ACLY_DICDI
ID ACLY_DICDI Reviewed; 622 AA.
AC Q54YA0;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Probable ATP-citrate synthase;
DE EC=2.3.3.8;
DE AltName: Full=ATP-citrate (pro-S-)-lyase;
DE AltName: Full=Citrate cleavage enzyme;
GN Name=acly; ORFNames=DDB_G0278345;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
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 [2]
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: ATP-citrate synthase is the primary enzyme responsible for
CC the synthesis of cytosolic acetyl-CoA in many tissues. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + ADP + oxaloacetate + phosphate = ATP + citrate +
CC CoA; Xref=Rhea:RHEA:21160, ChEBI:CHEBI:16452, ChEBI:CHEBI:16947,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57288, ChEBI:CHEBI:456216; EC=2.3.3.8;
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the succinate/malate
CC CoA ligase beta subunit family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the succinate/malate
CC CoA ligase alpha subunit family. {ECO:0000305}.
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DR EMBL; AAFI02000023; EAL68345.1; -; Genomic_DNA.
DR RefSeq; XP_642302.1; XM_637210.1.
DR AlphaFoldDB; Q54YA0; -.
DR SMR; Q54YA0; -.
DR STRING; 44689.DDB0235360; -.
DR PaxDb; Q54YA0; -.
DR PRIDE; Q54YA0; -.
DR EnsemblProtists; EAL68345; EAL68345; DDB_G0278345.
DR GeneID; 8621508; -.
DR KEGG; ddi:DDB_G0278345; -.
DR dictyBase; DDB_G0278345; acly.
DR eggNOG; KOG1254; Eukaryota.
DR HOGENOM; CLU_006587_4_2_1; -.
DR InParanoid; Q54YA0; -.
DR OMA; IHVPDTF; -.
DR PhylomeDB; Q54YA0; -.
DR Reactome; R-DDI-6798695; Neutrophil degranulation.
DR Reactome; R-DDI-75105; Fatty acyl-CoA biosynthesis.
DR PRO; PR:Q54YA0; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0045335; C:phagocytic vesicle; HDA:dictyBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003878; F:ATP citrate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 1.10.230.10; -; 1.
DR Gene3D; 1.10.580.10; -; 1.
DR Gene3D; 3.40.50.261; -; 1.
DR InterPro; IPR017440; Cit_synth/succinyl-CoA_lig_AS.
DR InterPro; IPR016142; Citrate_synth-like_lrg_a-sub.
DR InterPro; IPR016143; Citrate_synth-like_sm_a-sub.
DR InterPro; IPR002020; Citrate_synthase.
DR InterPro; IPR036969; Citrate_synthase_sf.
DR InterPro; IPR033847; Citrt_syn/SCS-alpha_CS.
DR InterPro; IPR005811; CoA_ligase.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR017866; Succ-CoA_synthase_bsu_CS.
DR InterPro; IPR016102; Succinyl-CoA_synth-like.
DR Pfam; PF00285; Citrate_synt; 1.
DR Pfam; PF00549; Ligase_CoA; 1.
DR SUPFAM; SSF48256; SSF48256; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS01216; SUCCINYL_COA_LIG_1; 1.
DR PROSITE; PS00399; SUCCINYL_COA_LIG_2; 1.
DR PROSITE; PS01217; SUCCINYL_COA_LIG_3; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Lipid biosynthesis; Lipid metabolism; Magnesium;
KW Metal-binding; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Transferase.
FT CHAIN 1..622
FT /note="Probable ATP-citrate synthase"
FT /id="PRO_0000342146"
FT ACT_SITE 287
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000250"
FT BINDING 228..248
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 245
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 279..305
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 306..316
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000255"
SQ SEQUENCE 622 AA; 67320 MW; 05C2BDE798311D6B CRC64;
MTNSNFNHGN HGSNLPARLF TKQSQALIYN YKEAAVQRML DFDNVSQRDT PSVGGLIHPG
SDGGMYKAFF GFKELVIPVY NSVSEACQQC PNADVFLNFA SHRSAYQSSL LALREPSIQT
VVIIAEGVPE NEARSLISIA KKLGKVIIGP ATVGGIQAGC FKIGNTAGTI VYIMACKLYR
SGSVGFVSKS GGLSNEMYNV LSRCTDGIYE GIAIGGDAFP GSTLTDHALR YEKLPEVQMI
VILGELGGWD EYGIVEALKK GEITKPICAW VSGTVAKIFP TEVQFGHAGA KSGGETESAD
AKNKALREAG AVVPTSFEDF SNVIAATYAK LQSKGLVKPV EEPTPPELPL DFKTAVKAGK
VRKPTSIIST ICDDRGDELS YAGVPISEVC KEQYNMGDVI GLLWFKRKLP PYASKFFEMC
LKLVADHGPC VSGAHNTIVA ARAGKDLVSS LVSGLLTIGP RFGGAIDDSA RVFQDAVDNN
LQPSQFVEGM KSKGKRIPGI GHLIKSADEI DKRVVLLKDY AFTHFSSTKY LEYALEVEKY
TLQKANNLIL NVDGCIGVLF LDLLHSSGLF TQHEIKEIID VGYLNGFFIV GRSVGLIGHA
LDQRRNKQGL YRHQADDVHY AL
