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Protein

Citrate synthase, mitochondrial

Gene

CS

Organism
Sus scrofa (Pig)
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: 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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Tricarboxylic acid cycle

Enzyme and pathway databases

BRENDAi2.3.3.1. 6170.
2.3.3.16. 6170.
SABIO-RKP00889.
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

GO - Cellular componenti

Complete GO annotation...

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

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

PaxDbiP00889.
PeptideAtlasiP00889.
PRIDEiP00889.

PTM databases

iPTMnetiP00889.

Expressioni

Gene expression databases

BgeeiENSSSCG00000022858.
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 – 186Combined sources7
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
Turni299 – 301Combined sources3
Helixi304 – 319Combined sources16
Helixi325 – 336Combined sources12
Turni337 – 339Combined sources3
Beta strandi345 – 349Combined sources5
Helixi355 – 367Combined sources13
Helixi372 – 390Combined sources19
Beta strandi394 – 399Combined sources6
Helixi401 – 403Combined sources3
Helixi405 – 411Combined sources7
Helixi417 – 419Combined sources3
Helixi420 – 441Combined sources22
Helixi454 – 463Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CTSX-ray2.70A28-464[»]
2CTSX-ray2.00A28-464[»]
3ENJX-ray1.78A28-464[»]
4CTSX-ray2.90A/B28-464[»]
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

Gene3Di1.10.580.10. 1 hit.
InterProiIPR016142. Citrate_synth-like_lrg_a-sub.
IPR002020. Citrate_synthase.
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.

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.

Cross-referencesi

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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CTSX-ray2.70A28-464[»]
2CTSX-ray2.00A28-464[»]
3ENJX-ray1.78A28-464[»]
4CTSX-ray2.90A/B28-464[»]
ProteinModelPortaliP00889.
SMRiP00889.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi1149646. 2 interactors.
STRINGi9823.ENSSSCP00000021332.

PTM databases

iPTMnetiP00889.

Proteomic databases

PaxDbiP00889.
PeptideAtlasiP00889.
PRIDEiP00889.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi397519.
KEGGissc:397519.

Organism-specific databases

CTDi1431.

Phylogenomic databases

eggNOGiKOG2617. Eukaryota.
COG0372. LUCA.
HOGENOMiHOG000130831.
HOVERGENiHBG005336.
InParanoidiP00889.
KOiK01647.
OrthoDBiEOG091G068F.

Enzyme and pathway databases

UniPathwayiUPA00223; UER00717.
BRENDAi2.3.3.1. 6170.
2.3.3.16. 6170.
SABIO-RKP00889.

Miscellaneous databases

EvolutionaryTraceiP00889.

Gene expression databases

BgeeiENSSSCG00000022858.
GenevisibleiP00889. SS.

Family and domain databases

Gene3Di1.10.580.10. 1 hit.
InterProiIPR016142. Citrate_synth-like_lrg_a-sub.
IPR002020. Citrate_synthase.
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...

Entry informationi

Entry nameiCISY_PIG
AccessioniPrimary (citable) accession number: P00889
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: October 1, 1989
Last modified: November 2, 2016
This is version 127 of the entry and version 2 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

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

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 one 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.