CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002938
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Glucose-6-phosphate isomerase 
Protein Synonyms/Alias
 GPI; Phosphoglucose isomerase; PGI; Phosphohexose isomerase; PHI 
Gene Name
 pgi 
Gene Synonyms/Alias
 b4025; JW3985 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
2******MKNINPTQTacetylation[1, 2]
17AAWQALQKHFDEMKDacetylation[2]
23QKHFDEMKDVTIADLacetylation[1, 2]
33TIADLFAKDGDRFSKacetylation[2]
65ITEETLAKLQDLAKEacetylation[1, 2]
71AKLQDLAKECDLAGAacetylation[1, 2]
80CDLAGAIKSMFSGEKacetylation[1, 2, 3]
87KSMFSGEKINRTENRacetylation[2]
114TPILVDGKDVMPEVNacetylation[2]
126EVNAVLEKMKTFSEAacetylation[1, 2]
128NAVLEKMKTFSEAIIacetylation[2]
140AIISGEWKGYTGKAIacetylation[2]
194THIAEVLKKVNPETTacetylation[2]
195HIAEVLKKVNPETTLacetylation[2]
208TLFLVASKTFTTQETacetylation[2]
228SARDWFLKAAGDEKHacetylation[2, 3]
234LKAAGDEKHVAKHFAacetylation[1, 2, 3]
238GDEKHVAKHFAALSTacetylation[1, 2]
435TEALAFGKSREVVEQacetylation[2]
449QEYRDQGKDPATLDYacetylation[1, 2, 4]
461LDYVVPFKVFEGNRPacetylation[2]
525NRILPELKDDKEISSacetylation[2]
528LPELKDDKEISSHDSacetylation[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
  
Sequence Annotation
 ACT_SITE 355 355 Proton donor (By similarity).
 ACT_SITE 386 386 By similarity.
 ACT_SITE 514 514 By similarity.
 MOD_RES 80 80 N6-acetyllysine.
 MOD_RES 228 228 N6-acetyllysine.
 MOD_RES 234 234 N6-acetyllysine.  
Keyword
 3D-structure; Acetylation; Complete proteome; Cytoplasm; Gluconeogenesis; Glycolysis; Isomerase; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 549 AA 
Protein Sequence
MKNINPTQTA AWQALQKHFD EMKDVTIADL FAKDGDRFSK FSATFDDQML VDYSKNRITE 60
ETLAKLQDLA KECDLAGAIK SMFSGEKINR TENRAVLHVA LRNRSNTPIL VDGKDVMPEV 120
NAVLEKMKTF SEAIISGEWK GYTGKAITDV VNIGIGGSDL GPYMVTEALR PYKNHLNMHF 180
VSNVDGTHIA EVLKKVNPET TLFLVASKTF TTQETMTNAH SARDWFLKAA GDEKHVAKHF 240
AALSTNAKAV GEFGIDTANM FEFWDWVGGR YSLWSAIGLS IVLSIGFDNF VELLSGAHAM 300
DKHFSTTPAE KNLPVLLALI GIWYNNFFGA ETEAILPYDQ YMHRFAAYFQ QGNMESNGKY 360
VDRNGNVVDY QTGPIIWGEP GTNGQHAFYQ LIHQGTKMVP CDFIAPAITH NPLSDHHQKL 420
LSNFFAQTEA LAFGKSREVV EQEYRDQGKD PATLDYVVPF KVFEGNRPTN SILLREITPF 480
SLGALIALYE HKIFTQGVIL NIFTFDQWGV ELGKQLANRI LPELKDDKEI SSHDSSTNGL 540
INRYKAWRG 549 
Gene Ontology
 GO:0005829; C:cytosol; IDA:UniProtKB.
 GO:0004347; F:glucose-6-phosphate isomerase activity; IDA:EcoCyc.
 GO:0034599; P:cellular response to oxidative stress; IMP:EcoCyc.
 GO:0006094; P:gluconeogenesis; IEA:HAMAP.
 GO:0006096; P:glycolysis; IMP:EcoCyc. 
Interpro
 IPR001672; G6P_Isomerase.
 IPR023096; G6P_Isomerase_C.
 IPR018189; Phosphoglucose_isomerase_CS. 
Pfam
 PF00342; PGI 
SMART
  
PROSITE
 PS00765; P_GLUCOSE_ISOMERASE_1
 PS00174; P_GLUCOSE_ISOMERASE_2
 PS51463; P_GLUCOSE_ISOMERASE_3 
PRINTS
 PR00662; G6PISOMERASE.