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Protein

Citrate synthase, mitochondrial

Gene

CS

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 3 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 sitei301 – 3011PROSITE-ProRule annotation
Active sitei347 – 3471PROSITE-ProRule annotation
Active sitei402 – 4021PROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Tricarboxylic acid cycle

Enzyme and pathway databases

ReactomeiREACT_347675. Citric acid cycle (TCA cycle).
UniPathwayiUPA00223; UER00717.

Names & Taxonomyi

Protein namesi
Recommended name:
Citrate synthase, mitochondrial (EC:2.3.3.1)
Alternative name(s):
Citrate (Si)-synthase
Gene namesi
Name:CS
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136 Componenti: Chromosome 5

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2727MitochondrionBy similarityAdd
BLAST
Chaini28 – 466439Citrate synthase, mitochondrialPRO_0000244377Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei57 – 571N6-succinyllysineBy similarity
Modified residuei76 – 761N6-acetyllysine; alternate1 Publication
Modified residuei76 – 761N6-succinyllysine; alternate1 Publication
Modified residuei103 – 1031N6-succinyllysineBy similarity
Modified residuei193 – 1931N6-succinyllysineBy similarity
Modified residuei321 – 3211N6-acetyllysine; alternateBy similarity
Modified residuei321 – 3211N6-succinyllysine; alternateBy similarity
Modified residuei327 – 3271N6-acetyllysine; alternateBy similarity
Modified residuei327 – 3271N6-succinyllysine; alternateBy similarity
Modified residuei375 – 3751N6-acetyllysine; alternateBy similarity
Modified residuei375 – 3751N6-succinyllysine; alternateBy similarity
Modified residuei382 – 3821N6-acetyllysineBy similarity
Modified residuei393 – 3931N6-acetyllysine; alternateBy similarity
Modified residuei393 – 3931N6-succinyllysine; alternateBy similarity
Modified residuei395 – 3951N6,N6,N6-trimethyllysineBy similarity
Modified residuei450 – 4501N6-succinyllysineBy similarity
Modified residuei459 – 4591N6-acetyllysine; alternateBy similarity
Modified residuei459 – 4591N6-succinyllysine; alternateBy similarity

Keywords - PTMi

Acetylation, Methylation

Proteomic databases

PaxDbiQ29RK1.
PRIDEiQ29RK1.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

IntActiQ29RK1. 1 interaction.
STRINGi9913.ENSBTAP00000005730.

Structurei

3D structure databases

ProteinModelPortaliQ29RK1.
SMRiQ29RK1. Positions 28-464.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the citrate synthase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0372.
GeneTreeiENSGT00390000006813.
HOGENOMiHOG000130831.
HOVERGENiHBG005336.
InParanoidiQ29RK1.
KOiK01647.
OMAiITDYLWS.
OrthoDBiEOG73BVCB.
TreeFamiTF300398.

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.

Q29RK1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALLTAAARL FGAKNASCLV LAARHASASS TNLKDILADL IPKEQTRVKA
60 70 80 90 100
FRQQHGKTVV GQITVDMMYG GMRGMKGLVY ETSVLDPDEG IRFRGYSIPE
110 120 130 140 150
CQKLLPKAKG GEEPLPEGLF WLLVTGQIPT EEQVSWLSQE WAKRAALPSH
160 170 180 190 200
VVTMLDNFPT NLHPMSQLSA AVTALNSEST FARAYSEGIN RTKYWELIYE
210 220 230 240 250
DSMDLIAKLP CVAAKIYRNL YREGSSIGAI DPKLDWSHNF TNMLGYTDAQ
260 270 280 290 300
FTELMRLYLT IHSDHEGGNV SAHTSHLVGS ALSDPYLSFA AAMNGLAGPL
310 320 330 340 350
HGLANQEVLV WLTQLQKEVG KDVSDEKLRD YIWNTLNSGR VVPGYGHAVL
360 370 380 390 400
RKTDPRYTCQ REFALKHLPQ DPMFKLVAQL YKIVPNILLE QGKAKNPWPN
410 420 430 440 450
VDAHSGVLLQ YYGMTEMNYY TVLFGVSRAL GVLAQLIWSR ALGFPLERPK
460
SMSTDGLMKF VDSKSG
Length:466
Mass (Da):51,773
Last modified:April 4, 2006 - v1
Checksum:i73C2CB93589084B3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC114138 mRNA. Translation: AAI14139.1.
RefSeqiNP_001038186.1. NM_001044721.1.
UniGeneiBt.106917.

Genome annotation databases

EnsembliENSBTAT00000005730; ENSBTAP00000005730; ENSBTAG00000004371.
GeneIDi280682.
KEGGibta:280682.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC114138 mRNA. Translation: AAI14139.1.
RefSeqiNP_001038186.1. NM_001044721.1.
UniGeneiBt.106917.

3D structure databases

ProteinModelPortaliQ29RK1.
SMRiQ29RK1. Positions 28-464.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ29RK1. 1 interaction.
STRINGi9913.ENSBTAP00000005730.

Chemistry

ChEMBLiCHEMBL2406901.

Proteomic databases

PaxDbiQ29RK1.
PRIDEiQ29RK1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000005730; ENSBTAP00000005730; ENSBTAG00000004371.
GeneIDi280682.
KEGGibta:280682.

Organism-specific databases

CTDi1431.

Phylogenomic databases

eggNOGiCOG0372.
GeneTreeiENSGT00390000006813.
HOGENOMiHOG000130831.
HOVERGENiHBG005336.
InParanoidiQ29RK1.
KOiK01647.
OMAiITDYLWS.
OrthoDBiEOG73BVCB.
TreeFamiTF300398.

Enzyme and pathway databases

UniPathwayiUPA00223; UER00717.
ReactomeiREACT_347675. Citric acid cycle (TCA cycle).

Miscellaneous databases

NextBioi20804872.
PROiQ29RK1.

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. NIH - Mammalian Gene Collection (MGC) project
    Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Hereford.
    Tissue: Heart ventricle.
  2. "Sirt5 is a NAD-dependent protein lysine demalonylase and desuccinylase."
    Du J., Zhou Y., Su X., Yu J.J., Khan S., Jiang H., Kim J., Woo J., Kim J.H., Choi B.H., He B., Chen W., Zhang S., Cerione R.A., Auwerx J., Hao Q., Lin H.
    Science 334:806-809(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION AT LYS-76, SUCCINYLATION AT LYS-76.

Entry informationi

Entry nameiCISY_BOVIN
AccessioniPrimary (citable) accession number: Q29RK1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: April 4, 2006
Last modified: May 27, 2015
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

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.