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Q0QEL7 (CISY_MESAU) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 38. 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
Gene names
Name:CS
OrganismMesocricetus auratus (Golden hamster)
Taxonomic identifier10036 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaCricetidaeCricetinaeMesocricetus

Protein attributes

Sequence length213 AA.
Sequence statusFragment.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Acetyl-CoA + H2O + oxaloacetate = citrate + CoA. UniProtKB P00889

Pathway

Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate from oxaloacetate: step 1/2. UniProtKB P00889

Subunit structure

Homodimer By similarity. UniProtKB P00889

Subcellular location

Mitochondrion matrix By similarity UniProtKB P00889.

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
   Molecular functionTransferase
   PTMAcetylation
Methylation
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

Chain‹1 – ›213›213Citrate synthase, mitochondrial
PRO_0000394310

Sites

Active site741 By similarity UniProtKB P00889
Active site1201 By similarity UniProtKB P00889
Active site1751 By similarity UniProtKB P00889

Amino acid modifications

Modified residue941N6-acetyllysine; alternate By similarity
Modified residue941N6-succinyllysine; alternate By similarity
Modified residue1001N6-acetyllysine; alternate By similarity
Modified residue1001N6-succinyllysine; alternate By similarity
Modified residue1481N6-acetyllysine; alternate By similarity
Modified residue1481N6-succinyllysine; alternate By similarity
Modified residue1551N6-acetyllysine By similarity UniProtKB O75390
Modified residue1661N6-acetyllysine; alternate By similarity
Modified residue1661N6-succinyllysine; alternate By similarity
Modified residue1681N6,N6,N6-trimethyllysine By similarity UniProtKB P00889

Experimental info

Non-terminal residue11
Non-terminal residue2131

Sequences

Sequence LengthMass (Da)Tools
Q0QEL7 [UniParc].

Last modified September 5, 2006. Version 1.
Checksum: F423CBF73DF89D63

FASTA21323,884
        10         20         30         40         50         60 
GAIDSKLDWS HNFTNMLGYT EPQFTELMRL YLTIHSDHEG GNVSAHTSHL VGSALSDPYL 

        70         80         90        100        110        120 
SFAAAMNGLA GPLHGLANQE VLVWLTQLQK EVGKDVSDEK LRDYIWNTLN SGRVVPGYGH 

       130        140        150        160        170        180 
AVLRKTDPRY SCQREFALKH LPNDPLFKLV AQLYKIVPNI LLEQGKAKNP WPNVDAHSGV 

       190        200        210 
LLQYYGMTEM NYYTVLFGVS RALGVLAQLI WSR 

« Hide

References

[1]"Housekeeping genes for phylogenetic analysis of eutherian relationships."
Kullberg M., Nilsson M.A., Arnason U., Harley E.H., Janke A.
Mol. Biol. Evol. 23:1493-1503(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[2]"Glucose-regulated protein precursor (GRP78) and tumor rejection antigen (GP96) are unique to hamster caput epididymal spermatozoa."
Kameshwari D.B., Bhande S., Sundaram C.S., Kota V., Siva A.B., Shivaji S.
Asian J. Androl. 12:344-355(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DQ403127 mRNA. Translation: ABD77260.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ0QEL7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG005336.

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.
[Graphical view]
PANTHERPTHR11739. PTHR11739. 1 hit.
PfamPF00285. Citrate_synt. 1 hit.
[Graphical view]
PRINTSPR00143. CITRTSNTHASE.
SUPFAMSSF48256. SSF48256. 1 hit.
PROSITEPS00480. CITRATE_SYNTHASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCISY_MESAU
AccessionPrimary (citable) accession number: Q0QEL7
Secondary accession number(s): P86224
Entry history
Integrated into UniProtKB/Swiss-Prot: May 18, 2010
Last sequence update: September 5, 2006
Last modified: March 19, 2014
This is version 38 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