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Protein

2,3-bisphosphoglycerate-independent phosphoglycerate mutase

Gene

gpmI

Organism
Geobacillus stearothermophilus (Bacillus stearothermophilus)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Essential for rapid growth and for sporulation. Catalyzes the interconversion of 2-phosphoglycerate (2-PGA) and 3-phosphoglycerate (3-PGA).2 Publications

Catalytic activityi

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

Cofactori

Mn2+4 PublicationsNote: Binds 2 manganese ions per subunit.4 Publications

Enzyme regulationi

Could be inhibited during sporulation by acidification of the forespore, thus allowing accumulation of the spore's large depot of 3-phosphoglyceric acid.1 Publication

Kineticsi

  1. KM=4.4 mM for 3-pGA1 Publication

    pH dependencei

    Very sensitive to pH. The enzyme activity rises 25-fold between pH 6 and 8.1 Publication

    Temperature dependencei

    Addition of manganese increases the thermal stability.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. Glyceraldehyde-3-phosphate dehydrogenase (gap)
    2. Phosphoglycerate kinase (pgk), Phosphoglycerate kinase (pgk), Phosphoglycerate kinase (pgk), Phosphoglycerate kinase (pgk)
    3. 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (gpmI), 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (gpmI), 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (gpmI), 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (gpmI_1)
    4. Enolase (eno), Enolase (eno), Enolase (eno)
    5. Pyruvate kinase (pyk), Pyruvate kinase (AA904_05055), Pyruvate kinase (pyk), Pyruvate kinase (GT94_09925), Pyruvate kinase (B4114_2369)
    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 bindingi12Manganese 22 Publications1
    Active sitei62Phosphoserine intermediate3 Publications1
    Metal bindingi62Manganese 22 Publications1
    Binding sitei123Substrate3 Publications1
    Binding sitei185Substrate3 Publications1
    Binding sitei191Substrate2 Publications1
    Binding sitei336Substrate2 Publications1
    Metal bindingi403Manganese 13 Publications1
    Metal bindingi407Manganese 13 Publications1
    Metal bindingi444Manganese 22 Publications1
    Metal bindingi445Manganese 22 Publications1
    Metal bindingi462Manganese 13 Publications1

    GO - Molecular functioni

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

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Isomerase

    Keywords - Biological processi

    Glycolysis, Sporulation

    Keywords - Ligandi

    Manganese, Metal-binding

    Enzyme and pathway databases

    BRENDAi5.4.2.12. 623.
    UniPathwayiUPA00109; UER00186.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    2,3-bisphosphoglycerate-independent phosphoglycerate mutase1 Publication (EC:5.4.2.121 Publication)
    Short name:
    23PGA-independent1 Publication
    Short name:
    BPG-independent PGAM1 Publication
    Short name:
    Phosphoglyceromutase1 Publication
    Short name:
    iPGM1 Publication
    Gene namesi
    Name:gpmIUniRule annotation
    Synonyms:pgm
    OrganismiGeobacillus stearothermophilus (Bacillus stearothermophilus)
    Taxonomic identifieri1422 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi12D → N: Loss of mutase activity. 1 Publication1
    Mutagenesisi42H → N: Decrease in activity. 1 Publication1
    Mutagenesisi62S → A: Loss of mutase activity. 2 Publications1
    Mutagenesisi66H → N: Strong decrease in the mutase activity. 1 Publication1
    Mutagenesisi123H → N: Strong decrease in the mutase activity. 1 Publication1
    Mutagenesisi125H → N: Decrease in activity. 1 Publication1
    Mutagenesisi128H → N: 5-fold decrease in activity. 1 Publication1
    Mutagenesisi261R → L: Loss of mutase activity. 1 Publication1
    Mutagenesisi407H → N: Loss of mutase activity. 1 Publication1
    Mutagenesisi445H → N: 5-fold decrease in the mutase activity. 1 Publication1
    Mutagenesisi462H → N: Strong decrease in the mutase activity. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Initiator methionineiRemoved1 Publication
    ChainiPRO_00002121272 – 5112,3-bisphosphoglycerate-independent phosphoglycerate mutaseAdd BLAST510

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei36PhosphotyrosineUniRule annotation1

    Keywords - PTMi

    Phosphoprotein

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Structurei

    Secondary structure

    1511
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi6 – 11Combined sources6
    Helixi24 – 27Combined sources4
    Helixi31 – 39Combined sources9
    Beta strandi42 – 46Combined sources5
    Helixi49 – 52Combined sources4
    Helixi62 – 71Combined sources10
    Helixi78 – 87Combined sources10
    Helixi91 – 93Combined sources3
    Helixi95 – 107Combined sources13
    Beta strandi111 – 116Combined sources6
    Helixi126 – 138Combined sources13
    Beta strandi144 – 150Combined sources7
    Beta strandi152 – 155Combined sources4
    Helixi160 – 174Combined sources15
    Beta strandi178 – 184Combined sources7
    Helixi185 – 188Combined sources4
    Helixi195 – 207Combined sources13
    Beta strandi212 – 215Combined sources4
    Helixi216 – 225Combined sources10
    Helixi230 – 232Combined sources3
    Beta strandi236 – 239Combined sources4
    Beta strandi243 – 246Combined sources4
    Beta strandi254 – 257Combined sources4
    Turni263 – 265Combined sources3
    Helixi266 – 273Combined sources8
    Beta strandi291 – 296Combined sources6
    Beta strandi300 – 302Combined sources3
    Beta strandi304 – 308Combined sources5
    Helixi317 – 323Combined sources7
    Beta strandi328 – 333Combined sources6
    Helixi334 – 336Combined sources3
    Helixi337 – 340Combined sources4
    Turni341 – 346Combined sources6
    Beta strandi355 – 360Combined sources6
    Helixi368 – 370Combined sources3
    Turni372 – 375Combined sources4
    Helixi376 – 388Combined sources13
    Beta strandi393 – 399Combined sources7
    Helixi401 – 406Combined sources6
    Turni407 – 409Combined sources3
    Helixi411 – 434Combined sources24
    Beta strandi438 – 442Combined sources5
    Beta strandi444 – 447Combined sources4
    Beta strandi467 – 471Combined sources5
    Beta strandi480 – 483Combined sources4
    Helixi484 – 486Combined sources3
    Helixi487 – 495Combined sources9

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1EJJX-ray1.90A1-511[»]
    1EQJX-ray1.70A1-511[»]
    1O98X-ray1.40A1-511[»]
    1O99X-ray2.65A1-511[»]
    ProteinModelPortaliQ9X519.
    SMRiQ9X519.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9X519.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni153 – 154Substrate binding3 Publications2
    Regioni261 – 264Substrate binding3 Publications4

    Sequence similaritiesi

    Phylogenomic databases

    KOiK15633.

    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.

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

    Q9X519-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSKKPVALII LDGFALRDET YGNAVAQANK PNFDRYWNEY PHTTLKACGE
    60 70 80 90 100
    AVGLPEGQMG NSEVGHLNIG AGRIVYQSLT RINIAIREGE FDRNETFLAA
    110 120 130 140 150
    MNHVKQHGTS LHLFGLLSDG GVHSHIHHLY ALLRLAAKEG VKRVYIHGFL
    160 170 180 190 200
    DGRDVGPQTA PQYIKELQEK IKEYGVGEIA TLSGRYYSMD RDKRWDRVEK
    210 220 230 240 250
    AYRAMVYGEG PTYRDPLECI EDSYKHGIYD EFVLPSVIVR EDGRPVATIQ
    260 270 280 290 300
    DNDAIIFYNF RPDRAIQISN TFTNEDFREF DRGPKHPKHL FFVCLTHFSE
    310 320 330 340 350
    TVKGYVAFKP TNLDNTIGEV LSQHGLRQLR IAETEKYPHV TFFMSGGREE
    360 370 380 390 400
    KFPGEDRILI NSPKVPTYDL KPEMSAYEVT DALLKEIEAD KYDAIILNYA
    410 420 430 440 450
    NPDMVGHSGK LEPTIKAVEA VDECLGKVVD AILAKGGIAI ITADHGNADE
    460 470 480 490 500
    VLTPDGKPQT AHTTNPVPVI VTKKGIKLRD GGILGDLAPT MLDLLGLPQP
    510
    KEMTGKSLIV K
    Length:511
    Mass (Da):57,003
    Last modified:January 23, 2007 - v3
    Checksum:i45E4F5CEE457A04B
    GO

    Mass spectrometryi

    Molecular mass is 56877 Da from positions 2 - 511. Determined by MALDI. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF120091 Genomic DNA. Translation: AAD26328.1.
    PIRiT46865.
    RefSeqiWP_033015095.1. NZ_LUCR01000219.1.

    Genome annotation databases

    KEGGiag:AAD26328.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF120091 Genomic DNA. Translation: AAD26328.1.
    PIRiT46865.
    RefSeqiWP_033015095.1. NZ_LUCR01000219.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1EJJX-ray1.90A1-511[»]
    1EQJX-ray1.70A1-511[»]
    1O98X-ray1.40A1-511[»]
    1O99X-ray2.65A1-511[»]
    ProteinModelPortaliQ9X519.
    SMRiQ9X519.
    ModBaseiSearch...
    MobiDBiSearch...

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    KEGGiag:AAD26328.

    Phylogenomic databases

    KOiK15633.

    Enzyme and pathway databases

    UniPathwayiUPA00109; UER00186.
    BRENDAi5.4.2.12. 623.

    Miscellaneous databases

    EvolutionaryTraceiQ9X519.

    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_GEOSE
    AccessioniPrimary (citable) accession number: Q9X519
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 10, 2003
    Last sequence update: January 23, 2007
    Last modified: November 2, 2016
    This is version 98 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    The pH sensitivity is physiologically relevant, since it allows for the regulation of iPGM activity during different parts of the developmental cycle.1 Publication

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    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.