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P62707

- GPMA_ECOLI

UniProt

P62707 - GPMA_ECOLI

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Protein
2,3-bisphosphoglycerate-dependent phosphoglycerate mutase
Gene
gpmA, gpm, pgm, pgmA, b0755, JW0738
Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.UniRule annotation

Catalytic activityi

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

Enzyme regulationi

Strongly inhibited by vanadate.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei11 – 111Tele-phosphohistidine intermediate1 Publication
Binding sitei17 – 1712-phospho-D-glycerate Inferred
Binding sitei62 – 6212-phospho-D-glycerate Inferred
Binding sitei100 – 10012-phospho-D-glycerate Inferred
Active sitei184 – 1841 By similarity
Binding sitei186 – 18612-phospho-D-glycerate Inferred

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 mutase (EC:5.4.2.11)
Short name:
BPG-dependent PGAM
Short name:
PGAM
Short name:
Phosphoglyceromutase
Short name:
dPGM
Gene namesi
Name:gpmA
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 mutaseUniRule annotation
PRO_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.UniRule annotation

Inductioni

Regulated by the fur protein.1 Publication

Gene expression databases

GenevestigatoriP62707.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

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

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1E58X-ray1.25A2-250[»]
1E59X-ray1.30A2-250[»]
ProteinModelPortaliP62707.
SMRiP62707. Positions 2-248.

Miscellaneous databases

EvolutionaryTraceiP62707.

Family & Domainsi

Region

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0588.
HOGENOMiHOG000221682.
KOiK01834.
OMAiKDDERFP.
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

MAVTKLVLVR HGESQWNKEN RFTGWYDVDL SEKGVSEAKA AGKLLKEEGY    50
SFDFAYTSVL KRAIHTLWNV LDELDQAWLP VEKSWKLNER HYGALQGLNK 100
AETAEKYGDE QVKQWRRGFA VTPPELTKDD ERYPGHDPRY AKLSEKELPL 150
TESLALTIDR VIPYWNETIL PRMKSGERVI IAAHGNSLRA LVKYLDNMSE 200
EEILELNIPT GVPLVYEFDE NFKPLKRYYL GNADEIAAKA AAVANQGKAK 250
Length:250
Mass (Da):28,556
Last modified:January 23, 2007 - v2
Checksum:iA6E0A49406F8482A
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
U00096 Genomic DNA. Translation: AAC73842.1 .
AP009048 Genomic DNA. Translation: BAA35417.1 .
J01591 Genomic DNA. No translation available.
PIRi C64811.
RefSeqi NP_415276.1. NC_000913.3.
YP_489028.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1E58 X-ray 1.25 A 2-250 [» ]
1E59 X-ray 1.30 A 2-250 [» ]
ProteinModelPortali P62707.
SMRi P62707. Positions 2-248.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-35899N.
IntActi P62707. 15 interactions.
MINTi MINT-1227975.
STRINGi 511145.b0755.

2D gel databases

SWISS-2DPAGE P62707.

Proteomic databases

PaxDbi P62707.
PRIDEi P62707.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC73842 ; AAC73842 ; b0755 .
BAA35417 ; BAA35417 ; BAA35417 .
GeneIDi 12930679.
945068.
KEGGi ecj:Y75_p0728.
eco:b0755.
PATRICi 32116709. VBIEscCol129921_0780.

Organism-specific databases

EchoBASEi EB1650.
EcoGenei EG11699. gpmA.

Phylogenomic databases

eggNOGi COG0588.
HOGENOMi HOG000221682.
KOi K01834.
OMAi KDDERFP.
OrthoDBi EOG6C8N1H.
PhylomeDBi P62707.

Enzyme and pathway databases

UniPathwayi UPA00109 ; UER00186 .
BioCyci EcoCyc:GPMA-MONOMER.
ECOL316407:JW0738-MONOMER.
MetaCyc:GPMA-MONOMER.
SABIO-RK P62707.

Miscellaneous databases

EvolutionaryTracei P62707.
PROi P62707.

Gene expression databases

Genevestigatori P62707.

Family and domain databases

Gene3Di 3.40.50.1240. 1 hit.
HAMAPi MF_01039. PGAM_GpmA.
InterProi IPR013078. His_Pase_superF_clade-1.
IPR029033. His_PPase_superfam.
IPR001345. PG/BPGM_mutase_AS.
IPR005952. Phosphogly_mut1.
[Graphical view ]
PANTHERi PTHR11931. PTHR11931. 1 hit.
Pfami PF00300. His_Phos_1. 1 hit.
[Graphical view ]
SMARTi SM00855. PGAM. 1 hit.
[Graphical view ]
SUPFAMi SSF53254. SSF53254. 1 hit.
TIGRFAMsi TIGR01258. pgm_1. 1 hit.
PROSITEi PS00175. PG_MUTASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: June 11, 2014
This is version 100 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

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