CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005948
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Phosphoglucosamine mutase 
Protein Synonyms/Alias
  
Gene Name
 glmM 
Gene Synonyms/Alias
 mrsA; yhbF; b3176; JW3143 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
5***MSNRKYFGTDGIacetylation[1]
35KLGWAAGKVLARHGSacetylation[1]
49SRKIIIGKDTRISGYacetylation[1]
135AIEAEMEKEISCVDSacetylation[2]
147VDSAELGKASRIVDAacetylation[1]
314GDRYVLEKMQEKGWRacetylation[1, 2, 3]
318VLEKMQEKGWRIGAEacetylation[1]
367HDLCSGMKMFPQILVacetylation[1]
392PLEHESVKAVTAEVEacetylation[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]
 [3] 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 conversion of glucosamine-6-phosphate to glucosamine-1-phosphate. Can also catalyze the formation of glucose-6-P from glucose-1-P, although at a 1400-fold lower rate. 
Sequence Annotation
 ACT_SITE 102 102 Phosphoserine intermediate.
 METAL 102 102 Magnesium; via phosphate group (By
 METAL 241 241 Magnesium (By similarity).
 METAL 243 243 Magnesium (By similarity).
 METAL 245 245 Magnesium (By similarity).
 MOD_RES 102 102 Phosphoserine; by autocatalysis.  
Keyword
 Complete proteome; Direct protein sequencing; Isomerase; Magnesium; Metal-binding; Phosphoprotein; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 445 AA 
Protein Sequence
MSNRKYFGTD GIRGRVGDAP ITPDFVLKLG WAAGKVLARH GSRKIIIGKD TRISGYMLES 60
ALEAGLAAAG LSALFTGPMP TPAVAYLTRT FRAEAGIVIS ASHNPFYDNG IKFFSIDGTK 120
LPDAVEEAIE AEMEKEISCV DSAELGKASR IVDAAGRYIE FCKATFPNEL SLSELKIVVD 180
CANGATYHIA PNVLRELGAN VIAIGCEPNG VNINAEVGAT DVRALQARVL AEKADLGIAF 240
DGDGDRVIMV DHEGNKVDGD QIMYIIAREG LRQGQLRGGA VGTLMSNMGL ELALKQLGIP 300
FARAKVGDRY VLEKMQEKGW RIGAENSGHV ILLDKTTTGD GIVAGLQVLA AMARNHMSLH 360
DLCSGMKMFP QILVNVRYTA GSGDPLEHES VKAVTAEVEA ALGNRGRVLL RKSGTEPLIR 420
VMVEGEDEAQ VTEFAHRIAD AVKAV 445 
Gene Ontology
 GO:0005829; C:cytosol; IBA:RefGenome.
 GO:0000287; F:magnesium ion binding; IEA:HAMAP.
 GO:0008966; F:phosphoglucosamine mutase activity; IDA:EcoCyc.
 GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
 GO:0046777; P:protein autophosphorylation; IDA:EcoCyc.
 GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; IMP:EcoCyc. 
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.
 IPR005841; Alpha-D-phosphohexomutase_SF.
 IPR006352; GlmM. 
Pfam
 PF02878; PGM_PMM_I
 PF02879; PGM_PMM_II
 PF02880; PGM_PMM_III
 PF00408; PGM_PMM_IV 
SMART
  
PROSITE
 PS00710; PGM_PMM 
PRINTS
 PR00509; PGMPMM.