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Protein

2,3-bisphosphoglycerate-dependent phosphoglycerate mutase

Gene

gpmA

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 and 3-phosphoglycerate.

Catalytic activityi

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

Enzyme regulationi

Strongly inhibited by vanadate.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei11 – 111Tele-phosphohistidine intermediate1 PublicationUniRule annotation
Binding sitei17 – 1712-phospho-D-glycerateCurated
Binding sitei62 – 6212-phospho-D-glycerateCurated
Binding sitei100 – 10012-phospho-D-glycerateCurated
Active sitei184 – 1841UniRule annotation
Binding sitei186 – 18612-phospho-D-glycerateCurated

GO - Molecular functioni

  1. 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity Source: EcoCyc

GO - Biological processi

  1. glycolytic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Glycolysis

Enzyme and pathway databases

BioCyciEcoCyc:GPMA-MONOMER.
ECOL316407:JW0738-MONOMER.
MetaCyc:GPMA-MONOMER.
SABIO-RKP62707.
UniPathwayiUPA00109; UER00186.

Names & Taxonomyi

Protein namesi
Recommended name:
2,3-bisphosphoglycerate-dependent phosphoglycerate mutaseUniRule annotation (EC:5.4.2.11UniRule annotation)
Short name:
BPG-dependent PGAMUniRule annotation
Short name:
PGAMUniRule annotation
Short name:
PhosphoglyceromutaseUniRule annotation
Short name:
dPGMUniRule annotation
Gene namesi
Name:gpmAUniRule annotation
Synonyms:gpm, pgm, pgmA
Ordered Locus Names:b0755, JW0738
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG11699. gpmA.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed4 Publications
Chaini2 – 2502492,3-bisphosphoglycerate-dependent phosphoglycerate mutasePRO_0000179873Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei18 – 181N6-acetyllysine1 Publication
Modified residuei100 – 1001N6-acetyllysine1 Publication
Modified residuei106 – 1061N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP62707.
PRIDEiP62707.

2D gel databases

SWISS-2DPAGEP62707.

Expressioni

Developmental stagei

Peak expression observed in mid to late log phase.

Inductioni

Regulated by the fur protein.1 Publication

Gene expression databases

GenevestigatoriP62707.

Interactioni

Subunit structurei

Homodimer.1 PublicationUniRule annotation

Protein-protein interaction databases

DIPiDIP-35899N.
IntActiP62707. 15 interactions.
MINTiMINT-1227975.
STRINGi511145.b0755.

Structurei

Secondary structure

1
250
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 107Combined sources
Helixi15 – 184Combined sources
Helixi32 – 4716Combined sources
Beta strandi53 – 575Combined sources
Helixi61 – 7414Combined sources
Beta strandi81 – 833Combined sources
Helixi85 – 873Combined sources
Helixi93 – 953Combined sources
Helixi100 – 1078Combined sources
Helixi109 – 1179Combined sources
Helixi134 – 1363Combined sources
Helixi138 – 1403Combined sources
Turni145 – 1473Combined sources
Helixi154 – 16714Combined sources
Helixi169 – 1746Combined sources
Beta strandi179 – 1835Combined sources
Helixi185 – 19511Combined sources
Helixi200 – 2056Combined sources
Beta strandi214 – 2185Combined sources
Beta strandi224 – 2296Combined sources
Helixi233 – 2397Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1E58X-ray1.25A2-250[»]
1E59X-ray1.30A2-250[»]
ProteinModelPortaliP62707.
SMRiP62707. Positions 2-248.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP62707.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni23 – 2422-phospho-D-glycerate bindingCurated
Regioni89 – 9242-phospho-D-glycerate bindingCurated
Regioni116 – 11722-phospho-D-glycerate bindingCurated

Sequence similaritiesi

Belongs to the phosphoglycerate mutase family. BPG-dependent PGAM subfamily.UniRule annotation

Phylogenomic databases

eggNOGiCOG0588.
HOGENOMiHOG000221682.
InParanoidiP62707.
KOiK01834.
OMAiDRVLPYW.
OrthoDBiEOG6C8N1H.
PhylomeDBiP62707.

Family and domain databases

Gene3Di3.40.50.1240. 1 hit.
HAMAPiMF_01039. PGAM_GpmA.
InterProiIPR013078. His_Pase_superF_clade-1.
IPR029033. His_PPase_superfam.
IPR001345. PG/BPGM_mutase_AS.
IPR005952. Phosphogly_mut1.
[Graphical view]
PANTHERiPTHR11931. PTHR11931. 1 hit.
PfamiPF00300. His_Phos_1. 1 hit.
[Graphical view]
SMARTiSM00855. PGAM. 1 hit.
[Graphical view]
SUPFAMiSSF53254. SSF53254. 1 hit.
TIGRFAMsiTIGR01258. pgm_1. 1 hit.
PROSITEiPS00175. PG_MUTASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P62707-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAVTKLVLVR HGESQWNKEN RFTGWYDVDL SEKGVSEAKA AGKLLKEEGY
60 70 80 90 100
SFDFAYTSVL KRAIHTLWNV LDELDQAWLP VEKSWKLNER HYGALQGLNK
110 120 130 140 150
AETAEKYGDE QVKQWRRGFA VTPPELTKDD ERYPGHDPRY AKLSEKELPL
160 170 180 190 200
TESLALTIDR VIPYWNETIL PRMKSGERVI IAAHGNSLRA LVKYLDNMSE
210 220 230 240 250
EEILELNIPT GVPLVYEFDE NFKPLKRYYL GNADEIAAKA AAVANQGKAK
Length:250
Mass (Da):28,556
Last modified:January 23, 2007 - v2
Checksum:iA6E0A49406F8482A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC73842.1.
AP009048 Genomic DNA. Translation: BAA35417.1.
J01591 Genomic DNA. No translation available.
PIRiC64811.
RefSeqiNP_415276.1. NC_000913.3.
YP_489028.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC73842; AAC73842; b0755.
BAA35417; BAA35417; BAA35417.
GeneIDi12930679.
945068.
KEGGiecj:Y75_p0728.
eco:b0755.
PATRICi32116709. VBIEscCol129921_0780.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC73842.1.
AP009048 Genomic DNA. Translation: BAA35417.1.
J01591 Genomic DNA. No translation available.
PIRiC64811.
RefSeqiNP_415276.1. NC_000913.3.
YP_489028.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1E58X-ray1.25A2-250[»]
1E59X-ray1.30A2-250[»]
ProteinModelPortaliP62707.
SMRiP62707. Positions 2-248.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-35899N.
IntActiP62707. 15 interactions.
MINTiMINT-1227975.
STRINGi511145.b0755.

