CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-003008
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 3,4-dihydroxy-2-butanone 4-phosphate synthase 
Protein Synonyms/Alias
 DHBP synthase 
Gene Name
 ribB 
Gene Synonyms/Alias
 htrP; b3041; JW3009 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
127AAIADGAKPSDLNRPacetylation[1]
194ECIEFANKHNMALVTacetylation[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 conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate. 
Sequence Annotation
 REGION 37 38 Substrate binding (By similarity).
 REGION 150 154 Substrate binding (By similarity).
 METAL 38 38 Magnesium or manganese 1 (By similarity).
 METAL 38 38 Magnesium or manganese 2 (By similarity).
 METAL 153 153 Magnesium or manganese 2 (By similarity).
 BINDING 42 42 Substrate (By similarity).
 BINDING 174 174 Substrate (By similarity).  
Keyword
 3D-structure; Cell membrane; Complete proteome; Direct protein sequencing; Lyase; Magnesium; Manganese; Membrane; Metal-binding; Reference proteome; Riboflavin biosynthesis; Stress response. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 217 AA 
Protein Sequence
MNQTLLSSFG TPFERVENAL AALREGRGVM VLDDEDRENE GDMIFPAETM TVEQMALTIR 60
HGSGIVCLCI TEDRRKQLDL PMMVENNTSA YGTGFTVTIE AAEGVTTGVS AADRITTVRA 120
AIADGAKPSD LNRPGHVFPL RAQAGGVLTR GGHTEATIDL MTLAGFKPAG VLCELTNDDG 180
TMARAPECIE FANKHNMALV TIEDLVAYRQ AHERKAS 217 
Gene Ontology
 GO:0005829; C:cytosol; IDA:UniProtKB.
 GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
 GO:0008686; F:3,4-dihydroxy-2-butanone-4-phosphate synthase activity; IDA:EcoCyc.
 GO:0000287; F:magnesium ion binding; IDA:EcoCyc.
 GO:0030145; F:manganese ion binding; IEA:HAMAP.
 GO:0006950; P:response to stress; IEA:UniProtKB-KW.
 GO:0009231; P:riboflavin biosynthetic process; IEA:HAMAP. 
Interpro
 IPR017945; DHBP_synth_RibB-like_a/b_dom.
 IPR000422; DHBP_synthase_RibB. 
Pfam
 PF00926; DHBP_synthase 
SMART
  
PROSITE
  
PRINTS