Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P62707

- GPMA_ECOLI

UniProt

P62707 - GPMA_ECOLI

Protein

2,3-bisphosphoglycerate-dependent phosphoglycerate mutase

Gene

gpmA

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 101 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.

    Catalytic activityi

    2-phospho-D-glycerate = 3-phospho-D-glycerate.UniRule annotation

    Enzyme regulationi

    Strongly inhibited by vanadate.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei11 – 111Tele-phosphohistidine intermediate1 PublicationUniRule annotation
    Binding sitei17 – 1712-phospho-D-glycerateCurated
    Binding sitei62 – 6212-phospho-D-glycerateCurated
    Binding sitei100 – 10012-phospho-D-glycerateCurated
    Active sitei184 – 1841UniRule annotation
    Binding sitei186 – 18612-phospho-D-glycerateCurated

    GO - Molecular functioni

    1. 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity Source: EcoCyc

    GO - Biological processi

    1. glycolytic process Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Isomerase

    Keywords - Biological processi

    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 mutaseUniRule annotation (EC:5.4.2.11UniRule annotation)
    Short name:
    BPG-dependent PGAMUniRule annotation
    Short name:
    PGAMUniRule annotation
    Short name:
    PhosphoglyceromutaseUniRule annotation
    Short name:
    dPGMUniRule 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: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG11699. gpmA.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB

    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.

    Inductioni

    Regulated by the fur protein.1 Publication

    Gene expression databases

    GenevestigatoriP62707.

    Interactioni

    Subunit structurei

    Homodimer.1 PublicationUniRule annotation

    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 – 107
    Helixi15 – 184
    Helixi32 – 4716
    Beta strandi53 – 575
    Helixi61 – 7414
    Beta strandi81 – 833
    Helixi85 – 873
    Helixi93 – 953
    Helixi100 – 1078
    Helixi109 – 1179
    Helixi134 – 1363
    Helixi138 – 1403
    Turni145 – 1473
    Helixi154 – 16714
    Helixi169 – 1746
    Beta strandi179 – 1835
    Helixi185 – 19511
    Helixi200 – 2056
    Beta strandi214 – 2185
    Beta strandi224 – 2296
    Helixi233 – 2397

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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
    Regioni23 – 2422-phospho-D-glycerate bindingCurated
    Regioni89 – 9242-phospho-D-glycerate bindingCurated
    Regioni116 – 11722-phospho-D-glycerate bindingCurated

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0588.
    HOGENOMiHOG000221682.
    KOiK01834.
    OMAiKDDERFP.
    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

    MAVTKLVLVR HGESQWNKEN RFTGWYDVDL SEKGVSEAKA AGKLLKEEGY    50
    SFDFAYTSVL KRAIHTLWNV LDELDQAWLP VEKSWKLNER HYGALQGLNK 100
    AETAEKYGDE QVKQWRRGFA VTPPELTKDD ERYPGHDPRY AKLSEKELPL 150
    TESLALTIDR VIPYWNETIL PRMKSGERVI IAAHGNSLRA LVKYLDNMSE 200
    EEILELNIPT GVPLVYEFDE NFKPLKRYYL GNADEIAAKA AAVANQGKAK 250
    Length:250
    Mass (Da):28,556
    Last modified:January 23, 2007 - v2
    Checksum:iA6E0A49406F8482A
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.
    YP_489028.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC73842; AAC73842; b0755.
    BAA35417; BAA35417; BAA35417.
    GeneIDi12930679.
    945068.
    KEGGiecj:Y75_p0728.
    eco:b0755.
    PATRICi32116709. VBIEscCol129921_0780.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U00096 Genomic DNA. Translation: AAC73842.1 .
    AP009048 Genomic DNA. Translation: BAA35417.1 .
    J01591 Genomic DNA. No translation available.
    PIRi C64811.
    RefSeqi NP_415276.1. NC_000913.3.
    YP_489028.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1E58 X-ray 1.25 A 2-250 [» ]
    1E59 X-ray 1.30 A 2-250 [» ]
    ProteinModelPortali P62707.
    SMRi P62707. Positions 2-248.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-35899N.
    IntActi P62707. 15 interactions.
    MINTi MINT-1227975.
    STRINGi 511145.b0755.

    2D gel databases

    SWISS-2DPAGE P62707.

    Proteomic databases

    PaxDbi P62707.
    PRIDEi P62707.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC73842 ; AAC73842 ; b0755 .
    BAA35417 ; BAA35417 ; BAA35417 .
    GeneIDi 12930679.
    945068.
    KEGGi ecj:Y75_p0728.
    eco:b0755.
    PATRICi 32116709. VBIEscCol129921_0780.

    Organism-specific databases

    EchoBASEi EB1650.
    EcoGenei EG11699. gpmA.

    Phylogenomic databases

    eggNOGi COG0588.
    HOGENOMi HOG000221682.
    KOi K01834.
    OMAi KDDERFP.
    OrthoDBi EOG6C8N1H.
    PhylomeDBi P62707.

    Enzyme and pathway databases

    UniPathwayi UPA00109 ; UER00186 .
    BioCyci EcoCyc:GPMA-MONOMER.
    ECOL316407:JW0738-MONOMER.
    MetaCyc:GPMA-MONOMER.
    SABIO-RK P62707.

    Miscellaneous databases

    EvolutionaryTracei P62707.
    PROi P62707.

    Gene expression databases

    Genevestigatori P62707.

    Family and domain databases

    Gene3Di 3.40.50.1240. 1 hit.
    HAMAPi MF_01039. PGAM_GpmA.
    InterProi IPR013078. His_Pase_superF_clade-1.
    IPR029033. His_PPase_superfam.
    IPR001345. PG/BPGM_mutase_AS.
    IPR005952. Phosphogly_mut1.
    [Graphical view ]
    PANTHERi PTHR11931. PTHR11931. 1 hit.
    Pfami PF00300. His_Phos_1. 1 hit.
    [Graphical view ]
    SMARTi SM00855. PGAM. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53254. SSF53254. 1 hit.
    TIGRFAMsi TIGR01258. pgm_1. 1 hit.
    PROSITEi PS00175. PG_MUTASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: CHARACTERIZATION.
    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: TRANSCRIPTIONAL REGULATION.
    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), ACTIVE SITE.
      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.

    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: October 1, 2014
    This is version 101 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.

    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