ATP-citrate synthase - Ovis aries (Sheep)

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Q2TCH3 (ACLY_SHEEP) Reviewed, UniProtKB/Swiss-Prot

Last modified September 21, 2011. Version 40. 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

Ovis aries (Sheep)

Taxonomic identifier

9940 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Caprinae › Ovis

Protein attributes

Sequence length	1101 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
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 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 – 1101

1101

ATP-citrate synthase

PRO_0000270816

Regions

Nucleotide binding

701 – 721

ATP By similarity

Nucleotide binding

752 – 778

ATP By similarity

Region

779 – 789

CoA-binding Potential

Sites

Active site

760

Tele-phosphohistidine intermediate By similarity

Metal binding

718

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 By similarity

Modified residue

478

Phosphoserine By similarity

Modified residue

481

Phosphoserine By similarity

Modified residue

546

N6-acetyllysine By similarity

Modified residue

554

N6-acetyllysine By similarity

Modified residue

639

Phosphothreonine By similarity

Modified residue

663

Phosphoserine By similarity

Modified residue

682

Phosphotyrosine By similarity

Modified residue

839

Phosphoserine By similarity

Modified residue

922

Phosphoserine By similarity

Modified residue

948

N6-acetyllysine By similarity

Modified residue

962

N6-acetyllysine By similarity

Modified residue

968

N6-acetyllysine By similarity

Modified residue

978

N6-acetyllysine By similarity

Modified residue

979

Phosphoserine By similarity

Modified residue

1077

N6-acetyllysine By similarity

Modified residue

1100

Phosphoserine By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q2TCH3 [UniParc].

Last modified January 24, 2006. Version 1.
Checksum: 92D0F0DCB0E2D445
Show »

FASTA

1,101

120,934

        10         20         30         40         50         60 
MSAKAISEQT GKELLYKYIC TTSAIQNRFK YARVTPDTDW ARLLQDHPWL LSQSLVVKPD 

        70         80         90        100        110        120 
QLIKRRGKLG LVGVNLTLDG VKSWLKPRLG QEATVGKATG FLKNFLIEPF VPHTQEEEFY 

       130        140        150        160        170        180 
VCIYATREGD YVLFHHEGGV DVGDVDAKAQ KLLVAVDEKL NPEDIKKHLL VHAPEDKKEI 

       190        200        210        220        230        240 
LASFISGLFN FYEDLYFTYL EINPLVVTKD GVYILDLAAK 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 KPAMPQDSVP 

       490        500        510        520        530        540 
SPRPLQGKSA TLFSRHTKAI VWGMQTRAVQ GMLDFDYVCS RDEPSVAAMV YPFTGDHKQK 

       550        560        570        580        590        600 
FYWGHKEILI PVFKNMADAM KKHPEVDVLI NFASLRSAYD STMETMNYTQ IRTIAIIAEG 

       610        620        630        640        650        660 
IPEALTRKLI KKAEQKGVTI IGPATVGGIK PGCFKIGNTG GMLDNILASK LYRPGSVAYV 

       670        680        690        700        710        720 
SRSGGMSNEL NNIISRTTDG VYEGVAIGGD RYPGSTFMDH VLRYQDTPGV KMIVVLGEIG 

       730        740        750        760        770        780 
GTEEYKICRG VTEGRITKPV VCWCIGTCAA MFSSEVQFGH AGACANQASE TAVAKNQALK 

       790        800        810        820        830        840 
EAGVFVPRSF DELGEIIQSV YEDLVARGVI VPAQEVPPPT VPMDYSWARE LGLIRKPASF 

       850        860        870        880        890        900 
MTSICDERGQ ELIYAGMPIT EVFKEEMGIG GVLGLLWFQK RLPKYSCQFI EMCLMVTADH 

       910        920        930        940        950        960 
GPAVSGAHNT IICARAGKDL VSSLTSGLLT IGDRFGGALD AAAKMFSKAF DSGIIPMEFV 

       970        980        990       1000       1010       1020 
NKMKKEGKLI MGIGHRVKSI NNPDMRVQIL KDYVRQHFPA TPLLDYALEV EKITTSKKPN 

      1030       1040       1050       1060       1070       1080 
LILNVDGLIG VAFVDMLRHC GSFTREEADE YIDIGALNGI FVLGRSMGFI GHYLDQKRLK 

      1090       1100 
QGLYRHPWDD ISYVLPEHMS M

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References

[1]	"Pineal ATP-citrate lyase: function and regulation." Morin F., Moller M., Mukda S., Benjamin W.B., Shi Q., Jaffe H., Malpaux B., Klein D.C. Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Pineal gland.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY971952 mRNA. Translation: AAY40742.1.
RefSeq	NP_001033711.1. NM_001038622.1.
UniGene	Oar.4803.
3D structure databases
ProteinModelPortal	Q2TCH3.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	654404.
Organism-specific databases
CTD	47.
Phylogenomic databases
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.
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_SHEEP

Accession

Primary (citable) accession number: Q2TCH3

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 9, 2007
Last sequence update:	January 24, 2006
Last modified:	September 21, 2011
This is version 40 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

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents