2,3-bisphosphoglycerate-dependent phosphoglycerate mutase

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P62707 (GPMA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 91. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
2,3-bisphosphoglycerate-dependent phosphoglycerate mutase
Short name=BPG-dependent PGAM
Short name=PGAM
Short name=Phosphoglyceromutase
Short name=dPGM
EC=5.4.2.1

Gene names

Name:	gpmA
Synonyms:	gpm, pgm, pgmA
Ordered Locus Names:	b0755, JW0738

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	250 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate. HAMAP-Rule MF_01039
Catalytic activity	2-phospho-D-glycerate = 3-phospho-D-glycerate. HAMAP-Rule MF_01039
Enzyme regulation	Strongly inhibited by vanadate. HAMAP-Rule MF_01039
Pathway	Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5. HAMAP-Rule MF_01039
Subunit structure	Homodimer.
Developmental stage	Peak expression observed in mid to late log phase. HAMAP-Rule MF_01039
Induction	Regulated by the fur protein. Ref.12
Miscellaneous	Has a 10-fold higher specific activity than BPG-independent phosphoglycerate mutase. HAMAP-Rule MF_01039
Sequence similarities	Belongs to the phosphoglycerate mutase family. BPG-dependent PGAM subfamily.

Ontologies

Keywords
Biological process	Glycolysis
Molecular function	Isomerase
PTM	Acetylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	glycolysis Inferred from electronic annotation. Source: HAMAP
Cellular_component	cytoplasm Inferred from direct assay PubMed 16858726. Source: UniProtKB
Molecular_function	2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity Inferred from direct assay Ref.11. Source: EcoCyc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.6 Ref.7 Ref.8 Ref.9

Chain

2 – 250

249

2,3-bisphosphoglycerate-dependent phosphoglycerate mutase HAMAP-Rule MF_01039

PRO_0000179873

Sites

Active site

Tele-phosphohistidine intermediate

Active site

184

By similarity

Site

Interaction with carboxyl group of phosphoglycerates By similarity

Amino acid modifications

Modified residue

N6-acetyllysine Ref.13

Modified residue

100

N6-acetyllysine Ref.13

Modified residue

106

N6-acetyllysine Ref.13

Secondary structure

250

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P62707 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: A6E0A49406F8482A
Show »

FASTA

250

28,556

        10         20         30         40         50         60 
MAVTKLVLVR HGESQWNKEN RFTGWYDVDL SEKGVSEAKA AGKLLKEEGY SFDFAYTSVL 

        70         80         90        100        110        120 
KRAIHTLWNV LDELDQAWLP VEKSWKLNER HYGALQGLNK AETAEKYGDE QVKQWRRGFA 

       130        140        150        160        170        180 
VTPPELTKDD ERYPGHDPRY AKLSEKELPL TESLALTIDR VIPYWNETIL PRMKSGERVI 

       190        200        210        220        230        240 
IAAHGNSLRA LVKYLDNMSE EEILELNIPT GVPLVYEFDE NFKPLKRYYL GNADEIAAKA 

       250 
AAVANQGKAK

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map." Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K. Horiuchi T. DNA Res. 3:137-155(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] 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]	Pasquali C., Sanchez J.-C., Ravier F., Golaz O., Hughes G.J., Frutiger S., Paquet N., Wilkins M., Appel R.D., Bairoch A., Hochstrasser D.F. Submitted (SEP-1994) to UniProtKB 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]	"Protein identification with N and C-terminal sequence tags in proteome projects." Wilkins M.R., Gasteiger E., Tonella L., Ou K., Tyler M., Sanchez J.-C., Gooley A.A., Walsh B.J., Bairoch A., Appel R.D., Williams K.L., Hochstrasser D.F. J. Mol. Biol. 278:599-608(1998) [PubMed] [Europe PMC] [Abstract] 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, 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). 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).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U00096 Genomic DNA. Translation: AAC73842.1.
AP009048 Genomic DNA. Translation: BAA35417.1.
J01591 Genomic DNA. No translation available.

PIR

C64811.

RefSeq

NP_415276.1. NC_000913.2.
YP_489028.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1E58	X-ray	1.25	A	2-250	[»]
1E59	X-ray	1.30	A	2-250	[»]

ProteinModelPortal

P62707.

SMR

P62707. Positions 2-248.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-35899N.

IntAct

P62707. 15 interactions.

MINT

MINT-1227975.

STRING

511145.b0755.

2D gel databases

SWISS-2DPAGE

P62707.

Proteomic databases

PaxDb

P62707.

PRIDE

P62707.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC73842; AAC73842; b0755.
BAA35417; BAA35417; BAA35417.

GeneID

12930679.
945068.

KEGG

ecj:Y75_p0728.
eco:b0755.

PATRIC

32116709. VBIEscCol129921_0780.

Organism-specific databases

EchoBASE

EB1650.

EcoGene

EG11699. gpmA.

Phylogenomic databases

eggNOG

COG0588.

HOGENOM

HOG000221682.

K01834.

OMA

GQSDWNL.

ProtClustDB

PRK14115.

Enzyme and pathway databases

BioCyc

EcoCyc:GPMA-MONOMER.
ECOL316407:JW0738-MONOMER.
MetaCyc:GPMA-MONOMER.

SABIO-RK

P62707.

UniPathway

UPA00109; UER00186.

Gene expression databases

Genevestigator

P62707.

Family and domain databases

HAMAP

MF_01039. PGAM_GpmA.

InterPro

IPR013078. His_Pase_superF_clade-1.
IPR001345. PG/BPGM_mutase_AS.
IPR005952. Phosphogly_mut1.
[Graphical view]

PANTHER

PTHR11931. PTHR11931. 1 hit.

Pfam

PF00300. His_Phos_1. 1 hit.
[Graphical view]

SMART

SM00855. PGAM. 1 hit.
[Graphical view]

TIGRFAMs

TIGR01258. pgm_1. 1 hit.

PROSITE

PS00175. PG_MUTASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P62707.

Entry information

Entry name

GPMA_ECOLI

Accession

Primary (citable) accession number: P62707
Secondary accession number(s): P31217

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2004
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 91 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents