CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-003156
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Glyceraldehyde-3-phosphate dehydrogenase A 
Protein Synonyms/Alias
 GAPDH-A 
Gene Name
 gapA 
Gene Synonyms/Alias
 b1779; JW1768 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
4****MTIKVGINGFGacetylation[1]
46DYMAYMLKYDSTHGRacetylation[1, 2]
61FDGTVEVKDGHLIVNacetylation[1, 2]
70GHLIVNGKKIRVTAEacetylation[2]
71HLIVNGKKIRVTAERacetylation[2]
108LTDETARKHITAGAKacetylation[1, 2]
115KHITAGAKKVVMTGPacetylation[1, 2]
116HITAGAKKVVMTGPSacetylation[1, 2]
124VVMTGPSKDNTPMFVacetylation[1, 2]
132DNTPMFVKGANFDKYacetylation[1, 2, 3, 4]
138VKGANFDKYAGQDIVacetylation[1, 2, 3]
160NCLAPLAKVINDNFGacetylation[1]
184HATTATQKTVDGPSHacetylation[1, 2, 4]
192TVDGPSHKDWRGGRGacetylation[1, 2, 3, 4]
213PSSTGAAKAVGKVLPacetylation[1, 2]
217GAAKAVGKVLPELNGacetylation[1, 2]
225VLPELNGKLTGMAFRacetylation[1, 2]
249DLTVRLEKAATYEQIacetylation[1, 2, 3]
249DLTVRLEKAATYEQIpupylation[5]
257AATYEQIKAAVKAAAacetylation[1, 2]
261EQIKAAVKAAAEGEMacetylation[1, 2]
321NETGYSNKVLDLIAHacetylation[1, 2]
331DLIAHISK*******acetylation[1]
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]
 [5] Reconstitution of the Mycobacterium tuberculosis pupylation pathway in Escherichia coli.
 Cerda-Maira FA, McAllister F, Bode NJ, Burns KE, Gygi SP, Darwin KH.
 EMBO Rep. 2011 Jul 8;12(8):863-70. [PMID: 21738222
Functional Description
  
Sequence Annotation
 NP_BIND 12 13 NAD (By similarity).
 REGION 149 151 Glyceraldehyde 3-phosphate binding.
 REGION 209 210 Glyceraldehyde 3-phosphate binding.
 ACT_SITE 150 150 Nucleophile.
 BINDING 34 34 NAD.
 BINDING 78 78 NAD; via carbonyl oxygen.
 BINDING 180 180 Glyceraldehyde 3-phosphate.
 BINDING 232 232 Glyceraldehyde 3-phosphate.
 BINDING 314 314 NAD.
 MOD_RES 115 115 N6-succinyllysine.
 MOD_RES 124 124 N6-succinyllysine.
 MOD_RES 132 132 N6-acetyllysine; alternate.
 MOD_RES 132 132 N6-succinyllysine; alternate.
 MOD_RES 138 138 N6-acetyllysine.
 MOD_RES 192 192 N6-acetyllysine; alternate.
 MOD_RES 192 192 N6-succinyllysine; alternate.
 MOD_RES 213 213 N6-succinyllysine.
 MOD_RES 217 217 N6-succinyllysine.
 MOD_RES 225 225 N6-succinyllysine.
 MOD_RES 249 249 N6-acetyllysine.
 MOD_RES 249 249 N6-succinyllysine.
 MOD_RES 257 257 N6-succinyllysine.
 MOD_RES 261 261 N6-succinyllysine.
 MOD_RES 331 331 N6-malonyllysine; alternate.
 MOD_RES 331 331 N6-succinyllysine; alternate.  
Keyword
 3D-structure; Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing; Glycolysis; NAD; Oxidoreductase; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 331 AA 
Protein Sequence
MTIKVGINGF GRIGRIVFRA AQKRSDIEIV AINDLLDADY MAYMLKYDST HGRFDGTVEV 60
KDGHLIVNGK KIRVTAERDP ANLKWDEVGV DVVAEATGLF LTDETARKHI TAGAKKVVMT 120
GPSKDNTPMF VKGANFDKYA GQDIVSNASC TTNCLAPLAK VINDNFGIIE GLMTTVHATT 180
ATQKTVDGPS HKDWRGGRGA SQNIIPSSTG AAKAVGKVLP ELNGKLTGMA FRVPTPNVSV 240
VDLTVRLEKA ATYEQIKAAV KAAAEGEMKG VLGYTEDDVV STDFNGEVCT SVFDAKAGIA 300
LNDNFVKLVS WYDNETGYSN KVLDLIAHIS K 331 
Gene Ontology
 GO:0005829; C:cytosol; IDA:UniProtKB.
 GO:0016020; C:membrane; IDA:UniProtKB.
 GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; IEA:EC.
 GO:0051287; F:NAD binding; IEA:InterPro.
 GO:0050661; F:NADP binding; IEA:InterPro.
 GO:0006096; P:glycolysis; IEA:UniProtKB-UniPathway. 
Interpro
 IPR020831; GlycerAld/Erythrose_P_DH.
 IPR020830; GlycerAld_3-P_DH_AS.
 IPR020829; GlycerAld_3-P_DH_cat.
 IPR020828; GlycerAld_3-P_DH_NAD(P)-bd.
 IPR006424; Glyceraldehyde-3-P_DH_1.
 IPR016040; NAD(P)-bd_dom. 
Pfam
 PF02800; Gp_dh_C
 PF00044; Gp_dh_N 
SMART
 SM00846; Gp_dh_N 
PROSITE
 PS00071; GAPDH 
PRINTS
 PR00078; G3PDHDRGNASE.