Reviewed, UniProtKB/Swiss-Prot Q54YA0 (ACLY_DICDI)

Names and origin

Protein names

Recommended name:
    Probable ATP-citrate synthase
    EC=2.3.3.8
Alternative name(s):
    ATP-citrate (pro-S-)-lyase
    Citrate cleavage enzyme

Gene names

Name:	acly
ORF Names:	DDB_G0278345

Organism

Dictyostelium discoideum (Slime mold) [Complete proteome]

Taxonomic identifier

44689 [NCBI]

Taxonomic lineage

Eukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium

Protein attributes

Sequence length	622 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	ATP-citrate synthase is the primary enzyme responsible for the synthesis of cytosolic acetyl-CoA in many tissues By similarity.
Catalytic activity	ADP + phosphate + acetyl-CoA + oxaloacetate = ATP + citrate + CoA.
Subunit structure	Homotetramer By similarity.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	In the N-terminal section; belongs to the succinate/malate CoA ligase beta subunit family. In the C-terminal section; belongs to the succinate/malate CoA ligase alpha subunit family.

Ontologies

Keywords
Biological process	Lipid synthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Transferase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	cellular carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro lipid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATP citrate synthase activity Inferred from electronic annotation. Source: EC magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW succinate-CoA ligase (ADP-forming) activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 622	622	Probable ATP-citrate synthase		PRO_0000342146
Regions
	Nucleotide binding	228 – 248	21	ATP By similarity
	Nucleotide binding	279 – 305	27	ATP By similarity
	Region	306 – 316	11	CoA-binding Potential
Sites
	Active site	287	1	Tele-phosphohistidine intermediate By similarity
	Metal binding	245	1	Magnesium By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q54YA0-1 [UniParc]. Last modified May 24, 2005. Version 1. Checksum: 05C2BDE798311D6B	FASTA	622	67,320
	10 20 30 40 50 60 MTNSNFNHGN HGSNLPARLF TKQSQALIYN YKEAAVQRML DFDNVSQRDT PSVGGLIHPG 70 80 90 100 110 120 SDGGMYKAFF GFKELVIPVY NSVSEACQQC PNADVFLNFA SHRSAYQSSL LALREPSIQT 130 140 150 160 170 180 VVIIAEGVPE NEARSLISIA KKLGKVIIGP ATVGGIQAGC FKIGNTAGTI VYIMACKLYR 190 200 210 220 230 240 SGSVGFVSKS GGLSNEMYNV LSRCTDGIYE GIAIGGDAFP GSTLTDHALR YEKLPEVQMI 250 260 270 280 290 300 VILGELGGWD EYGIVEALKK GEITKPICAW VSGTVAKIFP TEVQFGHAGA KSGGETESAD 310 320 330 340 350 360 AKNKALREAG AVVPTSFEDF SNVIAATYAK LQSKGLVKPV EEPTPPELPL DFKTAVKAGK 370 380 390 400 410 420 VRKPTSIIST ICDDRGDELS YAGVPISEVC KEQYNMGDVI GLLWFKRKLP PYASKFFEMC 430 440 450 460 470 480 LKLVADHGPC VSGAHNTIVA ARAGKDLVSS LVSGLLTIGP RFGGAIDDSA RVFQDAVDNN 490 500 510 520 530 540 LQPSQFVEGM KSKGKRIPGI GHLIKSADEI DKRVVLLKDY AFTHFSSTKY LEYALEVEKY 550 560 570 580 590 600 TLQKANNLIL NVDGCIGVLF LDLLHSSGLF TQHEIKEIID VGYLNGFFIV GRSVGLIGHA 610 620 LDQRRNKQGL YRHQADDVHY AL

References

[1]	"The genome of the social amoeba Dictyostelium discoideum." Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N. , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A. Nature 435:43-57(2005) [PubMed: 15875012] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AX4.
[2]	"Proteomics fingerprinting of phagosome maturation and evidence for the role of a Galpha during uptake." Gotthardt D., Blancheteau V., Bosserhoff A., Ruppert T., Delorenzi M., Soldati T. Mol. Cell. Proteomics 5:2228-2243(2006) [PubMed: 16926386] [Abstract] Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AAFI02000023 Genomic DNA. Translation: EAL68345.1.
RefSeq	XP_642302.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q54YA0.
Genome annotation databases
GeneID	3393363.
GenomeReviews	Gene locus acly in contig CM000152_GR.
KEGG	ddi:DDB_0235360.
Organism-specific databases
dictyBase	DDB_G0278345. acly.
Phylogenomic databases
OMA	NVDGTIG.
Family and domain databases
InterPro	IPR017440. Cit_synth/succinyl-CoA_lig_AS. IPR016142. Citrate_synth-like_lrg_a-sub. IPR005810. CoA_lig_alpha. IPR005811. CoA_ligase. IPR016040. NAD(P)-bd_dom. IPR017866. Succ-CoA_synthase_bsu_CS. IPR016102. Succinyl-CoA_synth-like. [Graphical view]
Gene3D	G3DSA:1.10.580.10. Citrate_synthase_lrg_a-sub. 1 hit. G3DSA:3.40.50.720. NAD(P)-bd. 1 hit. G3DSA:3.40.50.261. Succinyl-CoA_synth-like. 1 hit.
Pfam	PF00549. Ligase_CoA. 1 hit. [Graphical view]
PRINTS	PR01798. SCOASYNTHASE.
PROSITE	PS01216. SUCCINYL_COA_LIG_1. 1 hit. PS00399. SUCCINYL_COA_LIG_2. 1 hit. PS01217. SUCCINYL_COA_LIG_3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ACLY_DICDI

Accession

Primary (citable) accession number: Q54YA0

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 2008
Last sequence update:	May 24, 2005
Last modified:	November 3, 2009
This is version 34 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)