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P79024 (CISY_CANTR) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. 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
Gene names
Name:CIT
OrganismCandida tropicalis (Yeast)
Taxonomic identifier5482 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesmitosporic SaccharomycetalesCandida

Protein attributes

Sequence length467 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

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

Pathway

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

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

The conserved active site Asp residue in position 402 is replaced by a Gly.

Ontologies

Keywords
   Biological processTricarboxylic acid cycle
   Cellular componentMitochondrion
   DomainTransit peptide
   Molecular functionTransferase
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 – ?Mitochondrion Potential
Chain? – 467Citrate synthase, mitochondrialPRO_0000005476

Sites

Active site3011 By similarity
Active site3471 By similarity

Sequences

Sequence LengthMass (Da)Tools
P79024 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: 4B194132C4198CA2

FASTA46752,004
        10         20         30         40         50         60 
MSALRSFQRS SNVAKSTLKN SVRTYATAEP TLKQRLEEIL PAKAEEVKQL KKDYGKTVIG 

        70         80         90        100        110        120 
EVLLEQAYGG MRGIKGLVWE GSVLDPIEGI RFRGRTIPDI QKELPKAPGG EEPLPEALFW 

       130        140        150        160        170        180 
LLLTGEVPTE AQTRALSEEF AARSALPKHV EELIDRSPSH LHPMAQFSIA VTALESESQF 

       190        200        210        220        230        240 
AKAYAKGVHK SEYWKYTYED SIELLAKLPT IAAKIYRNVF HDGKLPAQID SKLDYGANLA 

       250        260        270        280        290        300 
SLLGFGENKE FLELMRLYLT IHSDHEGGNV SAHTTHLVGS ALSSPFLSLA AGLNGLAGPL 

       310        320        330        340        350        360 
HGRANQEVLE WLFKLREELN GDYSKEAIEK YLWDTLNAGR VGPGYGHAVL RKTDPRYTAQ 

       370        380        390        400        410        420 
REFALKHMPD YELFKLVSNI YEVAPGVFDQ HGMTKNPWPN VGSHSGVLLQ YYGLTEESFY 

       430        440        450        460 
TVLFGVSRAF GVLPQLILDR GLGMPIERPK SFSTEKYIEL VKSIGKN 

« Hide

References

[1]Ueda M., Sanuki S., Kawachi H., Shimizu K., Atomi H., Tanaka A.
Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 20336 / pK233 / NCYC 997.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB001565 Genomic DNA. Translation: BAA19410.1.

3D structure databases

ProteinModelPortalP79024.
SMRP79024. Positions 32-463.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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...

Entry information

Entry nameCISY_CANTR
AccessionPrimary (citable) accession number: P79024
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 1, 1997
Last modified: October 16, 2013
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways