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Q53554

- CISY_PYRFU

UniProt

Q53554 - CISY_PYRFU

Protein

Citrate synthase

Gene

gltA

Organism
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 106 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      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 sitei263 – 2631PROSITE-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

    UniPathwayiUPA00223; UER00717.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Citrate synthase (EC:2.3.3.16)
    Gene namesi
    Name:gltA
    Ordered Locus Names:PF0203
    OrganismiPyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
    Taxonomic identifieri186497 [NCBI]
    Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus
    ProteomesiUP000001013: Chromosome

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: InterPro

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed
    Chaini2 – 377376Citrate synthasePRO_0000169976Add
    BLAST

    Proteomic databases

    PRIDEiQ53554.

    Interactioni

    Subunit structurei

    Homodimer.

    Protein-protein interaction databases

    STRINGi186497.PF0203.

    Structurei

    Secondary structure

    1
    377
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi9 – 113
    Beta strandi15 – 2511
    Turni26 – 294
    Beta strandi30 – 334
    Helixi38 – 447
    Helixi47 – 5610
    Helixi62 – 7312
    Helixi80 – 889
    Helixi95 – 10915
    Turni111 – 1144
    Helixi119 – 14426
    Helixi158 – 16710
    Helixi173 – 18614
    Helixi193 – 20210
    Turni203 – 2053
    Helixi208 – 22013
    Turni222 – 2265
    Helixi227 – 23812
    Helixi241 – 2433
    Helixi244 – 25411
    Helixi271 – 28313
    Helixi286 – 30217
    Turni303 – 3075
    Turni312 – 3154
    Helixi316 – 3216
    Turni322 – 3243
    Helixi327 – 3293
    Helixi330 – 35021
    Beta strandi359 – 3624
    Helixi373 – 3753

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1AJ8X-ray1.90A/B7-377[»]
    ProteinModelPortaliQ53554.
    SMRiQ53554. Positions 7-377.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ53554.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the citrate synthase family.Curated

    Phylogenomic databases

    eggNOGiCOG0372.
    HOGENOMiHOG000021225.
    KOiK01647.
    OMAiKVANPYP.

    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.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q53554-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNTEKYLAKG LEDVYIDQTN ICYIDGKEGK LYYRGYSVEE LAELSTFEEV    50
    VYLLWWGKLP SLSELENFKK ELAKSRGLPK EVIEIMEALP KNTHPMGALR 100
    TIISYLGNID DSGDIPVTPE EVYRIGISVT AKIPTIVANW YRIKNGLEYV 150
    PPKEKLSHAA NFLYMLHGEE PPKEWEKAMD VALILYAEHE INASTLAVMT 200
    VGSTLSDYYS AILAGIGALK GPIHGGAVEE AIKQFMEIGS PEKVEEWFFK 250
    ALQQKRKIMG AGHRVYKTYD PRARIFKKYA SKLGDKKLFE IAERLERLVE 300
    EYLSKKGISI NVDYWSGLVF YGMKIPIELY TTIFAMGRIA GWTAHLAEYV 350
    SHNRIIRPRL QYVGEIGKKY LPIELRR 377
    Length:377
    Mass (Da):43,050
    Last modified:January 23, 2007 - v2
    Checksum:iA73E70EF123BE44B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S81109 Genomic DNA. Translation: AAB35835.2.
    AE009950 Genomic DNA. Translation: AAL80327.1.
    RefSeqiNP_577932.1. NC_003413.1.
    WP_011011316.1. NC_003413.1.

    Genome annotation databases

    EnsemblBacteriaiAAL80327; AAL80327; PF0203.
    GeneIDi1468035.
    KEGGipfu:PF0203.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S81109 Genomic DNA. Translation: AAB35835.2 .
    AE009950 Genomic DNA. Translation: AAL80327.1 .
    RefSeqi NP_577932.1. NC_003413.1.
    WP_011011316.1. NC_003413.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1AJ8 X-ray 1.90 A/B 7-377 [» ]
    ProteinModelPortali Q53554.
    SMRi Q53554. Positions 7-377.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 186497.PF0203.

    Proteomic databases

    PRIDEi Q53554.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAL80327 ; AAL80327 ; PF0203 .
    GeneIDi 1468035.
    KEGGi pfu:PF0203.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00223 ; UER00717 .

    Miscellaneous databases

    EvolutionaryTracei Q53554.

    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. "Citrate synthase from the hyperthermophilic Archaeon, Pyrococcus furiosus."
      Muir J.M., Russell R.J., Hough D.W., Danson M.J.
      Protein Eng. 8:583-592(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
    2. "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences."
      Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M., DiRuggiero J., Robb F.T.
      Genetics 152:1299-1305(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.
    3. "The crystal structure of citrate synthase from the hyperthermophilic archaeon Pyrococcus furiosus at 1.9-A resolution."
      Russell R.J., Ferguson J.M., Hough D.W., Danson M.J., Taylor G.L.
      Biochemistry 36:9983-9994(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).

    Entry informationi

    Entry nameiCISY_PYRFU
    AccessioniPrimary (citable) accession number: Q53554
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 106 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    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