Tag | Content |
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CPLM ID | CPLM-003007 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | GTP cyclohydrolase-2 |
Protein Synonyms/Alias | GTP cyclohydrolase II |
Gene Name | ribA |
Gene Synonyms/Alias | b1277; JW1269 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
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101 | RNIGLLNKIRAYALQ | 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 conversion of GTP to 2,5-diamino-6- ribosylamino-4(3H)-pyrimidinone 5'-phosphate (DARP), formate and pyrophosphate. |
Sequence Annotation | NP_BIND 49 53 GTP. NP_BIND 92 94 GTP. ACT_SITE 126 126 Proton acceptor (Potential). ACT_SITE 128 128 Nucleophile. METAL 54 54 Zinc; catalytic. METAL 65 65 Zinc; catalytic. METAL 67 67 Zinc; catalytic. BINDING 70 70 GTP. BINDING 114 114 GTP. BINDING 149 149 GTP. BINDING 154 154 GTP. |
Keyword | 3D-structure; Complete proteome; Direct protein sequencing; GTP-binding; Hydrolase; Metal-binding; Nucleotide-binding; Reference proteome; Riboflavin biosynthesis; Zinc. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 196 AA |
Protein Sequence | MQLKRVAEAK LPTPWGDFLM VGFEELATGH DHVALVYGDI SGHTPVLARV HSECLTGDAL 60 FSLRCDCGFQ LEAALTQIAE EGRGILLYHR QEGRNIGLLN KIRAYALQDQ GYDTVEANHQ 120 LGFAADERDF TLCADMFKLL GVNEVRLLTN NPKKVEILTE AGINIVERVP LIVGRNPNNE 180 HYLDTKAEKM GHLLNK 196 |
Gene Ontology | GO:0005525; F:GTP binding; IEA:UniProtKB-KW. GO:0003935; F:GTP cyclohydrolase II activity; IDA:EcoCyc. GO:0008270; F:zinc ion binding; IEA:HAMAP. GO:0009231; P:riboflavin biosynthetic process; IEA:HAMAP. |
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