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Protein

Citrate synthase, mitochondrial

Gene

CIT1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Acetyl-CoA + H2O + oxaloacetate = citrate + CoA.PROSITE-ProRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei312 – 3121PROSITE-ProRule annotation
Active sitei358 – 3581PROSITE-ProRule annotation
Active sitei413 – 4131PROSITE-ProRule annotation

GO - Molecular functioni

  1. citrate (Si)-synthase activity Source: SGD

GO - Biological processi

  1. acetyl-CoA catabolic process Source: SGD
  2. cellular carbohydrate metabolic process Source: InterPro
  3. citrate metabolic process Source: SGD
  4. glutamate biosynthetic process Source: SGD
  5. tricarboxylic acid cycle Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Tricarboxylic acid cycle

Enzyme and pathway databases

BioCyciYEAST:YNR001C-MONOMER.
BRENDAi2.3.3.16. 984.
ReactomeiREACT_278278. Citric acid cycle (TCA cycle).
REACT_334110. Mitochondrial protein import.
UniPathwayiUPA00223; UER00717.

Names & Taxonomyi

Protein namesi
Recommended name:
Citrate synthase, mitochondrial (EC:2.3.3.16)
Gene namesi
Name:CIT1
Synonyms:GLU3, LYS6
Ordered Locus Names:YNR001C
ORF Names:N2019
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome XIV

Organism-specific databases

CYGDiYNR001c.
SGDiS000005284. CIT1.

Subcellular locationi

Mitochondrion matrix 1 Publication

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. mitochondrial intermembrane space Source: Reactome
  3. mitochondrial matrix Source: UniProtKB-SubCell
  4. mitochondrion Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3737MitochondrionAdd
BLAST
Chaini38 – 479442Citrate synthase, mitochondrialPRO_0000005479Add
BLAST

Proteomic databases

MaxQBiP00890.
PaxDbiP00890.
PeptideAtlasiP00890.
PRIDEiP00890.

Expressioni

Gene expression databases

GenevestigatoriP00890.

Interactioni

Protein-protein interaction databases

BioGridi35825. 49 interactions.
DIPiDIP-4597N.
IntActiP00890. 5 interactions.
MINTiMINT-567581.
STRINGi4932.YNR001C.

Structurei

3D structure databases

ProteinModelPortaliP00890.
SMRiP00890. Positions 40-478.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the citrate synthase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0372.
GeneTreeiENSGT00780000122917.
HOGENOMiHOG000130831.
InParanoidiP00890.
KOiK01647.
OMAiITDYLWS.
OrthoDBiEOG7WQ82G.

Family and domain databases

Gene3Di1.10.580.10. 1 hit.
InterProiIPR016142. 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]
PANTHERiPTHR11739. PTHR11739. 1 hit.
PfamiPF00285. Citrate_synt. 1 hit.
[Graphical view]
PRINTSiPR00143. CITRTSNTHASE.
SUPFAMiSSF48256. SSF48256. 1 hit.
TIGRFAMsiTIGR01793. cit_synth_euk. 1 hit.
PROSITEiPS00480. CITRATE_SYNTHASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P00890-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSAILSTTSK SFLSRGSTRQ CQNMQKALFA LLNARHYSSA SEQTLKERFA
60 70 80 90 100
EIIPAKAEEI KKFKKEHGKT VIGEVLLEQA YGGMRGIKGL VWEGSVLDPE
110 120 130 140 150
EGIRFRGRTI PEIQRELPKA EGSTEPLPEA LFWLLLTGEI PTDAQVKALS
160 170 180 190 200
ADLAARSEIP EHVIQLLDSL PKDLHPMAQF SIAVTALESE SKFAKAYAQG
210 220 230 240 250
VSKKEYWSYT FEDSLDLLGK LPVIASKIYR NVFKDGKITS TDPNADYGKN
260 270 280 290 300
LAQLLGYENK DFIDLMRLYL TIHSDHEGGN VSAHTTHLVG SALSSPYLSL
310 320 330 340 350
AAGLNGLAGP LHGRANQEVL EWLFKLREEV KGDYSKETIE KYLWDTLNAG
360 370 380 390 400
RVVPGYGHAV LRKTDPRYTA QREFALKHFP DYELFKLVST IYEVAPGVLT
410 420 430 440 450
KHGKTKNPWP NVDSHSGVLL QYYGLTEASF YTVLFGVARA IGVLPQLIID
460 470
RAVGAPIERP KSFSTEKYKE LVKKIESKN
Length:479
Mass (Da):53,360
Last modified:February 1, 1994 - v2
Checksum:i280661B1CB248F14
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti58 – 581E → Q in CAA25359 (PubMed:6090126).Curated
Sequence conflicti78 – 781E → EE in CAA25359 (PubMed:6090126).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X00782 Genomic DNA. Translation: CAA25359.1.
Z23259 Genomic DNA. Translation: CAA80781.1.
X77395 Genomic DNA. Translation: CAA54569.1.
Z71616 Genomic DNA. Translation: CAA96277.1.
BK006947 Genomic DNA. Translation: DAA10543.1.
PIRiS35390. YKBY.
RefSeqiNP_014398.1. NM_001183178.1.

