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P23007

- CISY_CHICK

UniProt

P23007 - CISY_CHICK

Protein

Citrate synthase, mitochondrial

Gene

CS

Organism
Gallus gallus (Chicken)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 101 (01 Oct 2014)
      Sequence version 1 (01 Aug 1991)
      Previous versions | rss
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    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

    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 groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus
    ProteomesiUP000000539: Unplaced

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrial matrix Source: UniProtKB
    2. mitochondrion Source: AgBase

    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 – 2823
    Beta strandi31 – 344
    Helixi38 – 425
    Turni43 – 475
    Beta strandi49 – 524
    Beta strandi55 – 595
    Turni60 – 623
    Beta strandi63 – 664
    Helixi71 – 777
    Beta strandi85 – 873
    Helixi89 – 9810
    Helixi104 – 11714
    Helixi122 – 1309
    Helixi137 – 14711
    Helixi148 – 1514
    Helixi153 – 1597
    Helixi164 – 1663
    Helixi167 – 19428
    Turni195 – 1973
    Helixi209 – 2179
    Helixi222 – 23413
    Beta strandi240 – 2423
    Helixi243 – 25210
    Turni253 – 2553
    Helixi258 – 26912
    Turni272 – 2765
    Helixi277 – 29115
    Helixi298 – 31013
    Helixi328 – 34013
    Helixi345 – 36420
    Helixi375 – 38410
    Helixi390 – 3923
    Helixi393 – 41422
    Beta strandi423 – 4253
    Helixi427 – 4337

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    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

    ASSTNLKDVL AALIPKEQAR IKTFRQQHGG TALGQITVDM SYGGMRGMKG    50
    LVYETSVLDP DEGIRFRGFS IPECQKLLPK GGXGGEPLPE GLFWLLVTGQ 100
    IPTGAQVSWL SKEWAKRAAL PSHVVTMLDN FPTNLHPMSQ LSAAITALNS 150
    ESNFARAYAE GILRTKYWEM VYESAMDLIA KLPCVAAKIY RNLYRAGSSI 200
    GAIDSKLDWS HNFTNMLGYT DAQFTELMRL YLTIHSDHEG GNVSAHTSHL 250
    VGSALSDPYL SFAAAMNGLA GPLHGLANQE VLGWLAQLQK AXXXAGADAS 300
    LRDYIWNTLN SGRVVPGYGH AVLRKTDPRY TCQREFALKH LPGDPMFKLV 350
    AQLYKIVPNV LLEQGAAANP WPNVDAHSGV LLQYYGMTEM NYYTVLFGVS 400
    RALGVLAQLI WSRALGFPLE RPKSMSTDGL IAL 433
    Length:433
    Mass (Da):47,378
    Last modified:August 1, 1991 - v1
    Checksum:i6942294BA95A9E06
    GO

    Cross-referencesi

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    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: October 1, 2014
    This is version 101 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