Tag | Content |
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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 |
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214 | SIIPVDTKLAAGITR | acetylation | [1] |
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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. |
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