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Protein

2,3-bisphosphoglycerate-dependent phosphoglycerate mutase

Gene

gpmA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the interconversion of 2-phosphoglycerate (2-PGA) and 3-phosphoglycerate (3-PGA).UniRule annotation1 Publication

Catalytic activityi

2-phospho-D-glycerate = 3-phospho-D-glycerate.UniRule annotation1 Publication

Enzyme regulationi

Strongly inhibited by vanadate.1 Publication

Kineticsi

Kcat is 330 sec(-1) for mutase with 3-PGA as substrate (at pH 7 and 30 degrees Celsius). Kcat is 220 sec(-1) for mutase with 2-PGA as substrate (at pH 7 and 30 degrees Celsius).1 Publication

  1. KM=190 µM for 2-PGA (at pH 7 and 30 degrees Celsius).1 Publication
  2. KM=200 µM for 3-PGA (at pH 7 and 30 degrees Celsius).1 Publication

    Pathway: glycolysis

    This protein is involved in step 3 of the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate.UniRule annotation
    Proteins known to be involved in the 5 steps of the subpathway in this organism are:
    1. Putative glyceraldehyde-3-phosphate dehydrogenase C (gapC), Glyceraldehyde-3-phosphate dehydrogenase A (gapA)
    2. Phosphoglycerate kinase (pgk), Phosphoglycerate kinase (pgk)
    3. Probable phosphoglycerate mutase GpmB (gpmB), 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA), 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (gpmM), 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA), 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (gpmI), Probable phosphoglycerate mutase GpmB (ytjC)
    4. Enolase (eno), Enolase (eno)
    5. Pyruvate kinase I (pykF), Pyruvate kinase (pykA), Pyruvate kinase II (pykA)
    This subpathway is part of the pathway glycolysis, which is itself part of Carbohydrate degradation.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate, the pathway glycolysis and in Carbohydrate degradation.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei11 – 111Tele-phosphohistidine intermediateUniRule annotation1 Publication
    Binding sitei62 – 621SubstrateUniRule annotation
    Binding sitei100 – 1001SubstrateUniRule annotation1 Publication
    Active sitei184 – 1841UniRule annotation1 Publication

    GO - Molecular functioni

    • 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity Source: EcoCyc

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Isomerase

    Keywords - Biological processi

    Gluconeogenesis, Glycolysis

    Enzyme and pathway databases

    BioCyciEcoCyc:GPMA-MONOMER.
    ECOL316407:JW0738-MONOMER.
    MetaCyc:GPMA-MONOMER.
    SABIO-RKP62707.
    UniPathwayiUPA00109; UER00186.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    2,3-bisphosphoglycerate-dependent phosphoglycerate mutase1 PublicationUniRule annotation (EC:5.4.2.11UniRule annotation1 Publication)
    Short name:
    BPG-dependent PGAM1 PublicationUniRule annotation
    Short name:
    PGAM1 PublicationUniRule annotation
    Short name:
    Phosphoglyceromutase1 PublicationUniRule annotation
    Short name:
    dPGM1 PublicationUniRule annotation
    Gene namesi
    Name:gpmAUniRule annotation
    Synonyms:gpm, pgm, pgmA
    Ordered Locus Names:b0755, JW0738
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG11699. gpmA.

    Subcellular locationi

    GO - Cellular componenti

    • cytoplasm Source: UniProtKB
    Complete GO annotation...

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed4 Publications
    Chaini2 – 2502492,3-bisphosphoglycerate-dependent phosphoglycerate mutasePRO_0000179873Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei18 – 181N6-acetyllysine1 Publication
    Modified residuei100 – 1001N6-acetyllysine1 Publication
    Modified residuei106 – 1061N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PaxDbiP62707.
    PRIDEiP62707.

    2D gel databases

    SWISS-2DPAGEP62707.

    Expressioni

    Developmental stagei

    Peak expression observed in mid to late log phase.1 Publication

    Inductioni

    Regulated by the fur protein.1 Publication

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation3 Publications

    Protein-protein interaction databases

    DIPiDIP-35899N.
    IntActiP62707. 15 interactions.
    MINTiMINT-1227975.
    STRINGi511145.b0755.

    Structurei

    Secondary structure

    1
    250
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 107Combined sources
    Helixi15 – 184Combined sources
    Helixi32 – 4716Combined sources
    Beta strandi53 – 575Combined sources
    Helixi61 – 7414Combined sources
    Beta strandi81 – 833Combined sources
    Helixi85 – 873Combined sources
    Helixi93 – 953Combined sources
    Helixi100 – 1078Combined sources
    Helixi109 – 1179Combined sources
    Helixi134 – 1363Combined sources
    Helixi138 – 1403Combined sources
    Turni145 – 1473Combined sources
    Helixi154 – 16714Combined sources
    Helixi169 – 1746Combined sources
    Beta strandi179 – 1835Combined sources
    Helixi185 – 19511Combined sources
    Helixi200 – 2056Combined sources
    Beta strandi214 – 2185Combined sources
    Beta strandi224 – 2296Combined sources
    Helixi233 – 2397Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1E58X-ray1.25A2-250[»]
    1E59X-ray1.30A2-250[»]
    ProteinModelPortaliP62707.
    SMRiP62707. Positions 2-248.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP62707.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni10 – 178Substrate bindingUniRule annotation1 Publication
    Regioni23 – 242Substrate bindingUniRule annotation2 Publications
    Regioni89 – 924Substrate bindingUniRule annotation1 Publication
    Regioni116 – 1172Substrate bindingUniRule annotation2 Publications
    Regioni185 – 1862Substrate bindingUniRule annotation1 Publication

    Sequence similaritiesi

    Belongs to the phosphoglycerate mutase family. BPG-dependent PGAM subfamily.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0588.
    HOGENOMiHOG000221682.
    InParanoidiP62707.
    KOiK01834.
    OMAiDRVLPYW.
    OrthoDBiEOG6C8N1H.
    PhylomeDBiP62707.

    Family and domain databases

    Gene3Di3.40.50.1240. 1 hit.
    HAMAPiMF_01039. PGAM_GpmA.
    InterProiIPR013078. His_Pase_superF_clade-1.
    IPR029033. His_PPase_superfam.
    IPR001345. PG/BPGM_mutase_AS.
    IPR005952. Phosphogly_mut1.
    [Graphical view]
    PANTHERiPTHR11931. PTHR11931. 1 hit.
    PfamiPF00300. His_Phos_1. 1 hit.
    [Graphical view]
    SMARTiSM00855. PGAM. 1 hit.
    [Graphical view]
    SUPFAMiSSF53254. SSF53254. 1 hit.
    TIGRFAMsiTIGR01258. pgm_1. 1 hit.
    PROSITEiPS00175. PG_MUTASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P62707-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MAVTKLVLVR HGESQWNKEN RFTGWYDVDL SEKGVSEAKA AGKLLKEEGY
    60 70 80 90 100
    SFDFAYTSVL KRAIHTLWNV LDELDQAWLP VEKSWKLNER HYGALQGLNK
    110 120 130 140 150
    AETAEKYGDE QVKQWRRGFA VTPPELTKDD ERYPGHDPRY AKLSEKELPL
    160 170 180 190 200
    TESLALTIDR VIPYWNETIL PRMKSGERVI IAAHGNSLRA LVKYLDNMSE
    210 220 230 240 250
    EEILELNIPT GVPLVYEFDE NFKPLKRYYL GNADEIAAKA AAVANQGKAK
    Length:250
    Mass (Da):28,556
    Last modified:January 23, 2007 - v2
    Checksum:iA6E0A49406F8482A
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U00096 Genomic DNA. Translation: AAC73842.1.
    AP009048 Genomic DNA. Translation: BAA35417.1.
    J01591 Genomic DNA. No translation available.
    PIRiC64811.
    RefSeqiNP_415276.1. NC_000913.3.

    Genome annotation databases

    EnsemblBacteriaiAAC73842; AAC73842; b0755.
    BAA35417; BAA35417; BAA35417.
    GeneIDi945068.
    KEGGiecj:Y75_p0728.
    eco:b0755.
    PATRICi32116709. VBIEscCol129921_0780.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U00096 Genomic DNA. Translation: AAC73842.1.
    AP009048 Genomic DNA. Translation: BAA35417.1.
    J01591 Genomic DNA. No translation available.
    PIRiC64811.
    RefSeqiNP_415276.1. NC_000913.3.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1E58X-ray1.25A2-250[»]
    1E59X-ray1.30A2-250[»]
    ProteinModelPortaliP62707.
    SMRiP62707. Positions 2-248.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    DIPiDIP-35899N.
    IntActiP62707. 15 interactions.
    MINTiMINT-1227975.
    STRINGi511145.b0755.

    2D gel databases

    SWISS-2DPAGEP62707.

    Proteomic databases

    PaxDbiP62707.
    PRIDEiP62707.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC73842; AAC73842; b0755.
    BAA35417; BAA35417; BAA35417.
    GeneIDi945068.
    KEGGiecj:Y75_p0728.
    eco:b0755.
    PATRICi32116709. VBIEscCol129921_0780.

