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Protein

D-glycerate 2-kinase

Gene

TM_1585

Organism
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the degradation of serine via 3-hydroxypyruvate. Catalyzes the ATP-dependent phosphorylation of D-glycerate to 2-phosphoglycerate.1 Publication

Catalytic activityi

ATP + D-glycerate = ADP + 2-phospho-D-glycerate.1 Publication

Cofactori

Mg2+1 Publication

Kineticsi

Kcat is 14.4 sec(-1) for phosphorylation of D-glycerate.

  1. KM=0.095 mM for ATP1 Publication
  2. KM=0.15 mM for D-glycerate1 Publication

    GO - Molecular functioni

    • ATP binding Source: UniProtKB-KW
    • glycerate kinase activity Source: GO_Central
    • magnesium ion binding Source: UniProtKB
    • phosphotransferase activity, alcohol group as acceptor Source: UniProtKB

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    SABIO-RKQ9X1S1.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    D-glycerate 2-kinase (EC:2.7.1.165)
    Short name:
    GCK
    Gene namesi
    Ordered Locus Names:TM_1585
    ORF Names:THEMA_06355, Tmari_1593
    OrganismiThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
    Taxonomic identifieri243274 [NCBI]
    Taxonomic lineageiBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga
    Proteomesi
    • UP000013901 Componenti: Chromosome
    • UP000008183 Componenti: Chromosome

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi47K → A: Very low residual kinase activity. 1 Publication1
    Mutagenesisi47K → R: Significant decrease of the kinase activity with a 180-fold decrease of catalytic efficiency. 1 Publication1
    Mutagenesisi325R → A or K: Significant decrease of the kinase activity with a 17-fold decrease of catalytic efficiency. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00004289941 – 417D-glycerate 2-kinaseAdd BLAST417

    Interactioni

    Subunit structurei

    Homodimer.2 Publications

    Protein-protein interaction databases

    STRINGi243274.TM1585.

    Structurei

    Secondary structure

    1417
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi5 – 20Combined sources16
    Helixi24 – 29Combined sources6
    Helixi32 – 35Combined sources4
    Beta strandi39 – 46Combined sources8
    Helixi49 – 60Combined sources12
    Helixi61 – 63Combined sources3
    Beta strandi64 – 72Combined sources9
    Beta strandi84 – 88Combined sources5
    Beta strandi90 – 92Combined sources3
    Helixi95 – 108Combined sources14
    Beta strandi116 – 121Combined sources6
    Helixi125 – 128Combined sources4
    Helixi138 – 150Combined sources13
    Helixi155 – 163Combined sources9
    Beta strandi166 – 168Combined sources3
    Turni169 – 171Combined sources3
    Helixi172 – 177Combined sources6
    Beta strandi180 – 187Combined sources8
    Turni195 – 197Combined sources3
    Helixi198 – 200Combined sources3
    Helixi210 – 219Combined sources10
    Helixi226 – 232Combined sources7
    Beta strandi241 – 249Combined sources9
    Helixi251 – 264Combined sources14
    Beta strandi268 – 276Combined sources9
    Helixi280 – 297Combined sources18
    Beta strandi303 – 311Combined sources9
    Helixi325 – 336Combined sources12
    Turni337 – 339Combined sources3
    Beta strandi343 – 349Combined sources7
    Beta strandi355 – 358Combined sources4
    Beta strandi361 – 365Combined sources5
    Helixi368 – 374Combined sources7
    Helixi379 – 384Combined sources6
    Helixi388 – 394Combined sources7
    Beta strandi410 – 416Combined sources7

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2B8NX-ray2.53A/B1-417[»]
    ProteinModelPortaliQ9X1S1.
    SMRiQ9X1S1.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9X1S1.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycerate kinase type-1 family.Curated

    Phylogenomic databases

    eggNOGiENOG4105D1Z. Bacteria.
    COG2379. LUCA.
    InParanoidiQ9X1S1.
    KOiK11529.
    OMAiTHTNVND.
    OrthoDBiPOG091H0MJG.

