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P80148

- CISY_SULSO

UniProt

P80148 - CISY_SULSO

Protein

Citrate synthase

Gene

gltA

Organism
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 107 (01 Oct 2014)
      Sequence version 3 (01 Jun 2001)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    Acetyl-CoA + H2O + oxaloacetate = citrate + CoA.PROSITE-ProRule annotation

    Enzyme regulationi

    Allosterically inhibited by NADH.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei258 – 2581PROSITE-ProRule annotation
    Active sitei313 – 3131PROSITE-ProRule annotation

    GO - Molecular functioni

    1. transferase activity, transferring acyl groups, acyl groups converted into alkyl on transfer Source: InterPro

    GO - Biological processi

    1. cellular carbohydrate metabolic process Source: InterPro
    2. tricarboxylic acid cycle Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    Tricarboxylic acid cycle

    Enzyme and pathway databases

    BioCyciSSOL273057:GCH2-2399-MONOMER.
    UniPathwayiUPA00223; UER00717.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Citrate synthase (EC:2.3.3.16)
    Gene namesi
    Name:gltA
    Ordered Locus Names:SSO2589
    OrganismiSulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
    Taxonomic identifieri273057 [NCBI]
    Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeSulfolobus
    ProteomesiUP000001974: Chromosome

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: InterPro

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 377377Citrate synthasePRO_0000169977Add
    BLAST

    Post-translational modificationi

    The N-terminus is blocked by acetylation.1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PRIDEiP80148.

    Interactioni

    Subunit structurei

    Homodimer.

    Protein-protein interaction databases

    STRINGi273057.SSO2589.

    Structurei

    Secondary structure

    1
    377
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi6 – 83
    Beta strandi12 – 2211
    Turni23 – 264
    Beta strandi27 – 304
    Helixi35 – 417
    Helixi44 – 5310
    Helixi59 – 7012
    Helixi77 – 859
    Helixi92 – 10615
    Beta strandi112 – 1154
    Helixi116 – 13823
    Helixi152 – 16110
    Helixi167 – 18014
    Helixi187 – 19711
    Helixi202 – 21312
    Turni216 – 2205
    Helixi221 – 23212
    Helixi235 – 2373
    Helixi238 – 2458
    Turni246 – 2494
    Helixi266 – 27914
    Helixi283 – 30321
    Turni304 – 3074
    Turni312 – 3154
    Helixi316 – 3238
    Helixi327 – 3293
    Helixi330 – 35223
    Beta strandi360 – 3634

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1O7XX-ray2.70A/B/C/D1-377[»]
    ProteinModelPortaliP80148.
    SMRiP80148. Positions 3-372.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP80148.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the citrate synthase family.Curated

    Phylogenomic databases

    eggNOGiCOG0372.
    HOGENOMiHOG000021225.
    KOiK01647.
    OMAiIDHEANA.

    Family and domain databases

    Gene3Di1.10.230.10. 1 hit.
    1.10.580.10. 1 hit.
    InterProiIPR011278. 2-MeCitrate/Citrate_synth_II.
    IPR016142. Citrate_synth-like_lrg_a-sub.
    IPR016143. Citrate_synth-like_sm_a-sub.
    IPR002020. Citrate_synthase-like.
    IPR016141. Citrate_synthase-like_core.
    IPR019810. Citrate_synthase_AS.
    IPR024176. Citrate_synthase_bac-typ.
    [Graphical view]
    PANTHERiPTHR11739. PTHR11739. 1 hit.
    PfamiPF00285. Citrate_synt. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001369. Citrate_synth. 1 hit.
    PRINTSiPR00143. CITRTSNTHASE.
    SUPFAMiSSF48256. SSF48256. 1 hit.
    TIGRFAMsiTIGR01800. cit_synth_II. 1 hit.
    PROSITEiPS00480. CITRATE_SYNTHASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P80148-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSVVSKGLEN VIIKVTNLTF IDGEKGILRY RGYNIEDLVN YGSYEETIYL    50
    MLYGKLPTKK ELNDLKAKLN EEYEVPQEVL DTIYLMPKEA DAIGLLEVGT 100
    AALASIDKNF KWKENDKEKA ISIIAKMATL VANVYRRKEG NKPRIPEPSD 150
    SFAKSFLLAS FAREPTTDEI NAMDKALILY TDHEVPASTT AALVAASTLS 200
    DMYSSLTAAL AALKGPLHGG AAEEAFKQFI EIGDPNRVQN WFNDKVVNQK 250
    NRLMGFGHRV YKTYDPRAKI FKKLALTLIE RNADARRYFE IAQKLEELGI 300
    KQFSSKGIYP NTDFYSGIVF YALGFPVYMF TALFALSRTL GWLAHIIEYV 350
    EEQHRLIRPR ALYVGPEYQE YVSIDKR 377
    Length:377
    Mass (Da):42,752
    Last modified:June 1, 2001 - v3
    Checksum:iE3036E232F134F11
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti10 – 101N → D AA sequence (PubMed:1521537)Curated
    Sequence conflicti12 – 121I → Y AA sequence (PubMed:1521537)Curated
    Sequence conflicti15 – 151V → S AA sequence (PubMed:1521537)Curated
    Sequence conflicti17 – 171N → S AA sequence (PubMed:1521537)Curated
    Sequence conflicti20 – 201F → Y AA sequence (PubMed:1521537)Curated
    Sequence conflicti24 – 252EK → VN AA sequence (PubMed:1521537)Curated
    Sequence conflicti27 – 271I → V AA sequence (PubMed:1521537)Curated
    Sequence conflicti57 – 571P → R in AAB09594. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U70879 Genomic DNA. Translation: AAB09594.1.
    AE006641 Genomic DNA. Translation: AAK42713.1.
    PIRiB90432.
    RefSeqiNP_343923.1. NC_002754.1.
    WP_009989299.1. NC_002754.1.

