U.S. flag

An official website of the United States government

Format

Send to:

Choose Destination

CIT3 citrate (Si)-synthase CIT3 [ Saccharomyces cerevisiae S288C ]

Gene ID: 856107, updated on 13-Apr-2024

Summary

Go to the top of the page Help
Gene symbol
CIT3
Gene description
citrate (Si)-synthase CIT3
Primary source
SGD:S000006205
Locus tag
YPR001W
See related
AllianceGenome:SGD:S000006205
Gene type
protein coding
RefSeq status
REVIEWED
Organism
Saccharomyces cerevisiae S288C (strain: S288C)
Lineage
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
Summary
Enables 2-methylcitrate synthase activity and citrate (Si)-synthase activity. Involved in propionate catabolic process, 2-methylcitrate cycle and tricarboxylic acid cycle. Located in mitochondrion. Orthologous to human CS (citrate synthase). [provided by Alliance of Genome Resources, Apr 2022]
NEW
Try the new Gene table
Try the new Transcript table

Genomic context

Go to the top of the page Help
Location:
chromosome: XVI
Exon count:
1
Sequence:
Chromosome: XVI; NC_001148.4 (556377..557837)

Chromosome XVI - NC_001148.4Genomic Context describing neighboring genes Neighboring gene ESCRT-II subunit protein SNF8 Neighboring gene histone acetyltransferase catalytic subunit HAT1 Neighboring gene putative 2-methylcitrate dehydratase Neighboring gene tRNA-Phe

Genomic regions, transcripts, and products

Go to the top of the page Help
Genomic Sequence:
NC_001148.4

Go to nucleotide: Graphics FASTA GenBank

Bibliography

Go to the top of the pageHelp

Related articles in PubMed

  1. The CIT3 gene of Saccharomyces cerevisiae encodes a second mitochondrial isoform of citrate synthase. Jia YK, et al. Mol Microbiol, 1997 Apr. PMID 9140965
  2. Functional comparison of citrate synthase isoforms from S. cerevisiae. Graybill ER, et al. Arch Biochem Biophys, 2007 Sep 1. PMID 17570335
  3. Modulation of citrate metabolism alters aluminum tolerance in yeast and transgenic canola overexpressing a mitochondrial citrate synthase. Anoop VM, et al. Plant Physiol, 2003 Aug. PMID 12913175, Free PMC Article
  4. In vitro translation of mRNA for yeast citrate synthase. Alam T, et al. J Biol Chem, 1982 Sep 25. PMID 6809768
  5. Aspartate facilitates mitochondrial function, growth arrest and survival during doxorubicin exposure. Dornfeld K, et al. Cell Cycle, 2015. PMID 26317891, Free PMC Article

See all (37) citations in PubMed

GeneRIFs: Gene References Into Functions

Pathways from PubChem

Go to the top of the page

Interactions

Go to the top of the page Help
Products Interactant Other Gene Complex Source Pubs Description

General gene information

Go to the top of the page Help

Homology

Gene Ontology Provided by SGD

Function Evidence Code Pubs
enables 2-methylcitrate synthase activity IBA
Inferred from Biological aspect of Ancestor
more info
  
enables 2-methylcitrate synthase activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables 2-methylcitrate synthase activity IMP
Inferred from Mutant Phenotype
more info
 PubMed 
enables acyltransferase activity, acyl groups converted into alkyl on transfer IEA
Inferred from Electronic Annotation
more info
  
enables citrate (Si)-synthase activity IBA
Inferred from Biological aspect of Ancestor
more info
  
enables citrate (Si)-synthase activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables citrate (Si)-synthase activity IEA
Inferred from Electronic Annotation
more info
  
enables citrate (Si)-synthase activity IMP
Inferred from Mutant Phenotype
more info
 PubMed 
enables citrate synthase activity IEA
Inferred from Electronic Annotation
more info
  
enables transferase activity IEA
Inferred from Electronic Annotation
more info
  
Process Evidence Code Pubs
involved_in carbohydrate metabolic process IBA
Inferred from Biological aspect of Ancestor
more info
  
involved_in propionate catabolic process, 2-methylcitrate cycle IGI
Inferred from Genetic Interaction
more info
 PubMed 
involved_in tricarboxylic acid cycle IBA
Inferred from Biological aspect of Ancestor
more info
  
involved_in tricarboxylic acid cycle IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in tricarboxylic acid cycle IEA
Inferred from Electronic Annotation
more info
  
Component Evidence Code Pubs
is_active_in mitochondrial matrix IBA
Inferred from Biological aspect of Ancestor
more info
  
located_in mitochondrion HDA PubMed 
located_in mitochondrion IDA
Inferred from Direct Assay
more info
 PubMed 
located_in mitochondrion IEA
Inferred from Electronic Annotation
more info
  

General protein information

Go to the top of the page Help
Preferred Names
citrate (Si)-synthase CIT3
NP_015325.1
  • Dual specificity mitochondrial citrate and methylcitrate synthase; catalyzes the condensation of acetyl-CoA and oxaloacetate to form citrate and that of propionyl-CoA and oxaloacetate to form 2-methylcitrate

NCBI Reference Sequences (RefSeq)

Go to the top of the page Help

NEW Try the new Transcript table

Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

  1. NC_001148.4 Reference assembly

    Range
    556377..557837
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NM_001184098.1 → NP_015325.1  TPA: citrate (Si)-synthase CIT3 [Saccharomyces cerevisiae S288C]

    See identical proteins and their annotated locations for NP_015325.1

    Status: REVIEWED

    UniProtKB/Swiss-Prot
    D6W412, P43635
    UniProtKB/TrEMBL
    A0A8H4BU05, B3LL62, B5VTG1, C7GV45, C8ZJ26, N1P1X2
    Conserved Domains (1) summary
    cd06106
    Location:29 → 474
    ScCit3_like; Saccharomyces cerevisiae (Sc) 2-methylcitrate synthase Cit3-like. 2-methylcitrate synthase (2MCS) catalyzes the condensation of propionyl-coenzyme A (PrCoA) and oxaloacetate (OAA) to form 2-methylcitrate and CoA. Citrate synthase (CS) catalyzes the ...
Nucleotide Protein
Heading Accession and Version
Protein Accession Links
GenPept Link UniProtKB Link
P43635.1

Gene LinkOut

The following LinkOut resources are supplied by external providers. These providers are responsible for maintaining the links.

Other Literature Sources
Molecular Biology Databases
Research Materials
Tools
Miscellaneous