CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005413
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Riboflavin biosynthesis protein RibD 
Protein Synonyms/Alias
 Diaminohydroxyphosphoribosylaminopyrimidine deaminase; DRAP deaminase; Riboflavin-specific deaminase; 5-amino-6-(5-phosphoribosylamino)uracil reductase; HTP reductase 
Gene Name
 ribD 
Gene Synonyms/Alias
 ribG; ybaE; b0414; JW0404 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
276TLLIPEHKGHLDLVVacetylation[1]
341CTLPGLEKLADAPQFacetylation[1]
349LADAPQFKFKEIRHVacetylation[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
 Converts 2,5-diamino-6-(ribosylamino)-4(3h)-pyrimidinone 5'-phosphate into 5-amino-6-(ribosylamino)-2,4(1h,3h)- pyrimidinedione 5'-phosphate. 
Sequence Annotation
 NP_BIND 161 164 NADP.
 NP_BIND 301 304 NADP.
 REGION 1 145 Deaminase.
 REGION 146 367 Reductase.
 ACT_SITE 52 52 Proton donor (By similarity).
 METAL 50 50 Zinc; catalytic (By similarity).
 METAL 75 75 Zinc; catalytic (By similarity).
 METAL 84 84 Zinc; catalytic (By similarity).
 BINDING 168 168 Substrate.
 BINDING 170 170 NADP.
 BINDING 184 184 Substrate.
 BINDING 196 196 NADP.
 BINDING 200 200 NADP.
 BINDING 204 204 Substrate; via amide nitrogen.
 BINDING 207 207 Substrate.
 BINDING 234 234 NADP.
 BINDING 299 299 Substrate.  
Keyword
 3D-structure; Complete proteome; Hydrolase; Metal-binding; Multifunctional enzyme; NADP; Oxidoreductase; Reference proteome; Riboflavin biosynthesis; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 367 AA 
Protein Sequence
MQDEYYMARA LKLAQRGRFT THPNPNVGCV IVKDGEIVGE GYHQRAGEPH AEVHALRMAG 60
EKAKGATAYV TLEPCSHHGR TPPCCDALIA AGVARVVASM QDPNPQVAGR GLYRLQQAGI 120
DVSHGLMMSE AEQLNKGFLK RMRTGFPYIQ LKLGASLDGR TAMASGESQW ITSPQARRDV 180
QLLRAQSHAI LTSSATVLAD DPALTVRWSE LDEQTQALYP QQNLRQPIRI VIDSQNRVTP 240
VHRIVQQPGE TWFARTQEDS REWPETVRTL LIPEHKGHLD LVVLMMQLGK QQINSIWVEA 300
GPTLAGALLQ AGLVDELIVY IAPKLLGSDA RGLCTLPGLE KLADAPQFKF KEIRHVGPDV 360
CLHLVGA 367 
Gene Ontology
 GO:0008703; F:5-amino-6-(5-phosphoribosylamino)uracil reductase activity; IDA:EcoCyc.
 GO:0008835; F:diaminohydroxyphosphoribosylaminopyrimidine deaminase activity; IDA:EcoCyc.
 GO:0050661; F:NADP binding; IDA:EcoCyc.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0009231; P:riboflavin biosynthetic process; IDA:EcoCyc. 
Interpro
 IPR016192; APOBEC/CMP_deaminase_Zn-bd.
 IPR002125; CMP_dCMP_Zn-bd.
 IPR016193; Cytidine_deaminase-like.
 IPR024072; DHFR-like_dom.
 IPR004794; Eubact_RibD.
 IPR011549; RibD_C.
 IPR002734; RibDG_C. 
Pfam
 PF00383; dCMP_cyt_deam_1
 PF01872; RibD_C 
SMART
  
PROSITE
 PS00903; CYT_DCMP_DEAMINASES 
PRINTS