ID K7ZQ10_9STRA Unreviewed; 276 AA. AC K7ZQ10; DT 06-FEB-2013, integrated into UniProtKB/TrEMBL. DT 06-FEB-2013, sequence version 1. DT 16-MAR-2016, entry version 11. 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. ATCC 26185. OC Eukaryota; Stramenopiles; Labyrinthulomycetes; Thraustochytriaceae; OC Thraustochytrium; unclassified 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: A very-long-chain acyl-CoA + malonyl-CoA = CoA CC + a very-long-chain 3-oxoacyl-CoA + CO(2). CC {ECO:0000256|RuleBase:RU361115}. CC -!- SIMILARITY: Belongs to the ELO family. CC {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 GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW. 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; PTHR11157; 1. DR Pfam; PF01151; ELO; 1. DR PROSITE; PS01188; ELO; 1. PE 3: Inferred from homology; 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 Transferase {ECO:0000256|RuleBase:RU361115}; KW Transmembrane {ECO:0000256|RuleBase:RU361115}; KW Transmembrane helix {ECO:0000256|RuleBase:RU361115}. FT TRANSMEM 43 61 Helical. {ECO:0000256|RuleBase:RU361115}. FT TRANSMEM 73 90 Helical. {ECO:0000256|RuleBase:RU361115}. FT TRANSMEM 123 143 Helical. {ECO:0000256|RuleBase:RU361115}. FT TRANSMEM 155 172 Helical. {ECO:0000256|RuleBase:RU361115}. FT TRANSMEM 178 196 Helical. {ECO:0000256|RuleBase:RU361115}. FT TRANSMEM 208 225 Helical. {ECO:0000256|RuleBase:RU361115}. FT TRANSMEM 245 265 Helical. {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 //