Genome annotation databases

EnsemblFungiiYNR001C; YNR001C; YNR001C.
GeneIDi855732.
KEGGisce:YNR001C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X00782 Genomic DNA. Translation: CAA25359.1.
Z23259 Genomic DNA. Translation: CAA80781.1.
X77395 Genomic DNA. Translation: CAA54569.1.
Z71616 Genomic DNA. Translation: CAA96277.1.
BK006947 Genomic DNA. Translation: DAA10543.1.
PIRiS35390. YKBY.
RefSeqiNP_014398.1. NM_001183178.1.

3D structure databases

ProteinModelPortaliP00890.
SMRiP00890. Positions 40-478.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35825. 49 interactions.
DIPiDIP-4597N.
IntActiP00890. 5 interactions.
MINTiMINT-567581.
STRINGi4932.YNR001C.

Proteomic databases

MaxQBiP00890.
PaxDbiP00890.
PeptideAtlasiP00890.
PRIDEiP00890.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYNR001C; YNR001C; YNR001C.
GeneIDi855732.
KEGGisce:YNR001C.

Organism-specific databases

CYGDiYNR001c.
SGDiS000005284. CIT1.

Phylogenomic databases

eggNOGiCOG0372.
GeneTreeiENSGT00780000122917.
HOGENOMiHOG000130831.
InParanoidiP00890.
KOiK01647.
OMAiITDYLWS.
OrthoDBiEOG7WQ82G.

Enzyme and pathway databases

UniPathwayiUPA00223; UER00717.
BioCyciYEAST:YNR001C-MONOMER.
BRENDAi2.3.3.16. 984.
ReactomeiREACT_278278. Citric acid cycle (TCA cycle).
REACT_334110. Mitochondrial protein import.

Miscellaneous databases

NextBioi980117.

Gene expression databases

GenevestigatoriP00890.

Family and domain databases

Gene3Di1.10.580.10. 1 hit.
InterProiIPR016142. 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]
PANTHERiPTHR11739. PTHR11739. 1 hit.
PfamiPF00285. Citrate_synt. 1 hit.
[Graphical view]
PRINTSiPR00143. CITRTSNTHASE.
SUPFAMiSSF48256. SSF48256. 1 hit.
TIGRFAMsiTIGR01793. cit_synth_euk. 1 hit.
PROSITEiPS00480. CITRATE_SYNTHASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation of the nuclear yeast genes for citrate synthase and fifteen other mitochondrial proteins by a new screening method."
    Suissa M., Suda K., Schatz G.
    EMBO J. 3:1773-1781(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 24657 / D273-10B.
  2. "The effect of point mutations in the hinge of yeast citrate synthase."
    Lindner P., Plueckthun A.
    Submitted (JUN-1993) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
    Strain: ATCC 24657 / D273-10B.
  3. "Organization of the centromeric region of chromosome XIV in Saccharomyces cerevisiae."
    Lalo D., Stettler S., Mariotte S., Gendreau E., Thuriaux P.
    Yeast 10:523-533(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: S288c / GRF88.
  4. "Twelve open reading frames revealed in the 23.6 kb segment flanking the centromere on the Saccharomyces cerevisiae chromosome XIV right arm."
    Verhasselt P., Aert R., Voet M., Volckaert G.
    Yeast 10:1355-1361(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 96604 / S288c / FY1679.
  5. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications."
    Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J.
    , Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.
    Nature 387:93-98(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  6. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  7. "Yeast mitochondrial dehydrogenases are associated in a supramolecular complex."
    Grandier-Vazeille X., Bathany K., Chaignepain S., Camougrand N., Manon S., Schmitter J.-M.
    Biochemistry 40:9758-9769(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiCISY1_YEAST
AccessioniPrimary (citable) accession number: P00890
Secondary accession number(s): D6W1H7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: February 1, 1994
Last modified: April 1, 2015
This is version 145 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XIV
    Yeast (Saccharomyces cerevisiae) chromosome XIV: entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.