ID   FCSA_DICDI              Reviewed;         667 AA.
AC   Q55DR6; Q86PL9;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   25-MAY-2022, entry version 102.
DE   RecName: Full=Fatty acyl-CoA synthetase A;
DE            EC=6.2.1.3;
DE   AltName: Full=Long chain fatty acyl coenzyme A-synthetase 1;
DE            Short=LC-FACS 1;
DE   AltName: Full=Long-chain-fatty-acid--CoA synthetase 1;
GN   Name=fcsA; ORFNames=DDB_G0269242;
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], FUNCTION, SUBCELLULAR LOCATION, AND
RP   DEVELOPMENTAL STAGE.
RX   PubMed=14629118; DOI=10.1078/0171-9335-00342;
RA   von Loehneysen K., Pawolleck N., Ruehling H., Maniak M.;
RT   "A Dictyostelium long chain fatty acyl coenzyme A-synthetase mediates fatty
RT   acid retrieval from endosomes.";
RL   Eur. J. Cell Biol. 82:505-514(2003).
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   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=AX2;
RX   PubMed=16926386; DOI=10.1074/mcp.m600113-mcp200;
RA   Gotthardt D., Blancheteau V., Bosserhoff A., Ruppert T., Delorenzi M.,
RA   Soldati T.;
RT   "Proteomics fingerprinting of phagosome maturation and evidence for the
RT   role of a Galpha during uptake.";
RL   Mol. Cell. Proteomics 5:2228-2243(2006).
CC   -!- FUNCTION: Long chain fatty acid acyl-CoA synthetases catalyze the
CC       formation of a thiester bond between a free fatty acid and coenzyme A
CC       during fatty acid metabolic process. May mediate fatty acid retrieval
CC       from the lumen of endosomes into the cytoplasm.
CC       {ECO:0000269|PubMed:14629118}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a long-chain fatty acid + ATP + CoA = a long-chain fatty acyl-
CC         CoA + AMP + diphosphate; Xref=Rhea:RHEA:15421, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57560,
CC         ChEBI:CHEBI:83139, ChEBI:CHEBI:456215; EC=6.2.1.3;
CC   -!- SUBCELLULAR LOCATION: Endosome membrane {ECO:0000269|PubMed:14629118};
CC       Peripheral membrane protein {ECO:0000269|PubMed:14629118}; Cytoplasmic
CC       side {ECO:0000269|PubMed:14629118}. Note=Associates with endosomes a
CC       few minutes after their formation, remains bound through the acidic
CC       phase of endocytic maturation and dissociates early in the phase where
CC       the endosomal content is neutralized prior to exocytosis.
CC   -!- DEVELOPMENTAL STAGE: Expressed at all stages of development.
CC       {ECO:0000269|PubMed:14629118}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000305}.
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DR   EMBL; AY196478; AAO43007.1; -; mRNA.
DR   EMBL; AAFI02000005; EAL71971.1; -; Genomic_DNA.
DR   RefSeq; XP_646065.1; XM_640973.1.
DR   AlphaFoldDB; Q55DR6; -.
DR   SMR; Q55DR6; -.
DR   STRING; 44689.DDB0191105; -.
DR   PaxDb; Q55DR6; -.
DR   EnsemblProtists; EAL71971; EAL71971; DDB_G0269242.
DR   GeneID; 8617013; -.
DR   KEGG; ddi:DDB_G0269242; -.
DR   dictyBase; DDB_G0269242; fcsA.
DR   eggNOG; KOG1256; Eukaryota.
DR   HOGENOM; CLU_000022_45_4_1; -.
DR   InParanoid; Q55DR6; -.
DR   OMA; PRIWTKF; -.
DR   PhylomeDB; Q55DR6; -.
DR   Reactome; R-DDI-2046105; Linoleic acid (LA) metabolism.
DR   Reactome; R-DDI-2046106; alpha-linolenic acid (ALA) metabolism.
DR   Reactome; R-DDI-75876; Synthesis of very long-chain fatty acyl-CoAs.
DR   PRO; PR:Q55DR6; -.
DR   Proteomes; UP000002195; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; IDA:dictyBase.
DR   GO; GO:0010009; C:cytoplasmic side of endosome membrane; IDA:dictyBase.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0005811; C:lipid droplet; HDA:dictyBase.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0045335; C:phagocytic vesicle; HDA:dictyBase.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004467; F:long-chain fatty acid-CoA ligase activity; IBA:GO_Central.
DR   GO; GO:0006631; P:fatty acid metabolic process; IMP:dictyBase.
DR   GO; GO:0001676; P:long-chain fatty acid metabolic process; IBA:GO_Central.
DR   CDD; cd05927; LC-FACS_euk; 1.
DR   Gene3D; 3.40.50.12780; -; 1.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig.
DR   InterPro; IPR042099; ANL_N_sf.
DR   InterPro; IPR045311; LC-FACS_euk.
DR   Pfam; PF00501; AMP-binding; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Endosome; Fatty acid metabolism; Ligase; Lipid metabolism;
KW   Membrane; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..667
FT                   /note="Fatty acyl-CoA synthetase A"
FT                   /id="PRO_0000328558"
FT   CONFLICT        199
FT                   /note="K -> T (in Ref. 1; AAO43007)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   667 AA;  74609 MW;  3F7A9C4B4AFBB2B4 CRC64;
     MSSLSTKTDL LGDPDFIRLQ SVEVDGSEVI PGETRPRRNT KFPKLTNSPD GKTFTLYDVY
     RINKDSDSNF LGIRELLADG KRGDYKWISY KQACIRANNI GSALVQLGLN KGDRIGIFSI
     NRPEWVLSDM AAMNHSLVPV ALYATLGANA IEYVVNHSEI SVLLCEGKNV EKILSMPGTT
     IKTIVSYDPL PQATLDKFKD NENVKLYLLS DFEKLGEQNP AQHEVPSPED LCTLLYTSGS
     TGNPKGVMLT HTNMVSEVAG ANFSPAGVIP EDVHMSYLPL AHSFERAVVS LMCYVGGQIG
     FFSGLIPELF NDIQVLRPTF LCGAPRVWQR LHDKLWFTVN NDSWLKKFLF NWGLNSKQSA
     LRLGSTTPIW DKLVFSKTKD RLGGRVKFIL SGSAPLDPKL AEFLRACFCC PVVSGYGLSE
     NVGGASVAYP EDNNVGHVGP PLSACEMKLI DVPEMNYFST DKPCPRGEVC IRGFNVFKGY
     FKDPEKTKED LKEDGWFHTG DIGRWNENGT LSIIDRKKNI FKLSQGEYVA AEYLESVFVR
     SPFASQVFVY GDSLNSFLVG VVVPDFEVVQ KLFASKYPEL DVSNHATLAK SKELYKEILS
     SFDACAAEAK LHGFEKLKHI YVEHEPFTEE NNLLTPSFKP KRPQLKERYQ TIIDTLYAEY
     KRDHPDV