    Organism-specific databases

    EchoBASEiEB1650.
    EcoGeneiEG11699. gpmA.

    Phylogenomic databases

    eggNOGiCOG0588.
    HOGENOMiHOG000221682.
    InParanoidiP62707.
    KOiK01834.
    OMAiDRVLPYW.
    OrthoDBiEOG6C8N1H.
    PhylomeDBiP62707.

    Enzyme and pathway databases

    UniPathwayiUPA00109; UER00186.
    BioCyciEcoCyc:GPMA-MONOMER.
    ECOL316407:JW0738-MONOMER.
    MetaCyc:GPMA-MONOMER.
    SABIO-RKP62707.

    Miscellaneous databases

    EvolutionaryTraceiP62707.
    PROiP62707.

    Family and domain databases

    Gene3Di3.40.50.1240. 1 hit.
    HAMAPiMF_01039. PGAM_GpmA.
    InterProiIPR013078. His_Pase_superF_clade-1.
    IPR029033. His_PPase_superfam.
    IPR001345. PG/BPGM_mutase_AS.
    IPR005952. Phosphogly_mut1.
    [Graphical view]
    PANTHERiPTHR11931. PTHR11931. 1 hit.
    PfamiPF00300. His_Phos_1. 1 hit.
    [Graphical view]
    SMARTiSM00855. PGAM. 1 hit.
    [Graphical view]
    SUPFAMiSSF53254. SSF53254. 1 hit.
    TIGRFAMsiTIGR01258. pgm_1. 1 hit.
    PROSITEiPS00175. PG_MUTASE. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. Bouffard G.G., Ogihara N., Rudd K.E., Adhya S.L.
      Unpublished observations (MAY-1993)
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    5. "The nucleotide sequence of aroG, the gene for 3-deoxy-D-arabinoheptulosonate-7-phosphate synthetase (phe) in Escherichia coli K12."
      Davies W.D., Davidson B.E.
      Nucleic Acids Res. 10:4045-4058(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: PRELIMINARY NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 122-250.
      Strain: K12.
    6. "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
      Link A.J., Robison K., Church G.M.
      Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-20.
      Strain: K12 / EMG2.
    7. Cited for: PROTEIN SEQUENCE OF 2-11.
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    8. "Bacterial defense against aging: role of the Escherichia coli ArcA regulator in gene expression, readjusted energy flux and survival during stasis."
      Nystroem T., Larsson C., Gustafsson L.
      EMBO J. 15:3219-3228(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-11.
    9. Cited for: PROTEIN SEQUENCE OF 2-5.
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    10. "Escherichia coli proteome analysis using the gene-protein database."
      VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
      Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY 2D-GEL.
    11. "The two analogous phosphoglycerate mutases of Escherichia coli."
      Fraser H.I., Kvaratskhelia M., White M.F.
      FEBS Lett. 455:344-348(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, DEVELOPMENTAL STAGE, SUBUNIT.
    12. "A method for direct cloning of fur-regulated genes: identification of seven new fur-regulated loci in Escherichia coli."
      Vassinova N., Kozyrev D.
      Microbiology 146:3171-3182(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    13. "Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli."
      Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y.
      Mol. Cell. Proteomics 8:215-225(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-18; LYS-100 AND LYS-106, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.
    14. "High resolution structure of the phosphohistidine-activated form of Escherichia coli cofactor-dependent phosphoglycerate mutase."
      Bond C.S., White M.F., Hunter W.N.
      J. Biol. Chem. 276:3247-3253(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG, ACTIVE SITE, SUBUNIT.
      Strain: K12.
    15. "Mechanistic implications for Escherichia coli cofactor-dependent phosphoglycerate mutase based on the high-resolution crystal structure of a vanadate complex."
      Bond C.S., White M.F., Hunter W.N.
      J. Mol. Biol. 316:1071-1081(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) IN COMPLEX WITH VANADATE, SUBUNIT.

    Entry informationi

    Entry nameiGPMA_ECOLI
    AccessioniPrimary (citable) accession number: P62707
    Secondary accession number(s): P31217
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 19, 2004
    Last sequence update: January 23, 2007
    Last modified: June 24, 2015
    This is version 105 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Has a 10-fold higher specific activity than BPG-independent phosphoglycerate mutase.1 Publication
    Inhibition by vanadate is a diagnostic test for discrimination between the cofactor-dependent (GpmA) and -independent (GpmI) phosphoglycerate mutases.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    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 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.