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Protein

Citrate synthase, mitochondrial

Gene

CS

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Miscellaneous

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

Catalytic activityi

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

Pathwayi: tricarboxylic acid cycle

This protein is involved in step 1 of the subpathway that synthesizes isocitrate from oxaloacetate.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Citrate synthase, mitochondrial (CS)
  2. Aconitate hydratase, mitochondrial (ACO2)
This subpathway is part of the pathway tricarboxylic acid cycle, which is itself part of Carbohydrate metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes isocitrate from oxaloacetate, the pathway tricarboxylic acid cycle and in Carbohydrate metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei301PROSITE-ProRule annotation1
Active sitei347PROSITE-ProRule annotation1
Active sitei402PROSITE-ProRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionTransferase
Biological processTricarboxylic acid cycle

Enzyme and pathway databases

ReactomeiR-BTA-71403 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
Proteomesi
  • UP000009136 Componenti: Chromosome 5

Organism-specific databases

VGNCiVGNC:27748 CS

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL2406901

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 27MitochondrionBy similarityAdd BLAST27
ChainiPRO_000024437728 – 466Citrate synthase, mitochondrialAdd BLAST439

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei57N6-succinyllysineBy similarity1
Modified residuei76N6-acetyllysine; alternate1 Publication1
Modified residuei76N6-succinyllysine; alternate1 Publication1
Modified residuei103N6-succinyllysineBy similarity1
Modified residuei193N6-succinyllysineBy similarity1
Modified residuei226PhosphoserineBy similarity1
Modified residuei321N6-acetyllysine; alternateBy similarity1
Modified residuei321N6-succinyllysine; alternateBy similarity1
Modified residuei327N6-acetyllysine; alternateBy similarity1
Modified residuei327N6-succinyllysine; alternateBy similarity1
Modified residuei375N6-acetyllysine; alternateBy similarity1
Modified residuei375N6-succinyllysine; alternateBy similarity1
Modified residuei382N6-acetyllysineBy similarity1
Modified residuei393N6-acetyllysine; alternateBy similarity1
Modified residuei393N6-succinyllysine; alternateBy similarity1
Modified residuei395N6,N6,N6-trimethyllysineBy similarity1
Modified residuei450N6-succinyllysineBy similarity1
Modified residuei459N6-acetyllysine; alternateBy similarity1
Modified residuei459N6-succinyllysine; alternateBy similarity1

Post-translational modificationi

Methylated. Trimethylation at Lys-395 by CSKMT decreases citrate synthase activity.By similarity

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

PaxDbiQ29RK1
PeptideAtlasiQ29RK1
PRIDEiQ29RK1

PTM databases

iPTMnetiQ29RK1

Expressioni

Gene expression databases

BgeeiENSBTAG00000004371

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

IntActiQ29RK1, 1 interactor
STRINGi9913.ENSBTAP00000005730

Structurei

3D structure databases

ProteinModelPortaliQ29RK1
SMRiQ29RK1
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the citrate synthase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG2617 Eukaryota
COG0372 LUCA
GeneTreeiENSGT00390000006813
HOGENOMiHOG000130831
HOVERGENiHBG005336
InParanoidiQ29RK1
KOiK01647
OMAiTVGWCAQ
OrthoDBiEOG091G068F
TreeFamiTF300398

Family and domain databases

Gene3Di1.10.230.10, 1 hit
1.10.580.10, 2 hits
InterProiView protein in InterPro
IPR016142 Citrate_synth-like_lrg_a-sub
IPR016143 Citrate_synth-like_sm_a-sub
IPR002020 Citrate_synthase
IPR019810 Citrate_synthase_AS
IPR010109 Citrate_synthase_euk
IPR036969 Citrate_synthase_sf
PANTHERiPTHR11739 PTHR11739, 1 hit
PfamiView protein in Pfam
PF00285 Citrate_synt, 1 hit
PRINTSiPR00143 CITRTSNTHASE
SUPFAMiSSF48256 SSF48256, 1 hit
TIGRFAMsiTIGR01793 cit_synth_euk, 1 hit
PROSITEiView protein in PROSITE
PS00480 CITRATE_SYNTHASE, 1 hit

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

Similar proteinsi

Entry informationi

Entry nameiCISY_BOVIN
AccessioniPrimary (citable) accession number: Q29RK1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: April 4, 2006
Last modified: March 28, 2018
This is version 94 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health