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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

Manual assertion based on experiment ini

  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

    Pathwayi: glycolysis

    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)DescriptionActionsGraphical viewLength
    Metal bindingi14Manganese 2UniRule annotation1
    Active sitei64Phosphoserine intermediateUniRule annotation1
    Metal bindingi64Manganese 2UniRule annotation1
    Binding sitei125SubstrateUniRule annotation1
    Binding sitei187SubstrateUniRule annotation1
    Binding sitei193SubstrateUniRule annotation1
    Binding sitei336SubstrateUniRule annotation1
    Metal bindingi403Manganese 1UniRule annotation1
    Metal bindingi407Manganese 1UniRule annotation1
    Metal bindingi444Manganese 2UniRule annotation1
    Metal bindingi445Manganese 2UniRule annotation1
    Metal bindingi463Manganese 1UniRule annotation1

    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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG12296. gpmI.

    Subcellular locationi

    GO - Cellular componenti

    • cytoplasm Source: UniProtKB
    • cytosol Source: EcoCyc
    Complete GO annotation...

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00002121451 – 5142,3-bisphosphoglycerate-independent phosphoglycerate mutaseAdd BLAST514

    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

    BioGridi4263294. 13 interactors.
    DIPiDIP-12425N.
    IntActiP37689. 4 interactors.
    STRINGi511145.b3612.

    Structurei

    3D structure databases

    ProteinModelPortaliP37689.
    SMRiP37689.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni155 – 156Substrate bindingUniRule annotation2
    Regioni263 – 266Substrate bindingUniRule annotation4

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiENOG4105CJI. Bacteria.
    COG0696. LUCA.
    HOGENOMiHOG000223664.
    InParanoidiP37689.
    KOiK15633.
    OMAiLHIATMT.
    PhylomeDBiP37689.

    Family and domain databases

    Gene3Di3.40.1450.10. 1 hit.
    3.40.720.10. 2 hits.
    HAMAPiMF_01038. GpmI. 1 hit.
    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_LN832404.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76636; AAC76636; b3612.
    BAE77680; BAE77680; BAE77680.
    GeneIDi948130.
    KEGGiecj:JW3587.
    eco: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_LN832404.1.

    3D structure databases

    ProteinModelPortaliP37689.
    SMRiP37689.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4263294. 13 interactors.
    DIPiDIP-12425N.
    IntActiP37689. 4 interactors.
    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.
    KEGGiecj:JW3587.
    eco:b3612.
    PATRICi32122711. VBIEscCol129921_3732.

    Organism-specific databases

    EchoBASEiEB2204.
    EcoGeneiEG12296. gpmI.

    Phylogenomic databases

    eggNOGiENOG4105CJI. Bacteria.
    COG0696. LUCA.
    HOGENOMiHOG000223664.
    InParanoidiP37689.
    KOiK15633.
    OMAiLHIATMT.
    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. 1 hit.
    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...

    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: November 2, 2016
    This is version 133 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

    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 one 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.