ACL_RS06540
  | Uniprot: A9NHT6
Description: GTP cyclohydrolase II EC number: 3.5.4.25 Annotation score: 2 out of 5 Miscellaneous [CC]: Protein existence: Inferred from homology Catalytic activity: CATALYTIC ACTIVITY: GTP + 3 H(2)O = formate + 2,5-diamino-6-hydroxy-4-(5-phospho-D-ribosylamino)pyrimidine + diphosphate. {ECO:0000256|SAAS:SAAS00483582}. Cofactor: COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|SAAS:SAAS00606994}; Enzyme regulation: Function [CC]: FUNCTION: Catalyzes the conversion of GTP to 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate (DARP), formate and pyrophosphate. {ECO:0000256|SAAS:SAAS00483603}. Pathway: PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-ribitylamino)uracil from GTP: step 1/4. {ECO:0000256|SAAS:SAAS00317943}. Active site: Binding site: Calcium binding: DNA binding: Metal binding: Nucleotide binding: Site: Gene names (primary): ribBA Gene names (synonym): Mass: 44,068 Subunit structure [CC]: Gene ontology (GO): 3,4-dihydroxy-2-butanone-4-phosphate synthase activity [GO:0008686]; GTP binding [GO:0005525]; GTP cyclohydrolase II activity [GO:0003935]; metal ion binding [GO:0046872]; riboflavin biosynthetic process [GO:0009231] Gene ontology IDs: GO:0003935; GO:0005525; GO:0008686; GO:0009231; GO:0046872 Chain: Signal peptide: Domain [CC]: Sequence similarities: SIMILARITY: In the C-terminal section; belongs to the GTP cyclohydrolase II family. {ECO:0000256|SAAS:SAAS00589376}.; SIMILARITY: In the N-terminal section; belongs to the DHBP synthase family. {ECO:0000256|SAAS:SAAS00534513}. Protein families: GTP cyclohydrolase II family; DHBP synthase family Coiled coil: Domain [FT]: DOMAIN 203 367 GTP_cyclohydro2. {ECO:0000259|Pfam:PF00925}. Motif: Region: EMBL: CP000896 ProteinModelPortal: A9NHT6 MEROPS: EnsemblBacteria KO: ABX81916 UniPathway: K14652 CDD: Gene3D: cd00641 HAMAP: 3.90.870.10 InterPro: MF_00179 PANTHER: IPR017945;IPR000422;IPR032677;IPR000926 PIRSF: PRINTS: PROSITE: Pfam: ProDom: PF00926;PF00925 SMART: SUPFAM: TIGRFAMs: SSF142695;SSF55821 |
1379455-1380646(-) >nucleotide sequence ATTTTTTTCATTATGATTTAAAATAATAGGTTCTCTTGAAGTAATCTCCAAGCCATATCC AGATAACCCAGATATTTTAAGTGGGTTATTCGTCATTAATCTAATTTTACCCACACCTAA ATCTTTAAGAATTTGAGCACCAATACCGTAATCTCTTAAGTCTTCTTCAAAACCTAATGC GATGTTAGCTTCTACAGTATCCATACCTAAATCTTGTAAGTGATATGCTTTAATCTTATT GATTAAACCAATACCACGTCCTTCTTGTCTCATGTAAAGAAGTACACCTTTGCCCGCTTT TTCGATGTTATCTAAAGCAGCTTGAAGCTGTTCACCACAATCACATTTAAGTGATCCAAA AGCATCACCTGTTAAACATTCAGAGTGTACACGTACTAATACTTCTTCACCTGGTTTAAT ATCACCTTTAACTAAGGCAACATGATGTTCACCACTAATGGCATTTTCAAAACCAACCAT TCTAAACTCACCATGTTTTGTAGGAAGCTTAGCCTCAGCTGCTTTTTTTACTAAACTTTC AGTCATTTGACGGTATCTAATAATAGATTCAACAGAAACGATTGGTAGTGCATGTTTTGT AGCAAATGCTATAATCTCATCCATCTTCATTGGTTGTTTATCTTTATTTAATAATAGTGA TAACACACCAACTGGTTTAAGATTAGCTAGTTCAGACAAATCTACGATAGCTTCAGGATG TGCAACTCTTTTTAAAGTACCTCCTAATCTCGTAATTAAAGGAAATACAACACCATTTTT ATGGTATTCCACTTTCTTCTTATTTAATACAGATTGGGTGGTTGCCAATATATTGGATGG ATCGTCTTTATGAGTATCAGTTAGTGAAATAGTAGTATCTTTAAAAGCGTGCATAGACCC AACTACTTCATAAACTGGATCAATGTTTAAACCTTCATAAAATTGTTTACTTGCAGCAAC ATAGATGTATTTATCACCATACTCTTTTAAAAAATTGATGTTCTCTAAGTTTAATTTTTC TGCATTAAAAATTAAACTCCCCGTATTTTGTAAATCATGATCATCTACAACAATGACAGG CTTACTCATCTTGATTGCTTCAATGATGGATTGTACAGTATTAAACTCCAT >protein sequence SKQFYEGLNIDPVYEVVGSMHAFKDTTISLTDTHKDDPSNILATTQSVLNKKKVEYHKNG VVFPLITRLGGTLKRVAHPEAIVDLSELANLKPVGVLSLLLNKDKQPMKMDEIIAFATKH ALPIVSVESIIRYRQMTESLVKKAAEAKLPTKHGEFRMVGFENAISGEHHVALVKGDIKP GEEVLVRVHSECLTGDAFGSLKCDCGEQLQAALDNIEKAGKGVLLYMRQEGRGIGLINKI KAYHLQDLGMDTVEANIALGFEEDLRDYGIGAQILKDLGVGKIRLMTNNPLKISGLSGYG LEITSREPIILNHNEKNEEYLRTKQKKMGHLLKYKD |
© Fisunov Lab of Proteomics, 2016.