Reviewed, UniProtKB/Swiss-Prot Q32PF2 (ACLY_BOVIN)

Names and origin

Protein names

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

Gene names

Name:

ACLY

Organism

Bos taurus (Bovine)

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	1091 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	ATP citrate-lyase is the primary enzyme responsible for the synthesis of cytosolic acetyl-CoA in many tissues. Has a central role in de novo lipid synthesis. In nervous tissue it may be involved in the biosynthesis of acetylcholine 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	Acetylation Phosphoprotein
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 – 1091	1091	ATP-citrate synthase		PRO_0000270815
Regions
	Nucleotide binding	691 – 711	21	ATP By similarity
	Nucleotide binding	742 – 768	27	ATP By similarity
	Region	769 – 779	11	CoA-binding Potential
Sites
	Active site	750	1	Tele-phosphohistidine intermediate By similarity
	Metal binding	708	1	Magnesium By similarity
Amino acid modifications
	Modified residue	86	1	N6-acetyllysine By similarity
	Modified residue	131	1	Phosphotyrosine By similarity
	Modified residue	260	1	Phosphoserine By similarity
	Modified residue	442	1	Phosphoserine By similarity
	Modified residue	445	1	Phosphothreonine By similarity
	Modified residue	447	1	Phosphothreonine By similarity
	Modified residue	451	1	Phosphoserine By similarity
	Modified residue	453	1	Phosphothreonine By similarity
	Modified residue	455	1	Phosphoserine; by PKA By similarity
	Modified residue	536	1	N6-acetyllysine By similarity
	Modified residue	544	1	N6-acetyllysine By similarity
	Modified residue	629	1	Phosphothreonine By similarity
	Modified residue	653	1	Phosphoserine By similarity
	Modified residue	672	1	Phosphotyrosine By similarity
	Modified residue	829	1	Phosphoserine By similarity
	Modified residue	912	1	Phosphoserine By similarity
	Modified residue	938	1	N6-acetyllysine By similarity
	Modified residue	952	1	N6-acetyllysine By similarity
	Modified residue	958	1	N6-acetyllysine By similarity
	Modified residue	968	1	N6-acetyllysine By similarity
	Modified residue	969	1	Phosphoserine By similarity
	Modified residue	1067	1	N6-acetyllysine By similarity
	Modified residue	1090	1	Phosphoserine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q32PF2-1 [UniParc]. Last modified December 6, 2005. Version 1. Checksum: CC88C4054C6568D3	FASTA	1,091	119,789
	10 20 30 40 50 60 MSAKAISEQT GKELLYKYIC TTSAIQNRFK YARVTPDTDW ARLLQDHPWL LSQSLVVKPD 70 80 90 100 110 120 QLIKRRGKLG LIGVNLTLDG VKSWLKPRLG QEATVGKATG FLKNFLIEPF VPHTQEEEFY 130 140 150 160 170 180 VCIYATREGD YVLFHHEGGV DVGDVDAKAQ KLLVGVDEKL NPEDIKKHLL VHAPEDKKEI 190 200 210 220 230 240 LASFISGLFN FYEDLYFTYL EINPLVVTKD GVYVLDLAAK VDATADYICK VKWGDIEFPP 250 260 270 280 290 300 PFGREAYPEE AYIADLDAKS GASLKLTLLN PKGRIWTMVA GGGASVVYSD TICDLGGVNE 310 320 330 340 350 360 LANYGEYSGA PSEQQTYDYA KTILSLMTRE KHPDGKILII GGSIANFTNV AATFKGIVRA 370 380 390 400 410 420 IRDYQGPLKE HEVTIFVRRG GPNYQEGLRV MGEVGKTTGI PIHVFGTETH MTAIVGMALG 430 440 450 460 470 480 HRPIPNQPPT AAHTANFLLN ASGSTSTPAP SRTASFSESR TDEVAPAKKA KPAMLQGKSA 490 500 510 520 530 540 TLFSRHTKAI VWGMQTRAVQ GMLDFDYVCS RDEPSVAAMV YPFTGDHKQK FYWGHKEILI 550 560 570 580 590 600 PVFKNMADAM KKHPEVDVLI NFASLRSAYD STMETMNYAQ IRTIAIIAEG IPEALTRKLI 610 620 630 640 650 660 KKADQKGVTI IGPATVGGIK PGCFKIGNTG GMLDNILASK LYRPGSVAYV SRSGGMSNEL 670 680 690 700 710 720 NNIISRTTDG VYEGVAIGGD RYPGSTFMDH VLRYQDTAGV KMIVVLGEIG GTEEYKICRG 730 740 750 760 770 780 VTEGRITKPV VCWCIGTCAA MFSSEVQFGH AGACANQASE TAVAKNQALK EAGVFVPRSF 790 800 810 820 830 840 DELGEIIQSV YEDLVARGVI VPAQEVPPPT VPMDYSWARE LGLIRKPASF MTSICDERGQ 850 860 870 880 890 900 ELIYAGMPIT EVFKEEMGIG GVLGLLWFQK RLPKYSCQFI EMCLMVTADH GPAVSGAHNT 910 920 930 940 950 960 IICARAGKDL VSSLTSGLLT IGDRFGGALD AAAKMFSKAF DSGIIPMEFV NKMKKEGKLI 970 980 990 1000 1010 1020 MGIGHRVKSI NNPDMRVQIL KDYVRQHFPA TPLLDYALEV EKITTSKKPN LILNVDGLIG 1030 1040 1050 1060 1070 1080 VAFVDMLRHC GSFTREEADE YIDIGALNGI FVLGRSMGFI GHYLDQKRLK QGLYRHPWDD 1090 ISYVLPEHMS M

