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P00889

- CISY_PIG

UniProt

P00889 - CISY_PIG

Protein

Citrate synthase, mitochondrial

Gene

CS

Organism
Sus scrofa (Pig)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 112 (01 Oct 2014)
      Sequence version 2 (01 Oct 1989)
      Previous versions | rss
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    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

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    Tricarboxylic acid cycle

    Enzyme and pathway databases

    ReactomeiREACT_217226. Citric acid cycle (TCA cycle).
    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

    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 – 5523
    Beta strandi59 – 646
    Helixi65 – 695
    Turni70 – 745
    Beta strandi76 – 794
    Beta strandi82 – 865
    Turni87 – 893
    Beta strandi90 – 934
    Helixi98 – 1047
    Beta strandi109 – 1113
    Beta strandi112 – 1143
    Helixi116 – 12510
    Helixi131 – 14313
    Helixi149 – 1579
    Beta strandi160 – 1623
    Helixi164 – 17411
    Helixi175 – 1784
    Helixi180 – 1867
    Helixi191 – 1933
    Helixi194 – 22128
    Beta strandi232 – 2343
    Helixi236 – 2449
    Helixi249 – 26113
    Turni266 – 2683
    Helixi270 – 28011
    Helixi285 – 29612
    Turni299 – 3013
    Helixi304 – 31916
    Helixi325 – 33612
    Turni337 – 3393
    Beta strandi345 – 3495
    Helixi355 – 36713
    Helixi372 – 39019
    Beta strandi394 – 3996
    Helixi401 – 4033
    Helixi405 – 4117
    Helixi417 – 4193
    Helixi420 – 44122
    Helixi454 – 46310

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    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

    MALLTAAARL FGAKNASCLV LAARHASASS TNLKDILADL IPKEQARIKT    50
    FRQQHGNTVV GQITVDMMYG GMRGMKGLVY ETSVLDPDEG IRFRGYSIPE 100
    CQKMLPKAKG GEEPLPEGLF WLLVTGQIPT EEQVSWLSKE WAKRAALPSH 150
    VVTMLDNFPT NLHPMSQLSA AITALNSESN FARAYAEGIH RTKYWELIYE 200
    DCMDLIAKLP CVAAKIYRNL YREGSSIGAI DSKLDWSHNF TNMLGYTDAQ 250
    FTELMRLYLT IHSDHEGGNV SAHTSHLVGS ALSDPYLSFA AAMNGLAGPL 300
    HGLANQEVLV WLTQLQKEVG KDVSDEKLRD YIWNTLNSGR VVPGYGHAVL 350
    RKTDPRYTCQ REFALKHLPH DPMFKLVAQL YKIVPNVLLE QGKAKNPWPN 400
    VDAHSGVLLQ YYGMTEMNYY TVLFGVSRAL GVLAQLIWSR ALGFPLERPK 450
    SMSTDGLIKL VDSK 464
    Length:464
    Mass (Da):51,629
    Last modified:October 1, 1989 - v2
    Checksum:i66719A7504DF322A
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M21197 mRNA. Translation: AAA31017.1 .
    PIRi A29966. YKPG.
    RefSeqi NP_999441.1. NM_214276.1.
    UniGenei Ssc.16315.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1CTS X-ray 2.70 A 28-464 [» ]
    2CTS X-ray 2.00 A 28-464 [» ]
    3ENJ X-ray 1.78 A 28-464 [» ]
    4CTS X-ray 2.90 A/B 28-464 [» ]
    ProteinModelPortali P00889.
    SMRi P00889. Positions 28-464.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 1149646. 2 interactions.
    STRINGi 9823.ENSSSCP00000000410.

    Proteomic databases

    PaxDbi P00889.
    PRIDEi P00889.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 397519.
    KEGGi ssc:397519.

    Organism-specific databases

    CTDi 1431.

    Phylogenomic databases

    eggNOGi COG0372.
    HOGENOMi HOG000130831.
    HOVERGENi HBG005336.
    KOi K01647.

    Enzyme and pathway databases

    UniPathwayi UPA00223 ; UER00717 .
    Reactomei REACT_217226. Citric acid cycle (TCA cycle).
    SABIO-RK P00889.

    Miscellaneous databases

    EvolutionaryTracei P00889.

    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. "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.
    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: October 1, 2014
    This is version 112 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