CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002979
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Pyridoxine 5'-phosphate synthase 
Protein Synonyms/Alias
 PNP synthase 
Gene Name
 pdxJ 
Gene Synonyms/Alias
 b2564; JW2548 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
97FCCLVPEKRQEVTTEacetylation[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 complicated ring closure reaction between the two acyclic compounds 1-deoxy-D-xylulose-5-phosphate (DXP) and 3-amino-2-oxopropyl phosphate (1-amino-acetone-3-phosphate or AAP) to form pyridoxine 5'-phosphate (PNP) and inorganic phosphate. 
Sequence Annotation
 REGION 11 12 1-deoxy-D-xylulose 5-phosphate binding.
 REGION 215 216 3-amino-2-oxopropyl phosphate binding.
 ACT_SITE 45 45 Proton acceptor.
 ACT_SITE 72 72 Proton acceptor.
 ACT_SITE 193 193 Proton donor.
 BINDING 9 9 3-amino-2-oxopropyl phosphate.
 BINDING 20 20 3-amino-2-oxopropyl phosphate.
 BINDING 47 47 1-deoxy-D-xylulose 5-phosphate.
 BINDING 52 52 1-deoxy-D-xylulose 5-phosphate.
 BINDING 102 102 1-deoxy-D-xylulose 5-phosphate.
 BINDING 194 194 3-amino-2-oxopropyl phosphate; via amide  
Keyword
 3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing; Pyridoxine biosynthesis; Reference proteome; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 243 AA 
Protein Sequence
MAELLLGVNI DHIATLRNAR GTAYPDPVQA AFIAEQAGAD GITVHLREDR RHITDRDVRI 60
LRQTLDTRMN LEMAVTEEML AIAVETKPHF CCLVPEKRQE VTTEGGLDVA GQRDKMRDAC 120
KRLADAGIQV SLFIDADEEQ IKAAAEVGAP FIEIHTGCYA DAKTDAEQAQ ELARIAKAAT 180
FAASLGLKVN AGHGLTYHNV KAIAAIPEMH ELNIGHAIIG RAVMTGLKDA VAEMKRLMLE 240
ARG 243 
Gene Ontology
 GO:0005829; C:cytosol; IDA:UniProtKB.
 GO:0033856; F:pyridoxine 5'-phosphate synthase activity; IDA:EcoCyc.
 GO:0008615; P:pyridoxine biosynthetic process; IMP:EcoliWiki. 
Interpro
 IPR013785; Aldolase_TIM.
 IPR004569; PyrdxlP_synth_PdxJ. 
Pfam
 PF03740; PdxJ 
SMART
  
PROSITE
  
PRINTS