    Genome annotation databases

    EnsemblBacteriaiAAK42713; AAK42713; SSO2589.
    GeneIDi1454040.
    KEGGisso:SSO2589.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U70879 Genomic DNA. Translation: AAB09594.1 .
    AE006641 Genomic DNA. Translation: AAK42713.1 .
    PIRi B90432.
    RefSeqi NP_343923.1. NC_002754.1.
    WP_009989299.1. NC_002754.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1O7X X-ray 2.70 A/B/C/D 1-377 [» ]
    ProteinModelPortali P80148.
    SMRi P80148. Positions 3-372.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 273057.SSO2589.

    Proteomic databases

    PRIDEi P80148.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAK42713 ; AAK42713 ; SSO2589 .
    GeneIDi 1454040.
    KEGGi sso:SSO2589.

    Phylogenomic databases

    eggNOGi COG0372.
    HOGENOMi HOG000021225.
    KOi K01647.
    OMAi IDHEANA.

    Enzyme and pathway databases

    UniPathwayi UPA00223 ; UER00717 .
    BioCyci SSOL273057:GCH2-2399-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P80148.

    Family and domain databases

    Gene3Di 1.10.230.10. 1 hit.
    1.10.580.10. 1 hit.
    InterProi IPR011278. 2-MeCitrate/Citrate_synth_II.
    IPR016142. Citrate_synth-like_lrg_a-sub.
    IPR016143. Citrate_synth-like_sm_a-sub.
    IPR002020. Citrate_synthase-like.
    IPR016141. Citrate_synthase-like_core.
    IPR019810. Citrate_synthase_AS.
    IPR024176. Citrate_synthase_bac-typ.
    [Graphical view ]
    PANTHERi PTHR11739. PTHR11739. 1 hit.
    Pfami PF00285. Citrate_synt. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001369. Citrate_synth. 1 hit.
    PRINTSi PR00143. CITRTSNTHASE.
    SUPFAMi SSF48256. SSF48256. 1 hit.
    TIGRFAMsi TIGR01800. cit_synth_II. 1 hit.
    PROSITEi PS00480. CITRATE_SYNTHASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Sulfolobus solfataricus citrate synthase."
      Connaris H., Danson M.J., Hough D.W.
      Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 35091 / DSM 1616 / IFO 15331 / JCM 8930 / P1.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 35092 / DSM 1617 / JCM 11322 / P2.
    3. "Conversion, by limited proteolysis, of an archaebacterial citrate synthase into essentially a citryl-CoA hydrolase."
      Lill U., Lefrank S., Henschen A., Eggerer H.
      Eur. J. Biochem. 208:459-466(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 7-30, ACETYLATION.

    Entry informationi

    Entry nameiCISY_SULSO
    AccessioniPrimary (citable) accession number: P80148
    Secondary accession number(s): P77979
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 1992
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 107 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Citrate synthase is found in nearly all cells capable of oxidative metabolism.

    Keywords - Technical termi

    3D-structure, Allosteric enzyme, 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