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P18912

- PGK_GEOSE

UniProt

P18912 - PGK_GEOSE

Protein

Phosphoglycerate kinase

Gene

pgk

Organism
Geobacillus stearothermophilus (Bacillus stearothermophilus)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 89 (01 Oct 2014)
      Sequence version 2 (01 Aug 1992)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei36 – 361SubstrateBy similarity
    Binding sitei118 – 1181SubstrateBy similarity
    Binding sitei151 – 1511SubstrateBy similarity
    Binding sitei201 – 2011ATP
    Binding sitei316 – 3161ATP
    Binding sitei323 – 3231ATP

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi350 – 3534ATP

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. phosphoglycerate kinase activity Source: UniProtKB-HAMAP

    GO - Biological processi

    1. glycolytic process Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Biological processi

    Glycolysis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    SABIO-RKP18912.
    UniPathwayiUPA00109; UER00185.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phosphoglycerate kinase (EC:2.7.2.3)
    Gene namesi
    Name:pgk
    OrganismiGeobacillus stearothermophilus (Bacillus stearothermophilus)
    Taxonomic identifieri1422 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 394394Phosphoglycerate kinasePRO_0000145904Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei183 – 1831PhosphoserineBy similarity
    Modified residuei299 – 2991PhosphothreonineBy similarity

    Keywords - PTMi

    Phosphoprotein

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Structurei

    Secondary structure

    1
    394
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi6 – 83
    Beta strandi15 – 195
    Beta strandi30 – 323
    Helixi35 – 4915
    Beta strandi53 – 575
    Helixi69 – 713
    Helixi74 – 8411
    Beta strandi94 – 963
    Helixi97 – 1048
    Beta strandi111 – 1133
    Helixi117 – 1193
    Helixi122 – 1254
    Helixi128 – 1358
    Beta strandi139 – 1435
    Helixi146 – 1483
    Turni154 – 1574
    Helixi158 – 1614
    Beta strandi165 – 1673
    Helixi169 – 18315
    Beta strandi187 – 1937
    Helixi198 – 20811
    Turni209 – 2113
    Beta strandi213 – 2175
    Helixi221 – 2288
    Helixi240 – 2423
    Helixi243 – 25614
    Beta strandi259 – 2613
    Beta strandi264 – 27310
    Beta strandi278 – 2825
    Helixi283 – 2853
    Beta strandi291 – 2955
    Helixi297 – 30812
    Beta strandi311 – 3177
    Helixi325 – 3273
    Helixi329 – 34012
    Beta strandi345 – 3484
    Helixi351 – 3599
    Helixi363 – 3653
    Beta strandi366 – 3694
    Helixi374 – 3807
    Helixi386 – 3894

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1PHPX-ray1.65A1-394[»]
    ProteinModelPortaliP18912.
    SMRiP18912. Positions 1-394.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP18912.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni21 – 233Substrate bindingBy similarity
    Regioni59 – 624Substrate bindingBy similarity

    Sequence similaritiesi

    Belongs to the phosphoglycerate kinase family.Curated

    Family and domain databases

    Gene3Di3.40.50.1260. 1 hit.
    3.40.50.1270. 1 hit.
    HAMAPiMF_00145. Phosphoglyc_kinase.
    InterProiIPR001576. Phosphoglycerate_kinase.
    IPR015901. Phosphoglycerate_kinase_C.
    IPR015911. Phosphoglycerate_kinase_CS.
    IPR015824. Phosphoglycerate_kinase_N.
    [Graphical view]
    PANTHERiPTHR11406. PTHR11406. 1 hit.
    PfamiPF00162. PGK. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000724. Pgk. 1 hit.
    PRINTSiPR00477. PHGLYCKINASE.
    SUPFAMiSSF53748. SSF53748. 1 hit.
    PROSITEiPS00111. PGLYCERATE_KINASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P18912-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNKKTIRDVD VRGKRVFCRV DFNVPMEQGA ITDDTRIRAA LPTIRYLIEH    50
    GAKVILASHL GRPKGKVVEE LRLDAVAKRL GELLERPVAK TNEAVGDEVK 100
    AAVDRLNEGD VLLLENVRFY PGEEKNDPEL AKAFAELADL YVNDAFGAAH 150
    RAHASTEGIA HYLPAVAGFL MEKELEVLGK ALSNPDRPFT AIIGGAKVKD 200
    KIGVIDNLLE KVDNLIIGGG LAYTFVKALG HDVGKSLLEE DKIELAKSFM 250
    EKAKEKGVRF YMPVDVVVAD RFANDANTKV VPIDAIPADW SALDIGPKTR 300
    ELYRDVIRES KLVVWNGPMG VFEMDAFAHG TKAIAEALAE ALDTYSVIGG 350
    GDSAAAVEKF GLADKMDHIS TGGGASLEFM EGKQLPGVVA LEDK 394
    Length:394
    Mass (Da):42,730
    Last modified:August 1, 1992 - v2
    Checksum:i46BFA286F60E365A
    GO

