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P23007

- CISY_CHICK

UniProt

P23007 - CISY_CHICK

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Protein

Citrate synthase, mitochondrial

Gene

CS

Organism
Gallus gallus (Chicken)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Catalytic activityi

Acetyl-CoA + H2O + oxaloacetate = citrate + CoA.1 PublicationPROSITE-ProRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei274 – 2741
Active sitei320 – 3201
Active sitei375 – 3751

GO - Molecular functioni

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

GO - Biological processi

  1. carbohydrate metabolic process Source: UniProtKB
  2. cellular carbohydrate metabolic process Source: InterPro
  3. small molecule metabolic process Source: Reactome
  4. tricarboxylic acid cycle Source: Reactome
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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
ProteomesiUP000000539: Unplaced

Subcellular locationi

GO - Cellular componenti

  1. mitochondrial matrix Source: UniProtKB
  2. mitochondrion Source: AgBase
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
Entry Method Resolution (Å) Chain Positions PDBsum
1AL6 X-ray 1.85 A 1-433 [» ]
1AMZ X-ray 1.80 A 3-433 [» ]
1CSC X-ray 1.70 A 1-433 [» ]
1CSH X-ray 1.65 A 3-433 [» ]
1CSI X-ray 1.70 A 3-433 [» ]
1CSR X-ray 1.70 A 3-433 [» ]
1CSS X-ray 1.70 A 3-433 [» ]
2CSC X-ray 1.70 A 1-433 [» ]
3CSC X-ray 1.90 A 1-433 [» ]
4CSC X-ray 1.90 A 1-433 [» ]
5CSC X-ray 2.80 A/B 1-433 [» ]
5CTS X-ray 1.90 A 1-433 [» ]
6CSC X-ray 2.25 A/B 1-433 [» ]
6CTS X-ray 2.50 A 1-433 [» ]
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi P23007.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

HOVERGENi HBG005336.
InParanoidi P23007.
PhylomeDBi P23007.

Enzyme and pathway databases

UniPathwayi UPA00223 ; UER00717 .
Reactomei REACT_115536. The tricarboxylic acid cycle.

Miscellaneous databases

EvolutionaryTracei P23007.

Family and domain databases

Gene3Di 1.10.580.10. 1 hit.
InterProi IPR016142. 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 ]
PANTHERi PTHR11739. PTHR11739. 1 hit.
Pfami PF00285. Citrate_synt. 1 hit.
[Graphical view ]
PRINTSi PR00143. CITRTSNTHASE.
SUPFAMi SSF48256. SSF48256. 1 hit.
TIGRFAMsi TIGR01793. cit_synth_euk. 1 hit.
PROSITEi PS00480. CITRATE_SYNTHASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: November 26, 2014
This is version 103 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