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Protein

Citrate synthase, mitochondrial

Gene

CS

Organism
Gallus gallus (Chicken)
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 annotation1 Publication

Pathway: 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. no protein annotated in this organism
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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei274 – 2741
Active sitei320 – 3201
Active sitei375 – 3751

GO - Molecular functioni

  • citrate (Si)-synthase activity Source: AgBase
  • citrate synthase activity Source: AgBase

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Tricarboxylic acid cycle

Enzyme and pathway databases

ReactomeiREACT_115536. The tricarboxylic acid 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
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
ProteomesiUP000000539 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 433433Citrate synthase, mitochondrialPRO_0000169983Add
BLAST

Proteomic databases

PRIDEiP23007.

Interactioni

Subunit structurei

Homodimer.

Structurei

Secondary structure

1
433
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 2823Combined sources
Beta strandi31 – 344Combined sources
Helixi38 – 425Combined sources
Turni43 – 475Combined sources
Beta strandi49 – 524Combined sources
Beta strandi55 – 595Combined sources
Turni60 – 623Combined sources
Beta strandi63 – 664Combined sources
Helixi71 – 777Combined sources
Beta strandi85 – 873Combined sources
Helixi89 – 9810Combined sources
Helixi104 – 11714Combined sources
Helixi122 – 1309Combined sources
Helixi137 – 14711Combined sources
Helixi148 – 1514Combined sources
Helixi153 – 1597Combined sources
Helixi164 – 1663Combined sources
Helixi167 – 19428Combined sources
Turni195 – 1973Combined sources
Helixi209 – 2179Combined sources
Helixi222 – 23413Combined sources
Beta strandi240 – 2423Combined sources
Helixi243 – 25210Combined sources
Turni253 – 2553Combined sources
Helixi258 – 26912Combined sources
Turni272 – 2765Combined sources
Helixi277 – 29115Combined sources
Helixi298 – 31013Combined sources
Helixi328 – 34013Combined sources
Helixi345 – 36420Combined sources
Helixi375 – 38410Combined sources
Helixi390 – 3923Combined sources
Helixi393 – 41422Combined sources
Beta strandi423 – 4253Combined sources
Helixi427 – 4337Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AL6X-ray1.85A1-433[»]
1AMZX-ray1.80A3-433[»]
1CSCX-ray1.70A1-433[»]
1CSHX-ray1.65A3-433[»]
1CSIX-ray1.70A3-433[»]
1CSRX-ray1.70A3-433[»]
1CSSX-ray1.70A3-433[»]
2CSCX-ray1.70A1-433[»]
3CSCX-ray1.90A1-433[»]
4CSCX-ray1.90A1-433[»]
5CSCX-ray2.80A/B1-433[»]
5CTSX-ray1.90A1-433[»]
6CSCX-ray2.25A/B1-433[»]
6CTSX-ray2.50A1-433[»]
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP23007.

Family & Domainsi

Sequence similaritiesi

Belongs to the citrate synthase family.Curated

Phylogenomic databases

HOVERGENiHBG005336.
InParanoidiP23007.
PhylomeDBiP23007.

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.

P23007-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
ASSTNLKDVL AALIPKEQAR IKTFRQQHGG TALGQITVDM SYGGMRGMKG
60 70 80 90 100
LVYETSVLDP DEGIRFRGFS IPECQKLLPK GGXGGEPLPE GLFWLLVTGQ
110 120 130 140 150
IPTGAQVSWL SKEWAKRAAL PSHVVTMLDN FPTNLHPMSQ LSAAITALNS
160 170 180 190 200
ESNFARAYAE GILRTKYWEM VYESAMDLIA KLPCVAAKIY RNLYRAGSSI
210 220 230 240 250
GAIDSKLDWS HNFTNMLGYT DAQFTELMRL YLTIHSDHEG GNVSAHTSHL
260 270 280 290 300
VGSALSDPYL SFAAAMNGLA GPLHGLANQE VLGWLAQLQK AXXXAGADAS
310 320 330 340 350
LRDYIWNTLN SGRVVPGYGH AVLRKTDPRY TCQREFALKH LPGDPMFKLV
360 370 380 390 400
AQLYKIVPNV LLEQGAAANP WPNVDAHSGV LLQYYGMTEM NYYTVLFGVS
410 420 430
RALGVLAQLI WSRALGFPLE RPKSMSTDGL IAL
Length:433
Mass (Da):47,378
Last modified:August 1, 1991 - v1
Checksum:i6942294BA95A9E06
GO

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AL6X-ray1.85A1-433[»]
1AMZX-ray1.80A3-433[»]
1CSCX-ray1.70A1-433[»]
1CSHX-ray1.65A3-433[»]
1CSIX-ray1.70A3-433[»]
1CSRX-ray1.70A3-433[»]
1CSSX-ray1.70A3-433[»]
2CSCX-ray1.70A1-433[»]
3CSCX-ray1.90A1-433[»]
4CSCX-ray1.90A1-433[»]
5CSCX-ray2.80A/B1-433[»]
5CTSX-ray1.90A1-433[»]
6CSCX-ray2.25A/B1-433[»]
6CTSX-ray2.50A1-433[»]
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP23007.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG005336.
InParanoidiP23007.
PhylomeDBiP23007.

Enzyme and pathway databases

UniPathwayiUPA00223; UER00717.
ReactomeiREACT_115536. The tricarboxylic acid cycle.

Miscellaneous databases

EvolutionaryTraceiP23007.

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. "Proposed mechanism for the condensation reaction of citrate synthase: 1.9-A structure of the ternary complex with oxaloacetate and carboxymethyl coenzyme A."
    Karpusas M., Branchaud B., Remington S.J.
    Biochemistry 29:2213-2219(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), CATALYTIC ACTIVITY.
    Tissue: Heart muscle.
  2. "Crystal structure of an open conformation of citrate synthase from chicken heart at 2.8-A resolution."
    Liao D.-I., Karpusas M., Remington S.J.
    Biochemistry 30:6031-6036(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF OPEN CONFORMATION.

Entry informationi

Entry nameiCISY_CHICK
AccessioniPrimary (citable) accession number: P23007
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: August 1, 1991
Last modified: May 27, 2015
This is version 106 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.

Caution

This is an X-ray determined sequence which was established using the sequence of pig citrate synthase and modifying it based on the observed electron density.Curated

Keywords - Technical termi

3D-structure, Complete proteome, 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.