CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-006782
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 2,3-bisphosphoglycerate-independent phosphoglycerate mutase 
Protein Synonyms/Alias
 BPG-independent PGAM; Phosphoglyceromutase; iPGM 
Gene Name
 gpmI 
Gene Synonyms/Alias
 pgmI; yibO; b3612; JW3587 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
89TRLDVEIKDRAFFANacetylation[1]
105VLTGAVDKAKNAGKAacetylation[1]
145AAERGAEKIYLHAFLacetylation[1]
168SAESSLKKFEEKFAAacetylation[1]
172SLKKFEEKFAALGKGacetylation[1]
237DENDEFVKATVIRAEacetylation[1]
323TFGEWMAKNDKTQLRacetylation[1]
364RILINSPKVATYDLQacetylation[1]
382SSAELTEKLVAAIKSacetylation[1]
391VAAIKSGKYDTIICNacetylation[1]
479YVGDKNVKAVEGGKLacetylation[1, 2]
Reference
 [1] 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]
 [2] 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] 
Functional Description
 Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate. 
Sequence Annotation
 ACT_SITE 64 64 Phosphoserine intermediate (By
 METAL 14 14 Manganese 2 (By similarity).
 METAL 64 64 Manganese 2 (By similarity).
 METAL 403 403 Manganese 1 (By similarity).
 METAL 407 407 Manganese 1 (By similarity).
 METAL 444 444 Manganese 2 (By similarity).
 METAL 445 445 Manganese 2 (By similarity).
 METAL 463 463 Manganese 1 (By similarity).  
Keyword
 Complete proteome; Glycolysis; Isomerase; Manganese; Metal-binding; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 514 AA 
Protein Sequence
MLVSKKPMVL VILDGYGYRE EQQDNAIFSA KTPVMDALWA NRPHTLIDAS GLEVGLPDRQ 60
MGNSEVGHVN LGAGRIVYQD LTRLDVEIKD RAFFANPVLT GAVDKAKNAG KAVHIMGLLS 120
AGGVHSHEDH IMAMVELAAE RGAEKIYLHA FLDGRDTPPR SAESSLKKFE EKFAALGKGR 180
VASIIGRYYA MDRDNRWDRV EKAYDLLTLA QGEFQADTAV AGLQAAYARD ENDEFVKATV 240
IRAEGQPDAA MEDGDALIFM NFRADRAREI TRAFVNADFD GFARKKVVNV DFVMLTEYAA 300
DIKTAVAYPP ASLVNTFGEW MAKNDKTQLR ISETEKYAHV TFFFNGGVEE SFKGEDRILI 360
NSPKVATYDL QPEMSSAELT EKLVAAIKSG KYDTIICNYP NGDMVGHTGV MEAAVKAVEA 420
LDHCVEEVAK AVESVGGQLL ITADHGNAEQ MRDPATGQAH TAHTNLPVPL IYVGDKNVKA 480
VEGGKLSDIA PTMLSLMGME IPQEMTGKPL FIVE 514 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:UniProtKB.
 GO:0046537; F:2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity; IDA:EcoCyc.
 GO:0030145; F:manganese ion binding; IDA:EcoCyc.
 GO:0006096; P:glycolysis; IEA:HAMAP. 
Interpro
 IPR017849; Alkaline_Pase-like_a/b/a.
 IPR017850; Alkaline_phosphatase_core.
 IPR011258; BPG-indep_PGM_N.
 IPR006124; Metalloenzyme.
 IPR005995; Pgm_bpd_ind. 
Pfam
 PF06415; iPGM_N
 PF01676; Metalloenzyme 
SMART
  
PROSITE
  
PRINTS