References

[1]	NIH - Mammalian Gene Collection (MGC) project Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Hereford. Tissue: Ascending colon.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BC108138 mRNA. Translation: AAI08139.1.
IPI	IPI00710354.
RefSeq	NP_001032534.1.
UniGene	Bt.41387
3D structure databases
SMR	Q32PF2. Positions 481-790, 820-1075, 866-1076.
ModBase	Search...
Protein-protein interaction databases
STRING	Q32PF2.
Proteomic databases
PRIDE	Q32PF2.
Genome annotation databases
Ensembl	ENSBTAT00000022258; ENSBTAP00000022258; ENSBTAG00000016740; Bos taurus. [Genome view]
GeneID	511135.
KEGG	bta:511135.
Organism-specific databases
CTD	511135.
Phylogenomic databases
eggNOG	maNOG07006.
HOVERGEN	Q32PF2.
Enzyme and pathway databases
BRENDA	2.3.3.8. 251.
Family and domain databases
InterPro	IPR014608. ATP-citrate_synthase. IPR013650. ATP-grasp_succ-CoA_synth-type. IPR013816. ATP_grasp_subdomain_2. IPR017440. Cit_synth/succinyl-CoA_lig_AS. IPR016143. Citrate_synth-like_sm_a-sub. IPR002020. Citrate_synthase-like. IPR016141. Citrate_synthase-like_core. IPR003781. CoA_bd. 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:3.30.470.20. ATP_grasp_subdomain_2. 1 hit. G3DSA:1.10.230.10. Citrate_synthase_sm_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	PF08442. ATP-grasp_2. 1 hit. PF00285. Citrate_synt. 1 hit. PF02629. CoA_binding. 1 hit. PF00549. Ligase_CoA. 1 hit. [Graphical view]
PIRSF	PIRSF036511. ATP_citrt_syn. 1 hit.
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_BOVIN

Accession

Primary (citable) accession number: Q32PF2

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 9, 2007
Last sequence update:	December 6, 2005
Last modified:	February 9, 2010
This is version 38 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)