Tag | Content |
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CPLM ID | CPLM-003568 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Riboflavin synthase |
Protein Synonyms/Alias | RS |
Gene Name | ribC |
Gene Synonyms/Alias | ribE; b1662; JW1654 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
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18 | KLVSIDEKPNFRTHV | acetylation | [1] | 77 | ITNLGDLKVGDWVNV | acetylation | [1] | 89 | VNVERAAKFSDEIGG | acetylation | [1] | 111 | MTTAEVAKILTSENN | acetylation | [1] | 124 | NNRQIWFKVQDSQLM | acetylation | [1] | 132 | VQDSQLMKYILYKGF | 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 dismutation of two molecules of 6,7- dimethyl-8-ribityllumazine, resulting in the formation of riboflavin and 5-amino-6-(D-ribitylamino)uracil. |
Sequence Annotation | REPEAT 1 97 Lumazine-binding 1. REPEAT 98 195 Lumazine-binding 2. REGION 4 6 Substrate binding. REGION 48 50 Substrate binding. REGION 62 67 Substrate binding. |
Keyword | 3D-structure; Complete proteome; Reference proteome; Repeat; Riboflavin biosynthesis; Transferase. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 213 AA |
Protein Sequence | MFTGIVQGTA KLVSIDEKPN FRTHVVELPD HMLDGLETGA SVAHNGCCLT VTEINGNHVS 60 FDLMKETLRI TNLGDLKVGD WVNVERAAKF SDEIGGHLMS GHIMTTAEVA KILTSENNRQ 120 IWFKVQDSQL MKYILYKGFI GIDGISLTVG EVTPTRFCVH LIPETLERTT LGKKKLGARV 180 NIEIDPQTQA VVDTVERVLA ARENAMNQPG TEA 213 |
Gene Ontology | GO:0016491; F:oxidoreductase activity; IEA:InterPro. GO:0004746; F:riboflavin synthase activity; IDA:EcoCyc. GO:0009231; P:riboflavin biosynthetic process; IDA:EcoCyc. |
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Pfam | |
SMART | |
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PRINTS | |