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Protein

2,3-bisphosphoglycerate-independent phosphoglycerate mutase

Gene

gpmI

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).1 Publication

Catalytic activityi

2-phospho-D-glycerate = 3-phospho-D-glycerate.1 Publication

Cofactori

Mn2+1 PublicationNote: Binds 2 manganese ions per subunit.1 Publication

Enzyme regulationi

Insensitive to vanadate.1 Publication

Kineticsi

Kcat is 22 sec(-1) for mutase with 3-PGA as substrate (at pH 7 and 30 degrees Celsius). Kcat is 10 sec(-1) for mutase with 2-PGA as substrate (at pH 7 and 30 degrees Celsius).1 Publication

  1. KM=210 µM for 3-PGA (at pH 7 and 30 degrees Celsius).1 Publication
  2. KM=97 µM for 2-PGA (at pH 7 and 30 degrees Celsius).1 Publication

    Pathway:iglycolysis

    This protein is involved in step 3 of the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate.Curated
    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)
    3. Probable phosphoglycerate mutase GpmB (gpmB), 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA), 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (gpmI)
    4. Enolase (eno)
    5. Pyruvate kinase I (pykF), 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
    Metal bindingi14 – 141Manganese 2UniRule annotation
    Active sitei64 – 641Phosphoserine intermediateUniRule annotation
    Metal bindingi64 – 641Manganese 2UniRule annotation
    Binding sitei125 – 1251SubstrateUniRule annotation
    Binding sitei187 – 1871SubstrateUniRule annotation
    Binding sitei193 – 1931SubstrateUniRule annotation
    Binding sitei336 – 3361SubstrateUniRule annotation
    Metal bindingi403 – 4031Manganese 1UniRule annotation
    Metal bindingi407 – 4071Manganese 1UniRule annotation
    Metal bindingi444 – 4441Manganese 2UniRule annotation
    Metal bindingi445 – 4451Manganese 2UniRule annotation
    Metal bindingi463 – 4631Manganese 1UniRule annotation

    GO - Molecular functioni

    • 2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity Source: EcoCyc
    • manganese ion binding Source: EcoCyc

    GO - Biological processi

    • glucose catabolic process Source: InterPro
    • glycolytic process Source: UniProtKB-HAMAP
    • response to oxidative stress Source: EcoCyc
    Complete GO annotation...

    Keywords - Molecular functioni

    Isomerase

    Keywords - Biological processi

    Glycolysis

    Keywords - Ligandi

    Manganese, Metal-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:PGMI-MONOMER.
    ECOL316407:JW3587-MONOMER.
    MetaCyc:PGMI-MONOMER.
    SABIO-RKP37689.
    UniPathwayiUPA00109; UER00186.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    2,3-bisphosphoglycerate-independent phosphoglycerate mutase1 Publication (EC:5.4.2.121 Publication)
    Short name:
    BPG-independent PGAM1 Publication
    Short name:
    Phosphoglyceromutase1 Publication
    Short name:
    iPGM1 Publication
    Gene namesi
    Name:gpmIUniRule annotation
    Synonyms:pgmI, yibO
    Ordered Locus Names:b3612, JW3587
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG12296. gpmI.

    Subcellular locationi

    GO - Cellular componenti

    • cytoplasm Source: UniProtKB
    Complete GO annotation...

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 5145142,3-bisphosphoglycerate-independent phosphoglycerate mutasePRO_0000212145Add
    BLAST

    Proteomic databases

    PaxDbiP37689.
    PRIDEiP37689.

    2D gel databases

    SWISS-2DPAGEP37689.

    Expressioni

    Developmental stagei

    Expressed most strongly in early exponential growth, with levels falling off as cells reached late log phase and stationary phase.1 Publication

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Protein-protein interaction databases

    DIPiDIP-12425N.
    IntActiP37689. 4 interactions.
    STRINGi511145.b3612.

    Structurei

    3D structure databases

    ProteinModelPortaliP37689.
    SMRiP37689. Positions 5-504.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni155 – 1562Substrate bindingUniRule annotation
    Regioni263 – 2664Substrate bindingUniRule annotation

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0696.
    HOGENOMiHOG000223664.
    InParanoidiP37689.
    KOiK15633.
    OMAiLHIATMT.
    OrthoDBiEOG6HJ22X.
    PhylomeDBiP37689.

