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P00889 (CISY_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
OrganismSus scrofa (Pig) [Reference proteome]
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus

Protein attributes

Sequence length464 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.

Subcellular location

Mitochondrion matrix.

Miscellaneous

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

Sequence similarities

Belongs to the citrate synthase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2727Mitochondrion Ref.2
Chain28 – 464437Citrate synthase, mitochondrial PubMed 6795632
PRO_0000005473

Sites

Active site3011
Active site3471
Active site4021

Amino acid modifications

Modified residue761N6-acetyllysine; alternate By similarity
Modified residue761N6-succinyllysine; alternate By similarity
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 Ref.2
Modified residue4501N6-succinyllysine By similarity
Modified residue4591N6-acetyllysine; alternate By similarity
Modified residue4591N6-succinyllysine; alternate By similarity

Secondary structure

...................................................................... 464
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00889 [UniParc].

Last modified October 1, 1989. Version 2.
Checksum: 66719A7504DF322A

FASTA46451,629
        10         20         30         40         50         60 
MALLTAAARL FGAKNASCLV LAARHASASS TNLKDILADL IPKEQARIKT FRQQHGNTVV 

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

       130        140        150        160        170        180 
WLLVTGQIPT EEQVSWLSKE WAKRAALPSH VVTMLDNFPT NLHPMSQLSA AITALNSESN 

       190        200        210        220        230        240 
FARAYAEGIH RTKYWELIYE DCMDLIAKLP CVAAKIYRNL YREGSSIGAI DSKLDWSHNF 

       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 
REFALKHLPH DPMFKLVAQL YKIVPNVLLE QGKAKNPWPN VDAHSGVLLQ YYGMTEMNYY 

       430        440        450        460 
TVLFGVSRAL GVLAQLIWSR ALGFPLERPK SMSTDGLIKL VDSK 

« Hide

References

[1]"Isolation, nucleotide sequence, and expression of a cDNA encoding pig citrate synthase."
Evans C.T., Owens D.D., Sumegi B., Kispal G., Srere P.A.
Biochemistry 27:4680-4686(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Complete amino acid sequence of porcine heart citrate synthase."
Bloxham D.P., Parmelee D.C., Kumar S., Walsh K.A., Titani K.
Biochemistry 21:2028-2036(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 28-464.
[3]"Crystallographic refinement and atomic models of two different forms of citrate synthase at 2.7- and 1.7-A resolution."
Remington S., Wiegand G., Huber R.
J. Mol. Biol. 158:111-152(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
[4]"Mutation of essential catalytic residues in pig citrate synthase."
Alter G.M., Casazza J.P., Zhi W., Nemeth P., Srere P.A., Evans C.T.
Biochemistry 29:7557-7563(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M21197 mRNA. Translation: AAA31017.1.
PIRYKPG. A29966.
RefSeqNP_999441.1. NM_214276.1.
UniGeneSsc.16315.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1CTSX-ray2.70A28-464[»]
2CTSX-ray2.00A28-464[»]
3ENJX-ray1.78A28-464[»]
4CTSX-ray2.90A/B28-464[»]
ProteinModelPortalP00889.
SMRP00889. Positions 28-464.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid1149646. 2 interactions.
STRING9823.ENSSSCP00000000410.

Proteomic databases

PaxDbP00889.
PRIDEP00889.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID397519.
KEGGssc:397519.

Organism-specific databases

CTD1431.

Phylogenomic databases

eggNOGCOG0372.
HOGENOMHOG000130831.
HOVERGENHBG005336.
KOK01647.

Enzyme and pathway databases

SABIO-RKP00889.
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

EvolutionaryTraceP00889.

Entry information

Entry nameCISY_PIG
AccessionPrimary (citable) accession number: P00889
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: October 1, 1989
Last modified: May 14, 2014
This is version 110 of the entry and version 2 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways