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Protein

2,3-bisphosphoglycerate-independent phosphoglycerate mutase

Gene

gpmI

Organism
Bacillus subtilis (strain 168)
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 and 3-phosphoglycerate.2 Publications

Catalytic activityi

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

Cofactori

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

Enzyme regulationi

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

pH dependencei

Very sensitive to pH. A pH change from 8 to 6 results in greater than 30- to 200-fold decreases in its activity. However, deactivation at pH 6 is reversed by shifting the enzyme to pH 7 or 8.1 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 1 (gapA)
  2. Phosphoglycerate kinase (pgk)
  3. 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (gpmI)
  4. Enolase (eno)
  5. Pyruvate kinase (pyk)
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 bindingi12 – 121Manganese 2UniRule annotation
Active sitei62 – 621Phosphoserine intermediateUniRule annotation
Metal bindingi62 – 621Manganese 2UniRule annotation
Binding sitei123 – 1231SubstrateUniRule annotation
Binding sitei185 – 1851SubstrateUniRule annotation
Binding sitei191 – 1911SubstrateUniRule 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 bindingi462 – 4621Manganese 1UniRule annotation

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

BioCyciBSUB:BSU33910-MONOMER.
SABIO-RKP39773.
UniPathwayiUPA00109; UER00186.

Names & Taxonomyi

Protein namesi
Recommended name:
2,3-bisphosphoglycerate-independent phosphoglycerate mutase1 Publication (EC:5.4.2.12UniRule annotation)
Short name:
BPG-independent PGAM1 Publication
Short name:
Phosphoglyceromutase1 Publication
Short name:
iPGM1 Publication
Alternative name(s):
Vegetative protein 107
Short name:
VEG107
Gene namesi
Name:gpmIUniRule annotation
Synonyms:pgm
Ordered Locus Names:BSU33910
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved2 Publications
Chaini2 – 5115102,3-bisphosphoglycerate-independent phosphoglycerate mutasePRO_0000212128Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei36 – 361Phosphotyrosine1 Publication
Modified residuei62 – 621Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP39773.

PTM databases

iPTMnetiP39773.

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

IntActiP39773. 1 interaction.
MINTiMINT-8365627.
STRINGi224308.Bsubs1_010100018391.

Structurei

3D structure databases

ProteinModelPortaliP39773.
SMRiP39773. Positions 2-509.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni153 – 1542Substrate bindingUniRule annotation
Regioni261 – 2644Substrate bindingUniRule annotation

Sequence similaritiesi

Belongs to the BPG-independent phosphoglycerate mutase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CJI. Bacteria.
COG0696. LUCA.
HOGENOMiHOG000223664.
InParanoidiP39773.
KOiK15633.
OMAiLHIATMT.
PhylomeDBiP39773.

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.

P39773-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKKPAALII LDGFGLRNET VGNAVALAKK PNFDRYWNQY PHQTLTASGE
60 70 80 90 100
AVGLPEGQMG NSEVGHLNIG AGRIVYQSLT RVNVAIREGE FERNQTFLDA
110 120 130 140 150
ISNAKENNKA LHLFGLLSDG GVHSHINHLF ALLKLAKKEG LTKVYIHGFL
160 170 180 190 200
DGRDVGPQTA KTYINQLNDQ IKEIGVGEIA SISGRYYSMD RDKRWDRVEK
210 220 230 240 250
AYRAMAYGEG PSYRSALDVV DDSYANGIYD EFVIPSVITK ENGEPVAKIQ
260 270 280 290 300
DGDSVIFYNF RPDRAIQISN TFTNKDFRDF DRGENYPKNL YFVCLTHFSE
310 320 330 340 350
TVDGYVAFKP INLDNTVGEV LSQHGLKQLR IAETEKYPHV TFFMSGGREA
360 370 380 390 400
EFPGEERILI NSPKVATYDL KPEMSAYEVK DALVKEIEAD KHDAIILNFA
410 420 430 440 450
NPDMVGHSGM VEPTIKAIEA VDECLGEVVD AILAKGGHAI ITADHGNADI
460 470 480 490 500
LITESGEPHT AHTTNPVPVI VTKEGITLRE GGILGDLAPT LLDLLGVEKP
510
KEMTGTSLIQ K
Length:511
Mass (Da):56,309
Last modified:January 23, 2007 - v4
Checksum:iB2823B683D634891
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti233 – 2331V → C in AAA21680 (PubMed:8021172).Curated
Sequence conflicti432 – 4332IL → MV in AAA21680 (PubMed:8021172).Curated
Sequence conflicti445 – 4451H → D in AAA21680 (PubMed:8021172).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L29475 Genomic DNA. Translation: AAA21680.1.
AL009126 Genomic DNA. Translation: CAB15396.1.
PIRiD69675.
RefSeqiNP_391271.1. NC_000964.3.
WP_003228330.1. NZ_JNCM01000033.1.

Genome annotation databases

EnsemblBacteriaiCAB15396; CAB15396; BSU33910.
GeneIDi938574.
KEGGibsu:BSU33910.
PATRICi18978782. VBIBacSub10457_3554.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L29475 Genomic DNA. Translation: AAA21680.1.
AL009126 Genomic DNA. Translation: CAB15396.1.
PIRiD69675.
RefSeqiNP_391271.1. NC_000964.3.
WP_003228330.1. NZ_JNCM01000033.1.

3D structure databases

ProteinModelPortaliP39773.
SMRiP39773. Positions 2-509.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP39773. 1 interaction.
MINTiMINT-8365627.
STRINGi224308.Bsubs1_010100018391.

PTM databases

iPTMnetiP39773.

Proteomic databases

PaxDbiP39773.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB15396; CAB15396; BSU33910.
GeneIDi938574.
KEGGibsu:BSU33910.
PATRICi18978782. VBIBacSub10457_3554.

Phylogenomic databases

eggNOGiENOG4105CJI. Bacteria.
COG0696. LUCA.
HOGENOMiHOG000223664.
InParanoidiP39773.
KOiK15633.
OMAiLHIATMT.
PhylomeDBiP39773.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00186.
BioCyciBSUB:BSU33910-MONOMER.
SABIO-RKP39773.

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_BACSU
AccessioniPrimary (citable) accession number: P39773
Secondary accession number(s): O32250
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: January 23, 2007
Last modified: September 7, 2016
This is version 130 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  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.