Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Citrate synthase, mitochondrial

Gene

CS

Organism
Sus scrofa (Pig)
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 sitei3011
Active sitei3471
Active sitei4021

GO - Molecular functioni

  • citrate (Si)-synthase activity Source: UniProtKB
  • citrate synthase activity Source: CAFA

GO - Biological processi

Keywordsi

Molecular functionTransferase
Biological processTricarboxylic acid cycle

Enzyme and pathway databases

BRENDAi2.3.3.1 6170
2.3.3.16 6170
SABIO-RKiP00889
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
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
Proteomesi
  • UP000008227 Componenti: Unplaced

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 27Mitochondrion1 PublicationAdd BLAST27
ChainiPRO_000000547328 – 464Citrate synthase, mitochondrialAdd BLAST437

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei76N6-acetyllysine; alternateBy similarity1
Modified residuei76N6-succinyllysine; alternateBy similarity1
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-trimethyllysine1 Publication1
Modified residuei450N6-succinyllysineBy similarity1
Modified residuei459N6-acetyllysine; alternateBy similarity1
Modified residuei459N6-succinyllysine; alternateBy similarity1

Post-translational modificationi

Methylated (PubMed:7093227). Trimethylation at Lys-395 by CSKMT decreases citrate synthase activity (By similarity).By similarity1 Publication

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

PaxDbiP00889
PeptideAtlasiP00889
PRIDEiP00889

PTM databases

iPTMnetiP00889

Expressioni

Gene expression databases

GenevisibleiP00889 SS

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

BioGridi1149646, 2 interactors
STRINGi9823.ENSSSCP00000021332

Structurei

Secondary structure

1464
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi33 – 55Combined sources23
Beta strandi59 – 64Combined sources6
Helixi65 – 69Combined sources5
Turni70 – 74Combined sources5
Beta strandi76 – 79Combined sources4
Beta strandi82 – 86Combined sources5
Turni87 – 89Combined sources3
Beta strandi90 – 93Combined sources4
Helixi98 – 104Combined sources7
Beta strandi109 – 111Combined sources3
Beta strandi112 – 114Combined sources3
Helixi116 – 125Combined sources10
Helixi131 – 143Combined sources13
Helixi149 – 157Combined sources9
Beta strandi160 – 162Combined sources3
Helixi164 – 174Combined sources11
Helixi175 – 178Combined sources4
Helixi180 – 187Combined sources8
Helixi191 – 193Combined sources3
Helixi194 – 221Combined sources28
Beta strandi232 – 234Combined sources3
Helixi236 – 244Combined sources9
Helixi249 – 261Combined sources13
Turni266 – 268Combined sources3
Helixi270 – 280Combined sources11
Helixi285 – 296Combined sources12
Helixi299 – 302Combined sources4
Helixi304 – 319Combined sources16
Helixi325 – 337Combined sources13
Beta strandi345 – 349Combined sources5
Helixi355 – 367Combined sources13
Helixi372 – 391Combined sources20
Beta strandi394 – 399Combined sources6
Helixi401 – 403Combined sources3
Helixi405 – 411Combined sources7
Helixi417 – 419Combined sources3
Helixi420 – 441Combined sources22
Beta strandi450 – 452Combined sources3
Helixi454 – 463Combined sources10

3D structure databases

ProteinModelPortaliP00889
SMRiP00889
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00889

Family & Domainsi

Sequence similaritiesi

Belongs to the citrate synthase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG2617 Eukaryota
COG0372 LUCA
HOGENOMiHOG000130831
HOVERGENiHBG005336
InParanoidiP00889
KOiK01647
OrthoDBiEOG091G068F

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.

P00889-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALLTAAARL FGAKNASCLV LAARHASASS TNLKDILADL IPKEQARIKT
60 70 80 90 100
FRQQHGNTVV GQITVDMMYG GMRGMKGLVY ETSVLDPDEG IRFRGYSIPE
110 120 130 140 150
CQKMLPKAKG GEEPLPEGLF WLLVTGQIPT EEQVSWLSKE WAKRAALPSH
160 170 180 190 200
VVTMLDNFPT NLHPMSQLSA AITALNSESN FARAYAEGIH RTKYWELIYE
210 220 230 240 250
DCMDLIAKLP CVAAKIYRNL YREGSSIGAI DSKLDWSHNF 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 REFALKHLPH DPMFKLVAQL YKIVPNVLLE QGKAKNPWPN
410 420 430 440 450
VDAHSGVLLQ YYGMTEMNYY TVLFGVSRAL GVLAQLIWSR ALGFPLERPK
460
SMSTDGLIKL VDSK
Length:464
Mass (Da):51,629
Last modified:October 1, 1989 - v2
Checksum:i66719A7504DF322A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M21197 mRNA Translation: AAA31017.1
PIRiA29966 YKPG
RefSeqiNP_999441.1, NM_214276.1
UniGeneiSsc.16315

Genome annotation databases

GeneIDi397519
KEGGissc:397519

Similar proteinsi

Entry informationi

Entry nameiCISY_PIG
AccessioniPrimary (citable) accession number: P00889
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: October 1, 1989
Last modified: April 25, 2018
This is version 136 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health