Tag | Content |
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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 |
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276 | TLLIPEHKGHLDLVV | acetylation | [1] | 341 | CTLPGLEKLADAPQF | acetylation | [1] | 349 | LADAPQFKFKEIRHV | 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 | 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. |
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