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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

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. 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)DescriptionActionsGraphical viewLength
Active sitei2741
Active sitei3201
Active sitei3751

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

ReactomeiR-GGA-372987. 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
Proteomesi
  • UP000000539 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001699831 – 433Citrate synthase, mitochondrialAdd BLAST433

Proteomic databases

PRIDEiP23007.

Interactioni

Subunit structurei

Homodimer.

Structurei

Secondary structure

1433
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi6 – 28Combined sources23
Beta strandi31 – 34Combined sources4
Helixi38 – 42Combined sources5
Turni43 – 47Combined sources5
Beta strandi49 – 52Combined sources4
Beta strandi55 – 59Combined sources5
Turni60 – 62Combined sources3
Beta strandi63 – 66Combined sources4
Helixi71 – 77Combined sources7
Beta strandi85 – 87Combined sources3
Helixi89 – 98Combined sources10
Helixi104 – 117Combined sources14
Helixi122 – 130Combined sources9
Helixi137 – 147Combined sources11
Helixi148 – 151Combined sources4
Helixi153 – 159Combined sources7
Helixi164 – 166Combined sources3
Helixi167 – 194Combined sources28
Turni195 – 197Combined sources3
Helixi209 – 217Combined sources9
Helixi222 – 234Combined sources13
Beta strandi240 – 242Combined sources3
Helixi243 – 252Combined sources10
Turni253 – 255Combined sources3
Helixi258 – 269Combined sources12
Turni272 – 276Combined sources5
Helixi277 – 291Combined sources15
Helixi298 – 310Combined sources13
Helixi328 – 340Combined sources13
Helixi345 – 364Combined sources20
Helixi375 – 384Combined sources10
Helixi390 – 392Combined sources3
Helixi393 – 414Combined sources22
Beta strandi423 – 425Combined sources3
Helixi427 – 433Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AL6X-ray1.85A1-80[»]
A82-433[»]
1AMZX-ray1.80A3-80[»]
A82-433[»]
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/B1-80[»]
A/B82-433[»]
6CTSX-ray2.50A1-433[»]
SMRiP23007.
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.
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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AL6X-ray1.85A1-80[»]
A82-433[»]
1AMZX-ray1.80A3-80[»]
A82-433[»]
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/B1-80[»]
A/B82-433[»]
6CTSX-ray2.50A1-433[»]
SMRiP23007.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP23007.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG005336.
InParanoidiP23007.
PhylomeDBiP23007.

Enzyme and pathway databases

UniPathwayiUPA00223; UER00717.
ReactomeiR-GGA-372987. 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.
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_CHICK
AccessioniPrimary (citable) accession number: P23007
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: August 1, 1991
Last modified: November 2, 2016
This is version 113 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

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.