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P83372 (CISY_FRAAN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 58. 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:MCSI
OrganismFragaria ananassa (Strawberry)
Taxonomic identifier3747 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsRosalesRosaceaeRosoideaePotentilleaeFragariinaeFragaria

Protein attributes

Sequence length469 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. UniProtKB P00889

Subcellular location

Mitochondrion matrix.

Miscellaneous

Citrate synthase is found in nearly all cells capable of oxidative metabolism. UniProtKB P00889

Sequence similarities

Belongs to the citrate synthase family. UniProtKB P00889

Ontologies

Keywords
   Biological processTricarboxylic acid cycle
   Cellular componentMitochondrion
   DomainTransit peptide
   Molecular functionTransferase
   Technical termDirect protein sequencing
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 – 2828Mitochondrion Ref.1
Chain29 – 469441Citrate synthase, mitochondrial Ref.1
PRO_0000005488

Sites

Active site3041 By similarity UniProtKB P00889
Active site3501 By similarity UniProtKB P00889
Active site4051 By similarity UniProtKB P00889

Sequences

Sequence LengthMass (Da)Tools
P83372 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: CD80AAED06246F65

FASTA46952,283
        10         20         30         40         50         60 
MAFFRTVTKL RSRLGQPPSL RDSVRCLQTQ ASSDLDLHSQ LKELIPEQQE RLKKLKKEHG 

        70         80         90        100        110        120 
KVQLGTITVD MVIGGMRGMT GLLWETSLLD PDEGIRFRGL SIPECQKVLP GATPGGEPLP 

       130        140        150        160        170        180 
EGLLWLLLTG KVPSRSKNMH YPVNNGVVPK FQIMCSRPLM LCLLEHIPMT QFTTGVMALQ 

       190        200        210        220        230        240 
VQSEFQKAYD KGIPKSRYWE PTYEDSLSLI AQLPVVASYV YRRIYKGGRM IPVDDSLDYG 

       250        260        270        280        290        300 
GNFSHLLGFD DHKMQELMRL YVTIHSDHEG GNVSAHTGHL VASALSDPFL SFAAALNGLA 

       310        320        330        340        350        360 
GPLHGLANQE VLLWIKSVVD ECGENITKDQ LKDYVWKTLN SGKVVPGFGH GVLRKTDPRY 

       370        380        390        400        410        420 
TCQREFALKH LPDDPLFRLV SKLYDVVPPI LTELGKVKNP WPNVDAHSGV LLNHFGLTEA 

       430        440        450        460 
RYFTVLFGVS RSIGIGSQLI WDRALGLPLE RPKSVTMESL ESFCKKAAS 

« Hide

References

[1]"Identification, cloning and expression analysis of strawberry (Fragaria x ananassa) mitochondrial citrate synthase and mitochondrial malate dehydrogenase."
Iannetta P.P.M., Escobar N.M., Ross H.A., Souleyre E.J., Hancock R.D., Witte C.P., Davies H.V.
Physiol. Plantarum 121:15-26(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE, PROTEIN SEQUENCE OF 29-46.
Strain: cv. Elsanta.
Tissue: Fruit.

Cross-references

3D structure databases

ProteinModelPortalP83372.
SMRP83372. Positions 35-465.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEP83372.

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_FRAAN
AccessionPrimary (citable) accession number: P83372
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 2002
Last sequence update: October 1, 2002
Last modified: February 19, 2014
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways