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Q43175 (CISY_SOLTU) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 81. 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=2.3.3.16
OrganismSolanum tuberosum (Potato) [Reference proteome]
Taxonomic identifier4113 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesSolanaceaeSolanoideaeSolaneaeSolanum

Protein attributes

Sequence length471 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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.

Subcellular location

Mitochondrion matrix.

Tissue specificity

Ubiquitous.

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
   DomainTransit peptide
   Molecular functionTransferase
   Technical termComplete proteome
Reference proteome
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: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – ?Mitochondrion Potential
Chain? – 471Citrate synthase, mitochondrialPRO_0000005489

Sites

Active site3091 By similarity
Active site3551 By similarity
Active site4091 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q43175 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: BC6B5673792564C6

FASTA47152,612
        10         20         30         40         50         60 
MVFYRSVSLL SKLRSRAVQQ SNVSNSVRWL QVQTSSGLDL RSELVQELIP EQQDRLKKIK 

        70         80         90        100        110        120 
SDMKGSIGNI TVDMVLGGMR GMTGLLWKPH YLDPDEGIRF RGLSIPECQK VLPAAKPGGE 

       130        140        150        160        170        180 
PLPEGLLWLL LTGKVPSKEQ VNSIVSGIAE SGIISLIIMY TTIDALPVTA HPMTQFATGV 

       190        200        210        220        230        240 
MALQVQSEFQ KAYEKGIHKS KYWEPTYEDS MNLIAQVPLV AAYVYRRMYK NGDTIPKDES 

       250        260        270        280        290        300 
LDYGANFAHM LGFSSSEMHE LLMRLYVTIH SDHEGGNVSA HTGHLVASAL SDPYLSFAAA 

       310        320        330        340        350        360 
LNGLAGPLHG LANQEVLLWI KSVVEECGEN ISKEQLKDYV WKTLNSGKVV PGFGHGVLRK 

       370        380        390        400        410        420 
TVPRYTCQRE FAMKHLPEDP LFQLVSKLYE VFLLFLQNLA KLKPWPNVDA HSGVLLNYYG 

       430        440        450        460        470 
LTEARYYTVL FGVSRALGIC SQLIWDRALG LPLERPKSVT MEWLENQCKK A 

« Hide

References

[1]"Mitochondrial citrate synthase from potato: predominant expression in mature leaves and young flower buds."
Landschuetze V., Willmitzer L., Mueller-Roeber B.
Planta 196:756-764(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Desiree.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X75082 mRNA. Translation: CAA52976.1.
PIRS44316.

3D structure databases

ProteinModelPortalQ43175.
SMRQ43175. Positions 39-469.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ43175.

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_SOLTU
AccessionPrimary (citable) accession number: Q43175
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1996
Last modified: June 11, 2014
This is version 81 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