    Family and domain databases

    Gene3Di3.40.1450.10. 1 hit.
    3.40.720.10. 2 hits.
    HAMAPiMF_01038. GpmI.
    InterProiIPR017849. Alkaline_Pase-like_a/b/a.
    IPR017850. Alkaline_phosphatase_core.
    IPR011258. BPG-indep_PGM_N.
    IPR006124. Metalloenzyme.
    IPR005995. Pgm_bpd_ind.
    [Graphical view]
    PfamiPF06415. iPGM_N. 1 hit.
    PF01676. Metalloenzyme. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001492. IPGAM. 1 hit.
    SUPFAMiSSF53649. SSF53649. 2 hits.
    SSF64158. SSF64158. 1 hit.
    TIGRFAMsiTIGR01307. pgm_bpd_ind. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P37689-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MLVSKKPMVL VILDGYGYRE EQQDNAIFSA KTPVMDALWA NRPHTLIDAS
    60 70 80 90 100
    GLEVGLPDRQ MGNSEVGHVN LGAGRIVYQD LTRLDVEIKD RAFFANPVLT
    110 120 130 140 150
    GAVDKAKNAG KAVHIMGLLS AGGVHSHEDH IMAMVELAAE RGAEKIYLHA
    160 170 180 190 200
    FLDGRDTPPR SAESSLKKFE EKFAALGKGR VASIIGRYYA MDRDNRWDRV
    210 220 230 240 250
    EKAYDLLTLA QGEFQADTAV AGLQAAYARD ENDEFVKATV IRAEGQPDAA
    260 270 280 290 300
    MEDGDALIFM NFRADRAREI TRAFVNADFD GFARKKVVNV DFVMLTEYAA
    310 320 330 340 350
    DIKTAVAYPP ASLVNTFGEW MAKNDKTQLR ISETEKYAHV TFFFNGGVEE
    360 370 380 390 400
    SFKGEDRILI NSPKVATYDL QPEMSSAELT EKLVAAIKSG KYDTIICNYP
    410 420 430 440 450
    NGDMVGHTGV MEAAVKAVEA LDHCVEEVAK AVESVGGQLL ITADHGNAEQ
    460 470 480 490 500
    MRDPATGQAH TAHTNLPVPL IYVGDKNVKA VEGGKLSDIA PTMLSLMGME
    510
    IPQEMTGKPL FIVE
    Length:514
    Mass (Da):56,194
    Last modified:October 1, 1994 - v1
    Checksum:iBD4173C2BA2CEDD8
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U00039 Genomic DNA. Translation: AAB18589.1.
    U00096 Genomic DNA. Translation: AAC76636.1.
    AP009048 Genomic DNA. Translation: BAE77680.1.
    PIRiS47833.
    RefSeqiNP_418069.1. NC_000913.3.
    WP_001350558.1. NZ_CP010445.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76636; AAC76636; b3612.
    BAE77680; BAE77680; BAE77680.
    GeneIDi948130.
    KEGGieco:b3612.
    PATRICi32122711. VBIEscCol129921_3732.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U00039 Genomic DNA. Translation: AAB18589.1.
    U00096 Genomic DNA. Translation: AAC76636.1.
    AP009048 Genomic DNA. Translation: BAE77680.1.
    PIRiS47833.
    RefSeqiNP_418069.1. NC_000913.3.
    WP_001350558.1. NZ_CP010445.1.

    3D structure databases

    ProteinModelPortaliP37689.
    SMRiP37689. Positions 5-504.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    DIPiDIP-12425N.
    IntActiP37689. 4 interactions.
    STRINGi511145.b3612.

    2D gel databases

    SWISS-2DPAGEP37689.

    Proteomic databases

    PaxDbiP37689.
    PRIDEiP37689.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC76636; AAC76636; b3612.
    BAE77680; BAE77680; BAE77680.
    GeneIDi948130.
    KEGGieco:b3612.
    PATRICi32122711. VBIEscCol129921_3732.

    Organism-specific databases

    EchoBASEiEB2204.
    EcoGeneiEG12296. gpmI.

    Phylogenomic databases

    eggNOGiCOG0696.
    HOGENOMiHOG000223664.
    InParanoidiP37689.
    KOiK15633.
    OMAiLHIATMT.
    OrthoDBiEOG6HJ22X.
    PhylomeDBiP37689.

    Enzyme and pathway databases

    UniPathwayiUPA00109; UER00186.
    BioCyciEcoCyc:PGMI-MONOMER.
    ECOL316407:JW3587-MONOMER.
    MetaCyc:PGMI-MONOMER.
    SABIO-RKP37689.

    Miscellaneous databases

    PROiP37689.

    Family and domain databases

    Gene3Di3.40.1450.10. 1 hit.
    3.40.720.10. 2 hits.
    HAMAPiMF_01038. GpmI.
    InterProiIPR017849. Alkaline_Pase-like_a/b/a.
    IPR017850. Alkaline_phosphatase_core.
    IPR011258. BPG-indep_PGM_N.
    IPR006124. Metalloenzyme.
    IPR005995. Pgm_bpd_ind.
    [Graphical view]
    PfamiPF06415. iPGM_N. 1 hit.
    PF01676. Metalloenzyme. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001492. IPGAM. 1 hit.
    SUPFAMiSSF53649. SSF53649. 2 hits.
    SSF64158. SSF64158. 1 hit.
    TIGRFAMsiTIGR01307. pgm_bpd_ind. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Analysis of the Escherichia coli genome. V. DNA sequence of the region from 76.0 to 81.5 minutes."
      Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.
      Nucleic Acids Res. 22:2576-2586(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    3. "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.
    4. "Enrichment of low abundance proteins of Escherichia coli by hydroxyapatite chromatography."
      Fountoulakis M., Takacs M.-F., Berndt P., Langen H., Takacs B.
      Electrophoresis 20:2181-2195(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: B / BL21.
    5. "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, COFACTOR, ENZYME REGULATION, DEVELOPMENTAL STAGE, SUBUNIT.

    Entry informationi

    Entry nameiGPMI_ECOLI
    AccessioniPrimary (citable) accession number: P37689
    Secondary accession number(s): Q2M7S6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1994
    Last sequence update: October 1, 1994
    Last modified: July 22, 2015
    This is version 126 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Inhibition by vanadate is a diagnostic test for discrimination between the cofactor-dependent (GpmA) and -independent (GpmI) phosphoglycerate mutases.1 Publication

    Keywords - Technical termi

    Complete proteome, 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. 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.