    Family and domain databases

    Gene3Di3.40.1480.10. 1 hit.
    InterProiIPR007835. MOFRL.
    IPR025286. MOFRL_assoc_dom.
    [Graphical view]
    PfamiPF13660. DUF4147. 1 hit.
    PF05161. MOFRL. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9X1S1-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MFDPESLKKL AIEIVKKSIE AVFPDRAVKE TLPKLNLDRV ILVAVGKAAW
    60 70 80 90 100
    RMAKAAYEVL GKKIRKGVVV TKYGHSEGPI DDFEIYEAGH PVPDENTIKT
    110 120 130 140 150
    TRRVLELVDQ LNENDTVLFL LSGGGSSLFE LPLEGVSLEE IQKLTSALLK
    160 170 180 190 200
    SGASIEEINT VRKHLSQVKG GRFAERVFPA KVVALVLSDV LGDRLDVIAS
    210 220 230 240 250
    GPAWPDSSTS EDALKVLEKY GIETSESVKR AILQETPKHL SNVEIHLIGN
    260 270 280 290 300
    VQKVCDEAKS LAKEKGFNAE IITTSLDCEA REAGRFIASI MKEVKFKDRP
    310 320 330 340 350
    LKKPAALIFG GETVVHVKGN GIGGRNQELA LSAAIALEGI EGVILCSAGT
    360 370 380 390 400
    DGTDGPTDAA GGIVDGSTAK TLKAMGEDPY QYLKNNDSYN ALKKSGALLI
    410
    TGPTGTNVND LIIGLIV
    Length:417
    Mass (Da):44,722
    Last modified:November 1, 1999 - v1
    Checksum:iFEE01EC89CC8E445
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE000512 Genomic DNA. Translation: AAD36652.1.
    CP004077 Genomic DNA. Translation: AGL50517.1.
    CP007013 Genomic DNA. Translation: AHD18518.1.
    PIRiA72236.
    RefSeqiNP_229385.1. NC_000853.1.
    WP_004082016.1. NZ_CP011107.1.

    Genome annotation databases

    EnsemblBacteriaiAAD36652; AAD36652; TM_1585.
    AGL50517; AGL50517; Tmari_1593.
    AHD18518; AHD18518; THEMA_06355.
    GeneIDi897953.
    KEGGitma:TM1585.
    tmi:THEMA_06355.
    tmm:Tmari_1593.
    tmw:THMA_1620.
    PATRICi23938134. VBITheMar51294_1604.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE000512 Genomic DNA. Translation: AAD36652.1.
    CP004077 Genomic DNA. Translation: AGL50517.1.
    CP007013 Genomic DNA. Translation: AHD18518.1.
    PIRiA72236.
    RefSeqiNP_229385.1. NC_000853.1.
    WP_004082016.1. NZ_CP011107.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2B8NX-ray2.53A/B1-417[»]
    ProteinModelPortaliQ9X1S1.
    SMRiQ9X1S1.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi243274.TM1585.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAD36652; AAD36652; TM_1585.
    AGL50517; AGL50517; Tmari_1593.
    AHD18518; AHD18518; THEMA_06355.
    GeneIDi897953.
    KEGGitma:TM1585.
    tmi:THEMA_06355.
    tmm:Tmari_1593.
    tmw:THMA_1620.
    PATRICi23938134. VBITheMar51294_1604.

    Phylogenomic databases

    eggNOGiENOG4105D1Z. Bacteria.
    COG2379. LUCA.
    InParanoidiQ9X1S1.
    KOiK11529.
    OMAiTHTNVND.
    OrthoDBiPOG091H0MJG.

    Enzyme and pathway databases

    SABIO-RKQ9X1S1.

    Miscellaneous databases

    EvolutionaryTraceiQ9X1S1.

    Family and domain databases

    Gene3Di3.40.1480.10. 1 hit.
    InterProiIPR007835. MOFRL.
    IPR025286. MOFRL_assoc_dom.
    [Graphical view]
    PfamiPF13660. DUF4147. 1 hit.
    PF05161. MOFRL. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiGCK_THEMA
    AccessioniPrimary (citable) accession number: Q9X1S1
    Secondary accession number(s): G4FFX3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 14, 2014
    Last sequence update: November 1, 1999
    Last modified: November 2, 2016
    This is version 95 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.