    Sequence cautioni

    The sequence AAA22462.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X58059 Genomic DNA. Translation: CAA41093.1.
    M24493 Genomic DNA. Translation: AAA22462.1. Different initiation.
    PIRiJQ1399.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X58059 Genomic DNA. Translation: CAA41093.1 .
    M24493 Genomic DNA. Translation: AAA22462.1 . Different initiation.
    PIRi JQ1399.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1PHP X-ray 1.65 A 1-394 [» ]
    ProteinModelPortali P18912.
    SMRi P18912. Positions 1-394.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00109 ; UER00185 .
    SABIO-RK P18912.

    Miscellaneous databases

    EvolutionaryTracei P18912.

    Family and domain databases

    Gene3Di 3.40.50.1260. 1 hit.
    3.40.50.1270. 1 hit.
    HAMAPi MF_00145. Phosphoglyc_kinase.
    InterProi IPR001576. Phosphoglycerate_kinase.
    IPR015901. Phosphoglycerate_kinase_C.
    IPR015911. Phosphoglycerate_kinase_CS.
    IPR015824. Phosphoglycerate_kinase_N.
    [Graphical view ]
    PANTHERi PTHR11406. PTHR11406. 1 hit.
    Pfami PF00162. PGK. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000724. Pgk. 1 hit.
    PRINTSi PR00477. PHGLYCKINASE.
    SUPFAMi SSF53748. SSF53748. 1 hit.
    PROSITEi PS00111. PGLYCERATE_KINASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Sequence and expression of the gene encoding 3-phosphoglycerate kinase from Bacillus stearothermophilus."
      Davies G.J., Littlechild J.A., Watson H.C., Hall L.
      Gene 109:39-45(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Nucleotide sequence determination of the DNA region coding for Bacillus stearothermophilus glyceraldehyde-3-phosphate dehydrogenase and of the flanking DNA regions required for its expression in Escherichia coli."
      Branlant C., Oster T., Branlant G.
      Gene 75:145-155(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-126.
    3. "Purification, crystallization and preliminary X-ray analysis of the 3-phosphoglycerate kinase from Bacillus stearothermophilus."
      Davies G.J., Gamblin S.J., Littlechild J.A., Watson H.C.
      J. Mol. Biol. 227:1263-1264(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
    4. "Structure of the ADP complex of the 3-phosphoglycerate kinase from Bacillus stearothermophilus at 1.65 A."
      Davies G.J., Gamblin S.J., Littlechild J.A., Dauter Z., Wilson K.S., Watson H.C.
      Acta Crystallogr. D 50:202-209(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS).
    5. "Is the structure of the N-domain of phosphoglycerate kinase affected by isolation from the intact molecule?"
      Hosszu L.L.P., Craven C.J., Spencer J., Parker M.J., Clarke A.R., Kelly M., Waltho J.P.
      Biochemistry 36:333-340(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 1-174 IN COMPLEX WITH ADP.

    Entry informationi

    Entry nameiPGK_GEOSE
    AccessioniPrimary (citable) accession number: P18912
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1990
    Last sequence update: August 1, 1992
    Last modified: October 1, 2014
    This is version 89 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

    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