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Protein

Probable phosphoglycerate mutase GpmB

Gene

gpmB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

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

Pathwayi: glycolysis

This protein is involved in step 3 of the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate.UniRule annotation
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
Active sitei9 – 91Tele-phosphohistidine intermediateUniRule annotationBy similarity
Binding sitei58 – 581SubstrateUniRule annotationBy similarity
Binding sitei60 – 601SubstrateUniRule annotationBy similarity
Active sitei82 – 821Proton donor/acceptorUniRule annotationBy similarity
Sitei150 – 1501Transition state stabilizerUniRule annotationBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Glycolysis

Enzyme and pathway databases

BioCyciEcoCyc:PGAM2-MONOMER.
ECOL316407:JW4358-MONOMER.
UniPathwayiUPA00109; UER00186.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable phosphoglycerate mutase GpmBUniRule annotation (EC:5.4.2.-UniRule annotation)
Alternative name(s):
PGAMUniRule annotation
PhosphoglyceromutaseUniRule annotation
Gene namesi
Name:gpmBUniRule annotation
Synonyms:ytjC
Ordered Locus Names:b4395, JW4358
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG12164. gpmB.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 215215Probable phosphoglycerate mutase GpmBPRO_0000179946Add
BLAST

Proteomic databases

EPDiP0A7A2.
PaxDbiP0A7A2.
PRIDEiP0A7A2.

Interactioni

Protein-protein interaction databases

BioGridi4261680. 6 interactions.
DIPiDIP-9829N.
IntActiP0A7A2. 5 interactions.
MINTiMINT-1235576.
STRINGi511145.b4395.

Structurei

3D structure databases

ProteinModelPortaliP0A7A2.
SMRiP0A7A2. Positions 1-206.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni8 – 158Substrate bindingUniRule annotationBy similarity
Regioni21 – 222Substrate bindingUniRule annotationBy similarity
Regioni82 – 854Substrate bindingUniRule annotationBy similarity
Regioni104 – 1052Substrate bindingUniRule annotationBy similarity
Regioni151 – 1522Substrate bindingUniRule annotationBy similarity

Sequence similaritiesi

Belongs to the phosphoglycerate mutase family. GpmB subfamily.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CVJ. Bacteria.
COG0406. LUCA.
HOGENOMiHOG000221683.
InParanoidiP0A7A2.
KOiK15634.
OMAiLGCLIST.
OrthoDBiEOG6MPX0C.
PhylomeDBiP0A7A2.

Family and domain databases

Gene3Di3.40.50.1240. 1 hit.
HAMAPiMF_01040. PGAM_GpmB.
InterProiIPR013078. His_Pase_superF_clade-1.
IPR029033. His_PPase_superfam.
IPR001345. PG/BPGM_mutase_AS.
IPR023086. Phosphoglycerate_mutase_GpmB.
[Graphical view]
PfamiPF00300. His_Phos_1. 1 hit.
[Graphical view]
SMARTiSM00855. PGAM. 1 hit.
[Graphical view]
SUPFAMiSSF53254. SSF53254. 1 hit.
PROSITEiPS00175. PG_MUTASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0A7A2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLQVYLVRHG ETQWNAERRI QGQSDSPLTA KGEQQAMQVA TRAKELGITH
60 70 80 90 100
IISSDLGRTR RTAEIIAQAC GCDIIFDSRL RELNMGVLEK RHIDSLTEEE
110 120 130 140 150
ENWRRQLVNG TVDGRIPEGE SMQELSDRVN AALESCRDLP QGSRPLLVSH
160 170 180 190 200
GIALGCLVST ILGLPAWAER RLRLRNCSIS RVDYQESLWL ASGWVVETAG
210
DISHLDAPAL DELQR
Length:215
Mass (Da):24,065
Last modified:June 7, 2005 - v1
Checksum:i3653DA0548B9E009
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti148 – 1481V → L (PubMed:8449900).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M97495 Genomic DNA. No translation available.
U14003 Genomic DNA. Translation: AAA97291.1.
U00096 Genomic DNA. Translation: AAC77348.1.
AP009048 Genomic DNA. Translation: BAE78384.1.
PIRiS56619.
RefSeqiNP_418812.1. NC_000913.3.
WP_000942344.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC77348; AAC77348; b4395.
BAE78384; BAE78384; BAE78384.
GeneIDi948918.
KEGGiecj:JW4358.
eco:b4395.
PATRICi32124408. VBIEscCol129921_4544.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M97495 Genomic DNA. No translation available.
U14003 Genomic DNA. Translation: AAA97291.1.
U00096 Genomic DNA. Translation: AAC77348.1.
AP009048 Genomic DNA. Translation: BAE78384.1.
PIRiS56619.
RefSeqiNP_418812.1. NC_000913.3.
WP_000942344.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliP0A7A2.
SMRiP0A7A2. Positions 1-206.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261680. 6 interactions.
DIPiDIP-9829N.
IntActiP0A7A2. 5 interactions.
MINTiMINT-1235576.
STRINGi511145.b4395.

Proteomic databases

EPDiP0A7A2.
PaxDbiP0A7A2.
PRIDEiP0A7A2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC77348; AAC77348; b4395.
BAE78384; BAE78384; BAE78384.
GeneIDi948918.
KEGGiecj:JW4358.
eco:b4395.
PATRICi32124408. VBIEscCol129921_4544.

Organism-specific databases

EchoBASEiEB2083.
EcoGeneiEG12164. gpmB.

Phylogenomic databases

eggNOGiENOG4105CVJ. Bacteria.
COG0406. LUCA.
HOGENOMiHOG000221683.
InParanoidiP0A7A2.
KOiK15634.
OMAiLGCLIST.
OrthoDBiEOG6MPX0C.
PhylomeDBiP0A7A2.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00186.
BioCyciEcoCyc:PGAM2-MONOMER.
ECOL316407:JW4358-MONOMER.

Miscellaneous databases

PROiP0A7A2.

Family and domain databases

Gene3Di3.40.50.1240. 1 hit.
HAMAPiMF_01040. PGAM_GpmB.
InterProiIPR013078. His_Pase_superF_clade-1.
IPR029033. His_PPase_superfam.
IPR001345. PG/BPGM_mutase_AS.
IPR023086. Phosphoglycerate_mutase_GpmB.
[Graphical view]
PfamiPF00300. His_Phos_1. 1 hit.
[Graphical view]
SMARTiSM00855. PGAM. 1 hit.
[Graphical view]
SUPFAMiSSF53254. SSF53254. 1 hit.
PROSITEiPS00175. PG_MUTASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A novel binding protein of the origin of the Escherichia coli chromosome."
    Skarstad K., Thoeny B., Hwang D.S., Kornberg A.
    J. Biol. Chem. 268:5365-5370(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  2. "Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes."
    Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.
    Nucleic Acids Res. 23:2105-2119(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  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.

Entry informationi

Entry nameiGPMB_ECOLI
AccessioniPrimary (citable) accession number: P0A7A2
Secondary accession number(s): P36942, Q2M5S2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: June 7, 2005
Last modified: July 6, 2016
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.