UniProt Accession

 GPMA_ECOLI; P62707; P31217 

Genbank Protein ID

 U00096; AP009048; J01591 

Genbank Nucleotide ID

 AAC73842.1; BAA35417.1 

Protein Name

 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase 

Protein Synonyms/Alias

 BPG-dependent PGAM; PGAM; Phosphoglyceromutase; dPGM 

Gene Name

 gpmA 

Gene Synonyms/Alias

 gpm; pgm; pgmA; b0755; JW0738 

Created Date

 July 27, 2013 

Organism

 Escherichia coli (strain K12) 

NCBI Taxa ID

 83333 

Lysine Modification

Position	Peptide	Type	References
5	***MAVTKLVLVRHG	acetylation	[1, 2]
18	HGESQWNKENRFTGW	acetylation	[2, 3]
33	YDVDLSEKGVSEAKA	acetylation	[1, 2]
39	EKGVSEAKAAGKLLK	acetylation	[2]
43	SEAKAAGKLLKEEGY	acetylation	[2]
46	KAAGKLLKEEGYSFD	acetylation	[2]
86	LPVEKSWKLNERHYG	acetylation	[2]
100	GALQGLNKAETAEKY	acetylation	[1, 2, 3, 4]
106	NKAETAEKYGDEQVK	acetylation	[1, 2, 3, 4]
113	KYGDEQVKQWRRGFA	acetylation	[2]
128	VTPPELTKDDERYPG	acetylation	[2]
142	GHDPRYAKLSEKELP	acetylation	[2]
146	RYAKLSEKELPLTES	acetylation	[1, 2]
239	NADEIAAKAAAVANQ	acetylation	[2]

Reference

 [1] Comprehensive profiling of protein lysine acetylation in Escherichia coli.
 Zhang K, Zheng S, Yang JS, Chen Y, Cheng Z.
 J Proteome Res. 2013 Feb 1;12(2):844-51. [PMID: 23294111]
 [2] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli.
 Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C.
 Mol Cell. 2013 Jul 25;51(2):265-72. [PMID: 23830618]
 [3] 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 CF, Grishin NV, Zhao Y.
 Mol Cell Proteomics. 2009 Feb;8(2):215-25. [PMID: 18723842]
 [4] The diversity of lysine-acetylated proteins in Escherichia coli.
 Yu BJ, Kim JA, Moon JH, Ryu SE, Pan JG.
 J Microbiol Biotechnol. 2008 Sep;18(9):1529-36. [PMID: 18852508] 

Functional Description

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

Sequence Annotation

 REGION 23 24 2-phospho-D-glycerate binding (Probable).
 REGION 89 92 2-phospho-D-glycerate binding (Probable).
 REGION 116 117 2-phospho-D-glycerate binding (Probable).
 ACT_SITE 11 11 Tele-phosphohistidine intermediate.
 ACT_SITE 184 184 By similarity.
 BINDING 17 17 2-phospho-D-glycerate (Probable).
 BINDING 62 62 2-phospho-D-glycerate (Probable).
 BINDING 100 100 2-phospho-D-glycerate (Probable).
 BINDING 186 186 2-phospho-D-glycerate (Probable).
 MOD_RES 18 18 N6-acetyllysine.
 MOD_RES 100 100 N6-acetyllysine.
 MOD_RES 106 106 N6-acetyllysine.  

Keyword

 3D-structure; Acetylation; Complete proteome; Direct protein sequencing; Glycolysis; Isomerase; Reference proteome. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 250 AA 

Protein Sequence

Gene Ontology

 GO:0005737; C:cytoplasm; IDA:UniProtKB.
 GO:0046538; F:2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity; IDA:EcoCyc.
 GO:0006096; P:glycolysis; IEA:HAMAP. 

Interpro

 IPR013078; His_Pase_superF_clade-1.
 IPR001345; PG/BPGM_mutase_AS.
 IPR005952; Phosphogly_mut1. 

Pfam

 PF00300; His_Phos_1 

SMART

 SM00855; PGAM 

PROSITE

 PS00175; PG_MUTASE 

PRINTS