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P40924

- PGK_BACSU

UniProt

P40924 - PGK_BACSU

Protein

Phosphoglycerate kinase

Gene

pgk

Organism
Bacillus subtilis (strain 168)
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 3 (15 Jul 1998)
      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 – 2011ATPBy similarity
    Binding sitei323 – 3231ATPBy similarity

    Regions

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

    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

    BioCyciBSUB:BSU33930-MONOMER.
    UniPathwayiUPA00109; UER00185.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phosphoglycerate kinase (EC:2.7.2.3)
    Gene namesi
    Name:pgk
    Ordered Locus Names:BSU33930
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001570: Chromosome

    Organism-specific databases

    GenoListiBSU33930. [Micado]

    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_0000145905Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei183 – 1831Phosphoserine1 Publication
    Modified residuei299 – 2991Phosphothreonine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiP40924.
    PRIDEiP40924.

    PTM databases

    PhosSiteiP0802229.

    Interactioni

    Subunit structurei

    Monomer.By similarity

    Protein-protein interaction databases

    STRINGi224308.BSU33930.

    Structurei

    3D structure databases

    ProteinModelPortaliP40924.
    SMRiP40924. Positions 1-394.
    ModBaseiSearch...
    MobiDBiSearch...

    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

    Phylogenomic databases

    eggNOGiCOG0126.
    HOGENOMiHOG000227108.
    KOiK00927.
    OMAiWEALDIG.
    OrthoDBiEOG64N9Z0.
    PhylomeDBiP40924.

    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.

    P40924-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNKKTLKDID VKGKVVFCRV DFNVPMKDGE VTDDTRIRAA LPTIKHLADQ    50
    GAKVLLASHL GRPKGEVVEE LRLTPVAARL GELLGKEVKK ADEAYGDAVK 100
    AQISEMKDGD VLVLENVRFY PGEEKNDPEL AKAFAELADV YVNDAFGAAH 150
    RAHASTAGIA EHLPAVAGFL MEKELDVLGK AVSNPDRPFT AIIGGAKVKD 200
    KIGVIESLLD KVDNLIIGGG LAYTFVKALG YEVGKSLLEE DKIELAKSFM 250
    DRAKEKGVNF YMPEDVLVAD DFSNDANVKI VPISEIPSDL EAIDIGTKTR 300
    ETYADVIKNS KLVVWNGPMG VFEIDLFAQG TKAVAEALAE AKDTYSVIGG 350
    GDSAAAVEKF GLADKMSHIS TGGGASLEFM EGKELPGVAA LNDK 394
    Length:394
    Mass (Da):42,190
    Last modified:July 15, 1998 - v3
    Checksum:iC909AF1D76AF0F83
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti388 – 3881V → A in AAA21678. (PubMed:8021172)Curated
    Sequence conflicti393 – 3942DK → R in AAA21678. (PubMed:8021172)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL009126 Genomic DNA. Translation: CAB15398.1.
    L29475 Genomic DNA. Translation: AAA21678.1.
    PIRiC69675.
    RefSeqiNP_391273.1. NC_000964.3.

    Genome annotation databases

    EnsemblBacteriaiCAB15398; CAB15398; BSU33930.
    GeneIDi938572.
    KEGGibsu:BSU33930.
    PATRICi18978786. VBIBacSub10457_3556.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL009126 Genomic DNA. Translation: CAB15398.1 .
    L29475 Genomic DNA. Translation: AAA21678.1 .
    PIRi C69675.
    RefSeqi NP_391273.1. NC_000964.3.

    3D structure databases

    ProteinModelPortali P40924.
    SMRi P40924. Positions 1-394.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 224308.BSU33930.

    PTM databases

    PhosSitei P0802229.

    Proteomic databases

    PaxDbi P40924.
    PRIDEi P40924.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB15398 ; CAB15398 ; BSU33930 .
    GeneIDi 938572.
    KEGGi bsu:BSU33930.
    PATRICi 18978786. VBIBacSub10457_3556.

    Organism-specific databases

    GenoListi BSU33930. [Micado ]

    Phylogenomic databases

    eggNOGi COG0126.
    HOGENOMi HOG000227108.
    KOi K00927.
    OMAi WEALDIG.
    OrthoDBi EOG64N9Z0.
    PhylomeDBi P40924.

    Enzyme and pathway databases

    UniPathwayi UPA00109 ; UER00185 .
    BioCyci BSUB:BSU33930-MONOMER.

    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. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
      Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
      , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
      Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 168.
    2. "Identification of vegetative proteins for a two-dimensional protein index of Bacillus subtilis."
      Schmid R., Bernhardt J., Antelmann H., Voelker U., Mach H., Voelker A., Hecker M.
      Microbiology 143:991-998(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-23.
      Strain: 168 / IS58.
    3. "Cloning and nucleotide sequences of the genes encoding triose phosphate isomerase, phosphoglycerate mutase, and enolase from Bacillus subtilis."
      Leyva-Vazquez M.A., Setlow P.
      J. Bacteriol. 176:3903-3910(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 377-394.
      Strain: 168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB 3610 / VKM B-501.
    4. "The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis."
      Macek B., Mijakovic I., Olsen J.V., Gnad F., Kumar C., Jensen P.R., Mann M.
      Mol. Cell. Proteomics 6:697-707(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183 AND THR-299, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: 168.

    Entry informationi

    Entry nameiPGK_BACSU
    AccessioniPrimary (citable) accession number: P40924
    Secondary accession number(s): O32252
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: July 15, 1998
    Last modified: October 1, 2014
    This is version 106 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Bacillus subtilis
      Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3