2D gel databases

SWISS-2DPAGEP62707.

Proteomic databases

PaxDbiP62707.
PRIDEiP62707.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73842; AAC73842; b0755.
BAA35417; BAA35417; BAA35417.
GeneIDi12930679.
945068.
KEGGiecj:Y75_p0728.
eco:b0755.
PATRICi32116709. VBIEscCol129921_0780.

Organism-specific databases

EchoBASEiEB1650.
EcoGeneiEG11699. gpmA.

Phylogenomic databases

eggNOGiCOG0588.
HOGENOMiHOG000221682.
InParanoidiP62707.
KOiK01834.
OMAiDRVLPYW.
OrthoDBiEOG6C8N1H.
PhylomeDBiP62707.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00186.
BioCyciEcoCyc:GPMA-MONOMER.
ECOL316407:JW0738-MONOMER.
MetaCyc:GPMA-MONOMER.
SABIO-RKP62707.

Miscellaneous databases

EvolutionaryTraceiP62707.
PROiP62707.

Gene expression databases

GenevestigatoriP62707.

Family and domain databases

Gene3Di3.40.50.1240. 1 hit.
HAMAPiMF_01039. PGAM_GpmA.
InterProiIPR013078. His_Pase_superF_clade-1.
IPR029033. His_PPase_superfam.
IPR001345. PG/BPGM_mutase_AS.
IPR005952. Phosphogly_mut1.
[Graphical view]
PANTHERiPTHR11931. PTHR11931. 1 hit.
PfamiPF00300. His_Phos_1. 1 hit.
[Graphical view]
SMARTiSM00855. PGAM. 1 hit.
[Graphical view]
SUPFAMiSSF53254. SSF53254. 1 hit.
TIGRFAMsiTIGR01258. pgm_1. 1 hit.
PROSITEiPS00175. PG_MUTASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Bouffard G.G., Ogihara N., Rudd K.E., Adhya S.L.
    Unpublished observations (MAY-1993)
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  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.
  5. "The nucleotide sequence of aroG, the gene for 3-deoxy-D-arabinoheptulosonate-7-phosphate synthetase (phe) in Escherichia coli K12."
    Davies W.D., Davidson B.E.
    Nucleic Acids Res. 10:4045-4058(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: PRELIMINARY NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 122-250.
    Strain: K12.
  6. "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
    Link A.J., Robison K., Church G.M.
    Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-20.
    Strain: K12 / EMG2.
  7. Cited for: PROTEIN SEQUENCE OF 2-11.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  8. "Bacterial defense against aging: role of the Escherichia coli ArcA regulator in gene expression, readjusted energy flux and survival during stasis."
    Nystroem T., Larsson C., Gustafsson L.
    EMBO J. 15:3219-3228(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-11.
  9. Cited for: PROTEIN SEQUENCE OF 2-5.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  10. "Escherichia coli proteome analysis using the gene-protein database."
    VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
    Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY 2D-GEL.
  11. "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: CHARACTERIZATION.
  12. "A method for direct cloning of fur-regulated genes: identification of seven new fur-regulated loci in Escherichia coli."
    Vassinova N., Kozyrev D.
    Microbiology 146:3171-3182(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: TRANSCRIPTIONAL REGULATION.
  13. "Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli."
    Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y.
    Mol. Cell. Proteomics 8:215-225(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-18; LYS-100 AND LYS-106, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.
  14. "High resolution structure of the phosphohistidine-activated form of Escherichia coli cofactor-dependent phosphoglycerate mutase."
    Bond C.S., White M.F., Hunter W.N.
    J. Biol. Chem. 276:3247-3253(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS), ACTIVE SITE.
    Strain: K12.
  15. "Mechanistic implications for Escherichia coli cofactor-dependent phosphoglycerate mutase based on the high-resolution crystal structure of a vanadate complex."
    Bond C.S., White M.F., Hunter W.N.
    J. Mol. Biol. 316:1071-1081(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) IN COMPLEX WITH VANADATE.

Entry informationi

Entry nameiGPMA_ECOLI
AccessioniPrimary (citable) accession number: P62707
Secondary accession number(s): P31217
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: January 23, 2007
Last modified: January 7, 2015
This is version 103 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Has a 10-fold higher specific activity than BPG-independent phosphoglycerate mutase.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.