHAS ISFIWGIIAR FAPGGDAYFS TILNSSVHVV LYGYYASTTL GYTFMRPLRP YITTIQLTQF MAMVVQSVYD YYNPCDYPQP LVKLLFWYML TMLGLFGNFF VQQYLKPKAP KKQKTI //