CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-003157
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 D-erythrose-4-phosphate dehydrogenase 
Protein Synonyms/Alias
 E4PDH 
Gene Name
 epd 
Gene Synonyms/Alias
 gapB; b2927; JW2894 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
214SIIPVDTKLAAGITRacetylation[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
Functional Description
 Catalyzes the NAD-dependent conversion of D-erythrose 4- phosphate to 4-phosphoerythronate. 
Sequence Annotation
 NP_BIND 12 13 NAD (By similarity).
 REGION 154 156 Substrate binding (Potential).
 REGION 213 214 Substrate binding (Potential).
 ACT_SITE 155 155 Nucleophile (By similarity).
 BINDING 81 81 NAD; via carbonyl oxygen (By similarity).
 BINDING 200 200 Substrate (Potential).
 BINDING 236 236 Substrate (Potential).
 BINDING 318 318 NAD (By similarity).  
Keyword
 3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing; NAD; Oxidoreductase; Pyridoxine biosynthesis; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 339 AA 
Protein Sequence
MTVRVAINGF GRIGRNVVRA LYESGRRAEI TVVAINELAD AAGMAHLLKY DTSHGRFAWE 60
VRQERDQLFV GDDAIRVLHE RSLQSLPWRE LGVDVVLDCT GVYGSREHGE AHIAAGAKKV 120
LFSHPGSNDL DATVVYGVNQ DQLRAEHRIV SNASCTTNCI IPVIKLLDDA YGIESGTVTT 180
IHSAMHDQQV IDAYHPDLRR TRAASQSIIP VDTKLAAGIT RFFPQFNDRF EAIAVRVPTI 240
NVTAIDLSVT VKKPVKANEV NLLLQKAAQG AFHGIVDYTE LPLVSVDFNH DPHSAIVDGT 300
QTRVSGAHLI KTLVWCDNEW GFANRMLDTT LAMATVAFR 339 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0048001; F:erythrose-4-phosphate dehydrogenase activity; IDA:EcoCyc.
 GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; IDA:EcoCyc.
 GO:0051287; F:NAD binding; IDA:EcoCyc.
 GO:0006006; P:glucose metabolic process; IDA:EcoCyc.
 GO:0042823; P:pyridoxal phosphate biosynthetic process; IDA:EcoCyc.
 GO:0008615; P:pyridoxine biosynthetic process; IMP:EcoCyc. 
Interpro
 IPR006422; E4P_DH_bac.
 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.
 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.