P62707 (GPMA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

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)

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 MF_01039
Catalytic activity	2-phospho-D-glycerate = 3-phospho-D-glycerate. HAMAP MF_01039
Enzyme regulation	Strongly inhibited by vanadate. HAMAP MF_01039
Pathway	Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5. HAMAP MF_01039
Subunit structure	Homodimer.
Developmental stage	Peak expression observed in mid to late log phase. HAMAP MF_01039
Induction	Regulated by the fur protein. Ref.11
Miscellaneous	Has a 10-fold higher specific activity than BPG-independent phosphoglycerate mutase. HAMAP 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: UniProtKB-KW
Cellular component	cytoplasm Inferred from direct assay. Source: UniProtKB
Molecular function	2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity Inferred from direct assay Ref.10. Source: EcoCyc protein homodimerization activity Inferred from direct assay Ref.10. Source: EcoCyc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

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

Chain

2 – 250

249

2,3-bisphosphoglycerate-dependent phosphoglycerate mutase HAMAP MF_01039

PRO_0000179873

Sites

Active site

11

1

Tele-phosphohistidine intermediate

Active site

184

1

By similarity

Site

62

1

Interaction with carboxyl group of phosphoglycerates By similarity

Amino acid modifications

Modified residue

18

1

N6-acetyllysine Ref.12

Modified residue

100

1

N6-acetyllysine Ref.12

Modified residue

106

1

N6-acetyllysine Ref.12

Secondary structure

1

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250

Helix Strand Turn

Details...

Beta strand

4 – 10

7

Helix

15 – 18

4

Helix

32 – 47

16

Beta strand

53 – 57

5

Helix

61 – 74

14

Beta strand

81 – 83

3

Helix

85 – 87

3

Helix

93 – 95

3

Helix

100 – 107

8

Helix

109 – 117

9

Helix

134 – 136

3

Helix

138 – 140

3

Turn

145 – 147

3

Helix

154 – 167

14

Helix

169 – 174

6

Beta strand

179 – 183

5

Helix

185 – 195

11

Helix

200 – 205

6

Beta strand

214 – 218

5

Beta strand

224 – 229

6

Helix

233 – 239

7

Sequences

	Sequence		Length	Mass (Da)
	P62707 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: A6E0A49406F8482A	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

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. , Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M., Horiuchi T. DNA Res. 3:137-155(1996) [PubMed: 8905232] [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: 9278503] [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: 16738553] [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: 6125934] [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: 9298646] [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: 8670822] [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: 9600841] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-5. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[10]	"The two analogous phosphoglycerate mutases of Escherichia coli." Fraser H.I., Kvaratskhelia M., White M.F. FEBS Lett. 455:344-348(1999) [PubMed: 10437801] [Abstract] Cited for: CHARACTERIZATION.
[11]	"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: 11101675] [Abstract] Cited for: TRANSCRIPTIONAL REGULATION.
[12]	"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: 18723842] [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.
[13]	"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: 11038361] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS). Strain: K12.
[14]	"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: 11884145] [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.

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.

2D gel databases

SWISS-2DPAGE

P62707.

2DBase-Ecoli

P62707.

ECO2DBASE

G027.1. 6TH EDITION.

Proteomic databases

PRIDE

P62707.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBESCT00000004553; EBESCP00000004553; EBESCG00000003716.
EBESCT00000015748; EBESCP00000015039; EBESCG00000014808.

GeneID

945068.

GenomeReviews

Gene locus JW0738 in contig AP009048_GR.
Gene locus b0755 in contig U00096_GR.

KEGG

ecj:JW0738.
eco:b0755.

PATRIC

32116709. VBIEscCol129921_0780.

Organism-specific databases

EchoBASE

EB1650.

EcoGene

EG11699. gpmA.

Phylogenomic databases

eggNOG

COG0588.

GeneTree

EBGT00050000010640.

HOGENOM

HBG658938.

OMA

EWNALNL.

PhylomeDB

P62707.

ProtClustDB

PRK14115.

Enzyme and pathway databases

BioCyc

EcoCyc:GPMA-MONOMER.
MetaCyc:GPMA-MONOMER.

Gene expression databases

Genevestigator

P62707.

Family and domain databases

HAMAP

MF_01039. PGAM_GpmA.
[Tree]

InterPro

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

KO

K01834.

PANTHER

PTHR11931. Phosphogly_mut1. 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...

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:	January 25, 2012
This is version 79 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program