CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-006686
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Phosphoglucomutase 
Protein Synonyms/Alias
 PGM; Glucose phosphomutase 
Gene Name
 pgm 
Gene Synonyms/Alias
 b0688; JW0675 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
30TAQYYVLKPEAGNAEacetylation[1]
41GNAEHAVKFGTSGHRacetylation[1]
171PADTNVTKVVEDRANacetylation[1]
186ALLADGLKGVKRISLacetylation[1]
189ADGLKGVKRISLDEAacetylation[1]
245GSGIEYWKRIGEYYNacetylation[1]
273FRFMHLDKDGAIRMDacetylation[1]
296GLLALRDKFDLAFANacetylation[1]
438EHYNELAKRFGAPSYacetylation[1]
457AAATSAQKAALSKLSacetylation[1]
462AQKAALSKLSPEMVSacetylation[1, 2]
516SGTEDAYKIYCESFLacetylation[1, 2]
533EHRKQIEKEAVEIVSacetylation[1]
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
 This enzyme participates in both the breakdown and synthesis of glucose. 
Sequence Annotation
 ACT_SITE 146 146 Phosphoserine intermediate (By
 METAL 146 146 Magnesium; via phosphate group (By
 METAL 304 304 Magnesium (By similarity).
 METAL 306 306 Magnesium (By similarity).
 METAL 308 308 Magnesium (By similarity).  
Keyword
 Carbohydrate metabolism; Complete proteome; Glucose metabolism; Isomerase; Magnesium; Metal-binding; Phosphoprotein; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 546 AA 
Protein Sequence
MAIHNRAGQP AQQSDLINVA QLTAQYYVLK PEAGNAEHAV KFGTSGHRGS AARHSFNEPH 60
ILAIAQAIAE ERAKNGITGP CYVGKDTHAL SEPAFISVLE VLAANGVDVI VQENNGFTPT 120
PAVSNAILVH NKKGGPLADG IVITPSHNPP EDGGIKYNPP NGGPADTNVT KVVEDRANAL 180
LADGLKGVKR ISLDEAMASG HVKEQDLVQP FVEGLADIVD MAAIQKAGLT LGVDPLGGSG 240
IEYWKRIGEY YNLNLTIVND QVDQTFRFMH LDKDGAIRMD CSSECAMAGL LALRDKFDLA 300
FANDPDYDRH GIVTPAGLMN PNHYLAVAIN YLFQHRPQWG KDVAVGKTLV SSAMIDRVVN 360
DLGRKLVEVP VGFKWFVDGL FDGSFGFGGE ESAGASFLRF DGTPWSTDKD GIIMCLLAAE 420
ITAVTGKNPQ EHYNELAKRF GAPSYNRLQA AATSAQKAAL SKLSPEMVSA STLAGDPITA 480
RLTAAPGNGA SIGGLKVMTD NGWFAARPSG TEDAYKIYCE SFLGEEHRKQ IEKEAVEIVS 540
EVLKNA 546 
Gene Ontology
 GO:0005829; C:cytosol; IBA:RefGenome.
 GO:0000287; F:magnesium ion binding; IEA:InterPro.
 GO:0004614; F:phosphoglucomutase activity; IDA:EcoCyc.
 GO:0016052; P:carbohydrate catabolic process; IMP:EcoCyc.
 GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW. 
Interpro
 IPR005844; A-D-PHexomutase_a/b/a-I.
 IPR016055; A-D-PHexomutase_a/b/a-I/II/III.
 IPR005845; A-D-PHexomutase_a/b/a-II.
 IPR005846; A-D-PHexomutase_a/b/a-III.
 IPR005843; A-D-PHexomutase_C.
 IPR016066; A-D-PHexomutase_CS.
 IPR005852; PGlcMutase_a-D-Glc-sp. 
Pfam
 PF02878; PGM_PMM_I
 PF02879; PGM_PMM_II
 PF02880; PGM_PMM_III
 PF00408; PGM_PMM_IV 
SMART
  
PROSITE
 PS00710; PGM_PMM 
PRINTS