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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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei301 – 3011
Active sitei347 – 3471
Active sitei402 – 4021

GO - Molecular functioni

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

GO - Biological processi

  1. carbohydrate metabolic process Source: UniProtKB
  2. cellular carbohydrate metabolic process Source: InterPro
  3. tricarboxylic acid cycle Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Tricarboxylic acid cycle

Enzyme and pathway databases

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
ProteomesiUP000008227: Unplaced

Subcellular locationi

GO - Cellular componenti

  1. mitochondrial matrix Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2727Mitochondrion1 PublicationAdd
BLAST
Chaini28 – 464437Citrate synthase, mitochondrialPRO_0000005473Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei76 – 761N6-acetyllysine; alternateBy similarity
Modified residuei76 – 761N6-succinyllysine; alternateBy similarity
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-trimethyllysine1 Publication
Modified residuei450 – 4501N6-succinyllysineBy similarity
Modified residuei459 – 4591N6-acetyllysine; alternateBy similarity
Modified residuei459 – 4591N6-succinyllysine; alternateBy similarity

Keywords - PTMi

Acetylation, Methylation

Proteomic databases

PaxDbiP00889.
PRIDEiP00889.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

BioGridi1149646. 2 interactions.
STRINGi9823.ENSSSCP00000000410.

Structurei

Secondary structure

1
464
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi33 – 5523Combined sources
Beta strandi59 – 646Combined sources
Helixi65 – 695Combined sources
Turni70 – 745Combined sources
Beta strandi76 – 794Combined sources
Beta strandi82 – 865Combined sources
Turni87 – 893Combined sources
Beta strandi90 – 934Combined sources
Helixi98 – 1047Combined sources
Beta strandi109 – 1113Combined sources
Beta strandi112 – 1143Combined sources
Helixi116 – 12510Combined sources
Helixi131 – 14313Combined sources
Helixi149 – 1579Combined sources
Beta strandi160 – 1623Combined sources
Helixi164 – 17411Combined sources
Helixi175 – 1784Combined sources
Helixi180 – 1867Combined sources
Helixi191 – 1933Combined sources
Helixi194 – 22128Combined sources
Beta strandi232 – 2343Combined sources
Helixi236 – 2449Combined sources
Helixi249 – 26113Combined sources
Turni266 – 2683Combined sources
Helixi270 – 28011Combined sources
Helixi285 – 29612Combined sources
Turni299 – 3013Combined sources
Helixi304 – 31916Combined sources
Helixi325 – 33612Combined sources
Turni337 – 3393Combined sources
Beta strandi345 – 3495Combined sources
Helixi355 – 36713Combined sources
Helixi372 – 39019Combined sources
Beta strandi394 – 3996Combined sources
Helixi401 – 4033Combined sources
Helixi405 – 4117Combined sources
Helixi417 – 4193Combined sources
Helixi420 – 44122Combined sources
Helixi454 – 46310Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CTSX-ray2.70A28-464[»]
2CTSX-ray2.00A28-464[»]
3ENJX-ray1.78A28-464[»]
4CTSX-ray2.90A/B28-464[»]
ProteinModelPortaliP00889.
SMRiP00889. Positions 28-464.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00889.

Family & Domainsi

Sequence similaritiesi

Belongs to the citrate synthase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0372.
HOGENOMiHOG000130831.
HOVERGENiHBG005336.
InParanoidiP00889.
KOiK01647.

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.

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
EntryMethodResolution (Å)ChainPositionsPDBsum
1CTSX-ray2.70A28-464[»]
2CTSX-ray2.00A28-464[»]
3ENJX-ray1.78A28-464[»]
4CTSX-ray2.90A/B28-464[»]
ProteinModelPortaliP00889.
SMRiP00889. Positions 28-464.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi1149646. 2 interactions.
STRINGi9823.ENSSSCP00000000410.

Proteomic databases

PaxDbiP00889.
PRIDEiP00889.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi397519.
KEGGissc:397519.

Organism-specific databases

CTDi1431.

Phylogenomic databases

eggNOGiCOG0372.
HOGENOMiHOG000130831.
HOVERGENiHBG005336.
InParanoidiP00889.
KOiK01647.

Enzyme and pathway databases

UniPathwayiUPA00223; UER00717.
SABIO-RKP00889.

Miscellaneous databases

EvolutionaryTraceiP00889.

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

  1. "Isolation, nucleotide sequence, and expression of a cDNA encoding pig citrate synthase."
    Evans C.T., Owens D.D., Sumegi B., Kispal G., Srere P.A.
    Biochemistry 27:4680-4686(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Complete amino acid sequence of porcine heart citrate synthase."
    Bloxham D.P., Parmelee D.C., Kumar S., Walsh K.A., Titani K.
    Biochemistry 21:2028-2036(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 28-464, METHYLATION AT LYS-395.
  3. "Crystallographic refinement and atomic models of two different forms of citrate synthase at 2.7- and 1.7-A resolution."
    Remington S., Wiegand G., Huber R.
    J. Mol. Biol. 158:111-152(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
  4. "Mutation of essential catalytic residues in pig citrate synthase."
    Alter G.M., Casazza J.P., Zhi W., Nemeth P., Srere P.A., Evans C.T.
    Biochemistry 29:7557-7563(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS.

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: March 4, 2015
This is version 116 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

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.