ATP-citrate synthase - Bos taurus (Bovine)

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Q32PF2 (ACLY_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 52. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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.
Post-translational modification	ISGylated 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 Ubl conjugation
Technical term	Complete proteome Reference 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
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATP citrate synthase activity Inferred from electronic annotation. Source: EC metal 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

ATP By similarity

Nucleotide binding

742 – 768

ATP By similarity

Region

769 – 779

CoA-binding Potential

Sites

Active site

750

Tele-phosphohistidine intermediate By similarity

Metal binding

708

Magnesium By similarity

Binding site

346

Citrate; via amide nitrogen By similarity

Binding site

348

Citrate By similarity

Binding site

379

Citrate By similarity

Amino acid modifications

Modified residue

N6-acetyllysine By similarity

Modified residue

131

Phosphotyrosine By similarity

Modified residue

260

Phosphoserine By similarity

Modified residue

442

Phosphoserine By similarity

Modified residue

445

Phosphothreonine By similarity

Modified residue

447

Phosphothreonine By similarity

Modified residue

451

Phosphoserine By similarity

Modified residue

453

Phosphothreonine By similarity

Modified residue

455

Phosphoserine; by PKA and PKB/AKT1 or PKB/AKT2 By similarity

Modified residue

536

N6-acetyllysine By similarity

Modified residue

544

N6-acetyllysine By similarity

Modified residue

629

Phosphothreonine By similarity

Modified residue

653

Phosphoserine By similarity

Modified residue

672

Phosphotyrosine By similarity

Modified residue

829

Phosphoserine By similarity

Modified residue

912

Phosphoserine By similarity

Modified residue

938

N6-acetyllysine By similarity

Modified residue

952

N6-acetyllysine By similarity

Modified residue

958

N6-acetyllysine By similarity

Modified residue

968

N6-acetyllysine By similarity

Modified residue

969

Phosphoserine By similarity

Modified residue

1067

N6-acetyllysine By similarity

Modified residue

1090

Phosphoserine By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q32PF2 [UniParc].

Last modified December 6, 2005. Version 1.
Checksum: CC88C4054C6568D3
Show »

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

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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	IPI00694767.
RefSeq	NP_001032534.1. NM_001037457.1.
UniGene	Bt.41387.
3D structure databases
ProteinModelPortal	Q32PF2.
ModBase	Search...
Protein-protein interaction databases
STRING	Q32PF2.
Proteomic databases
PRIDE	Q32PF2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSBTAT00000022258; ENSBTAP00000022258; ENSBTAG00000016740.
GeneID	511135.
KEGG	bta:511135.
Organism-specific databases
CTD	47.
Phylogenomic databases
eggNOG	maNOG07006.
GeneTree	ENSGT00530000063275.
HOVERGEN	HBG003318.
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. IPR016142. Citrate_synth-like_lrg_a-sub. 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:1.10.580.10. Citrate_synthase_lrg_a-sub. 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. 2 hits.
KO	K01648.
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.
SUPFAM	SSF48256. Citrate_synthase_core. 1 hit. SSF52210. CoA_ligase. 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:	November 16, 2011
This is version 52 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents