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
TTAATCTTTATACTTTAGAAGATGACCCATTTTCTTTTGTTTAGTTCTTAGGTATTCTTC
ATTTTTTTCATTATGATTTAAAATAATAGGTTCTCTTGAAGTAATCTCCAAGCCATATCC
AGATAACCCAGATATTTTAAGTGGGTTATTCGTCATTAATCTAATTTTACCCACACCTAA
ATCTTTAAGAATTTGAGCACCAATACCGTAATCTCTTAAGTCTTCTTCAAAACCTAATGC
GATGTTAGCTTCTACAGTATCCATACCTAAATCTTGTAAGTGATATGCTTTAATCTTATT
GATTAAACCAATACCACGTCCTTCTTGTCTCATGTAAAGAAGTACACCTTTGCCCGCTTT
TTCGATGTTATCTAAAGCAGCTTGAAGCTGTTCACCACAATCACATTTAAGTGATCCAAA
AGCATCACCTGTTAAACATTCAGAGTGTACACGTACTAATACTTCTTCACCTGGTTTAAT
ATCACCTTTAACTAAGGCAACATGATGTTCACCACTAATGGCATTTTCAAAACCAACCAT
TCTAAACTCACCATGTTTTGTAGGAAGCTTAGCCTCAGCTGCTTTTTTTACTAAACTTTC
AGTCATTTGACGGTATCTAATAATAGATTCAACAGAAACGATTGGTAGTGCATGTTTTGT
AGCAAATGCTATAATCTCATCCATCTTCATTGGTTGTTTATCTTTATTTAATAATAGTGA
TAACACACCAACTGGTTTAAGATTAGCTAGTTCAGACAAATCTACGATAGCTTCAGGATG
TGCAACTCTTTTTAAAGTACCTCCTAATCTCGTAATTAAAGGAAATACAACACCATTTTT
ATGGTATTCCACTTTCTTCTTATTTAATACAGATTGGGTGGTTGCCAATATATTGGATGG
ATCGTCTTTATGAGTATCAGTTAGTGAAATAGTAGTATCTTTAAAAGCGTGCATAGACCC
AACTACTTCATAAACTGGATCAATGTTTAAACCTTCATAAAATTGTTTACTTGCAGCAAC
ATAGATGTATTTATCACCATACTCTTTTAAAAAATTGATGTTCTCTAAGTTTAATTTTTC
TGCATTAAAAATTAAACTCCCCGTATTTTGTAAATCATGATCATCTACAACAATGACAGG
CTTACTCATCTTGATTGCTTCAATGATGGATTGTACAGTATTAAACTCCAT


>protein sequence
MEFNTVQSIIEAIKMSKPVIVVDDHDLQNTGSLIFNAEKLNLENINFLKEYGDKYIYVAA
SKQFYEGLNIDPVYEVVGSMHAFKDTTISLTDTHKDDPSNILATTQSVLNKKKVEYHKNG
VVFPLITRLGGTLKRVAHPEAIVDLSELANLKPVGVLSLLLNKDKQPMKMDEIIAFATKH
ALPIVSVESIIRYRQMTESLVKKAAEAKLPTKHGEFRMVGFENAISGEHHVALVKGDIKP
GEEVLVRVHSECLTGDAFGSLKCDCGEQLQAALDNIEKAGKGVLLYMRQEGRGIGLINKI
KAYHLQDLGMDTVEANIALGFEEDLRDYGIGAQILKDLGVGKIRLMTNNPLKISGLSGYG
LEITSREPIILNHNEKNEEYLRTKQKKMGHLLKYKD






















© Fisunov Lab of Proteomics, 2016.