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Q29RK1 (CISY_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 68. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Citrate synthase, mitochondrial

EC=2.3.3.1
Alternative name(s):
Citrate (Si)-synthase
Gene names
Name:CS
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length466 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Acetyl-CoA + H2O + oxaloacetate = citrate + CoA.

Pathway

Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate from oxaloacetate: step 1/2.

Subunit structure

Homodimer By similarity.

Subcellular location

Mitochondrion matrix By similarity.

Miscellaneous

Citrate synthase is found in nearly all cells capable of oxidative metabolism.

Sequence similarities

Belongs to the citrate synthase family.

Ontologies

Keywords
   Biological processTricarboxylic acid cycle
   Cellular componentMitochondrion
   DomainTransit peptide
   Molecular functionTransferase
   PTMAcetylation
Methylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular carbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

tricarboxylic acid cycle

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentmitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncitrate (Si)-synthase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2727Mitochondrion By similarity
Chain28 – 466439Citrate synthase, mitochondrial
PRO_0000244377

Sites

Active site3011 By similarity
Active site3471 By similarity
Active site4021 By similarity

Amino acid modifications

Modified residue571N6-succinyllysine By similarity
Modified residue761N6-acetyllysine; alternate Ref.2
Modified residue761N6-succinyllysine; alternate Ref.2
Modified residue1031N6-succinyllysine By similarity
Modified residue1931N6-succinyllysine By similarity
Modified residue3211N6-acetyllysine; alternate By similarity
Modified residue3211N6-succinyllysine; alternate By similarity
Modified residue3271N6-acetyllysine; alternate By similarity
Modified residue3271N6-succinyllysine; alternate By similarity
Modified residue3751N6-acetyllysine; alternate By similarity
Modified residue3751N6-succinyllysine; alternate By similarity
Modified residue3821N6-acetyllysine By similarity
Modified residue3931N6-acetyllysine; alternate By similarity
Modified residue3931N6-succinyllysine; alternate By similarity
Modified residue3951N6,N6,N6-trimethyllysine By similarity
Modified residue4501N6-succinyllysine By similarity
Modified residue4591N6-acetyllysine; alternate By similarity
Modified residue4591N6-succinyllysine; alternate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q29RK1 [UniParc].

Last modified April 4, 2006. Version 1.
Checksum: 73C2CB93589084B3

FASTA46651,773
        10         20         30         40         50         60 
MALLTAAARL FGAKNASCLV LAARHASASS TNLKDILADL IPKEQTRVKA FRQQHGKTVV 

        70         80         90        100        110        120 
GQITVDMMYG GMRGMKGLVY ETSVLDPDEG IRFRGYSIPE CQKLLPKAKG GEEPLPEGLF 

       130        140        150        160        170        180 
WLLVTGQIPT EEQVSWLSQE WAKRAALPSH VVTMLDNFPT NLHPMSQLSA AVTALNSEST 

       190        200        210        220        230        240 
FARAYSEGIN RTKYWELIYE DSMDLIAKLP CVAAKIYRNL YREGSSIGAI DPKLDWSHNF 

       250        260        270        280        290        300 
TNMLGYTDAQ FTELMRLYLT IHSDHEGGNV SAHTSHLVGS ALSDPYLSFA AAMNGLAGPL 

       310        320        330        340        350        360 
HGLANQEVLV WLTQLQKEVG KDVSDEKLRD YIWNTLNSGR VVPGYGHAVL RKTDPRYTCQ 

       370        380        390        400        410        420 
REFALKHLPQ DPMFKLVAQL YKIVPNILLE QGKAKNPWPN VDAHSGVLLQ YYGMTEMNYY 

       430        440        450        460 
TVLFGVSRAL GVLAQLIWSR ALGFPLERPK SMSTDGLMKF VDSKSG 

« Hide

References

« Hide 'large scale' references
[1]NIH - Mammalian Gene Collection (MGC) project
Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Hereford.
Tissue: Heart ventricle.
[2]"Sirt5 is a NAD-dependent protein lysine demalonylase and desuccinylase."
Du J., Zhou Y., Su X., Yu J.J., Khan S., Jiang H., Kim J., Woo J., Kim J.H., Choi B.H., He B., Chen W., Zhang S., Cerione R.A., Auwerx J., Hao Q., Lin H.
Science 334:806-809(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION AT LYS-76, SUCCINYLATION AT LYS-76.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC114138 mRNA. Translation: AAI14139.1.
RefSeqNP_001038186.1. NM_001044721.1.
UniGeneBt.106917.

3D structure databases

ProteinModelPortalQ29RK1.
SMRQ29RK1. Positions 28-464.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ29RK1. 1 interaction.
STRING9913.ENSBTAP00000005730.

Chemistry

ChEMBLCHEMBL2406901.

Proteomic databases

PaxDbQ29RK1.
PRIDEQ29RK1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000005730; ENSBTAP00000005730; ENSBTAG00000004371.
GeneID280682.
KEGGbta:280682.

Organism-specific databases

CTD1431.

Phylogenomic databases

eggNOGCOG0372.
GeneTreeENSGT00390000006813.
HOGENOMHOG000130831.
HOVERGENHBG005336.
InParanoidQ29RK1.
KOK01647.
OMAELIYEDC.
OrthoDBEOG73BVCB.
TreeFamTF300398.

Enzyme and pathway databases

UniPathwayUPA00223; UER00717.

Family and domain databases

Gene3D1.10.580.10. 1 hit.
InterProIPR016142. Citrate_synth-like_lrg_a-sub.
IPR002020. Citrate_synthase-like.
IPR016141. Citrate_synthase-like_core.
IPR019810. Citrate_synthase_AS.
IPR010109. Citrate_synthase_euk.
[Graphical view]
PANTHERPTHR11739. PTHR11739. 1 hit.
PfamPF00285. Citrate_synt. 1 hit.
[Graphical view]
PRINTSPR00143. CITRTSNTHASE.
SUPFAMSSF48256. SSF48256. 1 hit.
TIGRFAMsTIGR01793. cit_synth_euk. 1 hit.
PROSITEPS00480. CITRATE_SYNTHASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20804872.

Entry information

Entry nameCISY_BOVIN
AccessionPrimary (citable) accession number: Q29RK1
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: April 4, 2006
Last modified: June 11, 2014
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways