ELOA_DICDI
ID ELOA_DICDI Reviewed; 271 AA.
AC Q54CJ4;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 87.
DE RecName: Full=Elongation of fatty acids protein A;
DE EC=2.3.1.199;
DE AltName: Full=3-keto acyl-CoA synthase eloA;
DE AltName: Full=Fatty acid elongase A;
DE AltName: Full=Very-long-chain 3-oxoacyl-CoA synthase A;
GN Name=eloA; ORFNames=DDB_G0292896;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC STRAIN=AX3;
RX PubMed=18621026; DOI=10.1016/j.bbrc.2008.07.006;
RA Blacklock B.J., Kelley D., Patel S.;
RT "A fatty acid elongase ELO with novel activity from Dictyostelium
RT discoideum.";
RL Biochem. Biophys. Res. Commun. 374:226-230(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [3]
RP INDUCTION [LARGE SCALE ANALYSIS].
RX PubMed=18590548; DOI=10.1186/1471-2180-8-109;
RA Carilla-Latorre S., Calvo-Garrido J., Bloomfield G., Skelton J., Kay R.R.,
RA Ivens A., Martinez J.L., Escalante R.;
RT "Dictyostelium transcriptional responses to Pseudomonas aeruginosa: common
RT and specific effects from PAO1 and PA14 strains.";
RL BMC Microbiol. 8:109-109(2008).
CC -!- FUNCTION: Fatty acid elongase with strict substrate specificity for
CC monounsaturated fatty acids, in particular 16:1 (delta-9) to produce
CC the unusual 18:1 (delta-11) fatty acid. {ECO:0000269|PubMed:18621026}.
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;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- INDUCTION: Down-regulated by Pseudomonas aeruginosa, PAO1 strain and
CC PA14 strain infection. {ECO:0000269|PubMed:18590548}.
CC -!- SIMILARITY: Belongs to the ELO family. {ECO:0000305}.
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DR EMBL; EU826171; ACJ09597.1; -; mRNA.
DR EMBL; AAFI02000197; EAL60997.1; -; Genomic_DNA.
DR RefSeq; XP_629422.1; XM_629420.1.
DR AlphaFoldDB; Q54CJ4; -.
DR SMR; Q54CJ4; -.
DR STRING; 44689.DDB0252810; -.
DR PaxDb; Q54CJ4; -.
DR EnsemblProtists; EAL60997; EAL60997; DDB_G0292896.
DR GeneID; 8628941; -.
DR KEGG; ddi:DDB_G0292896; -.
DR dictyBase; DDB_G0292896; eloA.
DR eggNOG; KOG3071; Eukaryota.
DR HOGENOM; CLU_048483_6_1_1; -.
DR InParanoid; Q54CJ4; -.
DR OMA; SRFEMVV; -.
DR PhylomeDB; Q54CJ4; -.
DR BRENDA; 2.3.1.199; 1939.
DR BRENDA; 6.2.1.2; 1939.
DR PRO; PR:Q54CJ4; -.
DR Proteomes; UP000002195; Chromosome 6.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:dictyBase.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0009922; F:fatty acid elongase activity; IDA:dictyBase.
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; IDA:dictyBase.
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; IPR002076; ELO_fam.
DR PANTHER; PTHR11157; PTHR11157; 1.
DR Pfam; PF01151; ELO; 1.
PE 2: Evidence at transcript level;
KW Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis;
KW Lipid metabolism; Membrane; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..271
FT /note="Elongation of fatty acids protein A"
FT /id="PRO_0000393464"
FT TRANSMEM 35..55
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 68..88
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 102..122
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 139..159
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 165..185
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 198..220
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 237..257
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 271 AA; 32176 MW; 7FE8510BA0FF26B4 CRC64;
MEHIHDINFQ EFSKDPIGTI DRFRWKNEVT PFSNILFPIV CSFGYLALIY GLQIFMKNKK
EIKLHGFAMF HNLFLCLLSL LMFLGIVIPM AKYSFPHGLY NIICKPIDSG LVQFSYYIFY
LSKVYEFIDT IIQVLRKKSL LFLHVWHHFI TLWLVWANLK YDTGCQWVDI SANCFVHIVM
YFYYFQTERG INPWWKKHIT TCQIIQFIVD MSSHLAWHFY DTQGNHNSNY CSGTWATSAF
SDFVILSFLG LFIQFFVKAY KKKSSIKKKT N
