Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P23007 (CISY_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 97. 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
Gene names
Name:CS
OrganismGallus gallus (Chicken) [Reference proteome]
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus

Protein attributes

Sequence length433 AA.
Sequence statusComplete.
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.

Caution

This is an X-ray determined sequence which was established using the sequence of pig citrate synthase and modifying it based on the observed electron density.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 433433Citrate synthase, mitochondrial
PRO_0000169983

Sites

Active site2741
Active site3201
Active site3751

Secondary structure

............................................................ 433
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P23007 [UniParc].

Last modified August 1, 1991. Version 1.
Checksum: 6942294BA95A9E06

FASTA43347,378
        10         20         30         40         50         60 
ASSTNLKDVL AALIPKEQAR IKTFRQQHGG TALGQITVDM SYGGMRGMKG LVYETSVLDP 

        70         80         90        100        110        120 
DEGIRFRGFS IPECQKLLPK GGXGGEPLPE GLFWLLVTGQ IPTGAQVSWL SKEWAKRAAL 

       130        140        150        160        170        180 
PSHVVTMLDN FPTNLHPMSQ LSAAITALNS ESNFARAYAE GILRTKYWEM VYESAMDLIA 

       190        200        210        220        230        240 
KLPCVAAKIY RNLYRAGSSI GAIDSKLDWS HNFTNMLGYT DAQFTELMRL YLTIHSDHEG 

       250        260        270        280        290        300 
GNVSAHTSHL VGSALSDPYL SFAAAMNGLA GPLHGLANQE VLGWLAQLQK AXXXAGADAS 

       310        320        330        340        350        360 
LRDYIWNTLN SGRVVPGYGH AVLRKTDPRY TCQREFALKH LPGDPMFKLV AQLYKIVPNV 

       370        380        390        400        410        420 
LLEQGAAANP WPNVDAHSGV LLQYYGMTEM NYYTVLFGVS RALGVLAQLI WSRALGFPLE 

       430 
RPKSMSTDGL IAL 

« Hide

References

[1]"Proposed mechanism for the condensation reaction of citrate synthase: 1.9-A structure of the ternary complex with oxaloacetate and carboxymethyl coenzyme A."
Karpusas M., Branchaud B., Remington S.J.
Biochemistry 29:2213-2219(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
Tissue: Heart muscle.
[2]"Crystal structure of an open conformation of citrate synthase from chicken heart at 2.8-A resolution."
Liao D.-I., Karpusas M., Remington S.J.
Biochemistry 30:6031-6036(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF OPEN CONFORMATION.
+Additional computationally mapped references.

Cross-references

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AL6X-ray1.85A1-427[»]
1AMZX-ray1.80A3-427[»]
1CSCX-ray1.70A1-433[»]
1CSHX-ray1.65A3-430[»]
1CSIX-ray1.70A3-430[»]
1CSRX-ray1.70A3-430[»]
1CSSX-ray1.70A3-430[»]
2CSCX-ray1.70A1-433[»]
3CSCX-ray1.90A1-433[»]
4CSCX-ray1.90A1-433[»]
5CSCX-ray2.80A/B1-433[»]
5CTSX-ray1.90A1-433[»]
6CSCX-ray2.25A/B1-427[»]
6CTSX-ray2.50A1-433[»]
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEP23007.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG005336.
PhylomeDBP23007.

Enzyme and pathway databases

ReactomeREACT_115655. Metabolism.
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

EvolutionaryTraceP23007.

Entry information

Entry nameCISY_CHICK
AccessionPrimary (citable) accession number: P23007
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: August 1, 1991
Last modified: April 16, 2014
This is version 97 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways