ID D1CIT3_THET1 Unreviewed; 407 AA. AC D1CIT3; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 19-JAN-2010, sequence version 1. DT 06-FEB-2013, entry version 24. DE SubName: Full=GTP cyclohydrolase II; DE EC=3.5.4.25; GN OrderedLocusNames=Tter_2767; OS Thermobaculum terrenum (strain ATCC BAA-798 / YNP1). OC Bacteria; Thermobaculum. OX NCBI_TaxID=525904; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-798 / YNP1; RX DOI=10.4056/sigs.1153107; RA Kiss H., Cleland D., Lapidus A., Lucas S., Glavina Del Rio T., RA Nolan M., Tice H., Han C., Goodwin L., Pitluck S., Liolios K., RA Ivanova N., Mavromatis K., Ovchinnikova G., Pati A., Chen A., RA Palaniappan K., Land M., Hauser L., Chang Y., Jeffries C., Lu M., RA Brettin T., Detter J., Goker M., Tindall B., Beck B., McDermott T., RA Woyke T., Bristow J., Eisen J., Markowitz V., Hugenholtz P., RA Kyrpides N., Klenk H., Cheng J.; RT "Complete genome sequence of Thermobaculum terrenum type strain RT (YNP1T)."; RL Stand. Genomic Sci. 3:153-162(2010). CC -!- FUNCTION: Catalyzes the conversion of D-ribulose 5-phosphate to CC formate and 3,4-dihydroxy-2-butanone 4-phosphate (By similarity). CC -!- FUNCTION: Catalyzes the conversion of GTP to 2,5-diamino-6- CC ribosylamino-4(3H)-pyrimidinone 5'-phosphate (DARP), formate and CC pyrophosphate (By similarity). CC -!- CATALYTIC ACTIVITY: D-ribulose 5-phosphate = formate + L-3,4- CC dihydroxybutan-2-one 4-phosphate. CC -!- CATALYTIC ACTIVITY: GTP + 3 H(2)O = formate + 2,5-diamino-6- CC hydroxy-4-(5-phospho-D-ribosylamino)pyrimidine + diphosphate. CC -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity). CC -!- COFACTOR: Binds 2 divalent metal cations per subunit. Magnesium or CC manganese (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 2- CC hydroxy-3-oxobutyl phosphate from D-ribulose 5-phosphate: step CC 1/1. CC -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino- CC 6-(D-ribitylamino)uracil from GTP: step 1/4. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP001826; ACZ43653.1; -; Genomic_DNA. DR RefSeq; YP_003324476.1; NC_013526.1. DR GeneID; 8640796; -. DR GenomeReviews; CP001826_GR; Tter_2767. DR KEGG; ttr:Tter_2767; -. DR PATRIC; 32505981; VBITheTer68767_2950. DR HOGENOM; HOG000115440; -. DR KO; K14652; -. DR OMA; LRCDCRM; -. DR UniPathway; UPA00275; UER00399. DR GO; GO:0008686; F:3,4-dihydroxy-2-butanone-4-phosphate synthase activity; IEA:InterPro. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0003935; F:GTP cyclohydrolase II activity; IEA:EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0009231; P:riboflavin biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.90.870.10; DHBP_synth_RibB-like_a/b_dom; 1. DR HAMAP; MF_00179; RibA; 1; -. DR HAMAP; MF_00180; RibB; 1; -. DR HAMAP; MF_01283; RibBA; 1; -. DR InterPro; IPR017945; DHBP_synth_RibB-like_a/b_dom. DR InterPro; IPR000422; DHBP_synthase_RibB. DR InterPro; IPR000926; GTP_CycHdrlaseII_RibA. DR InterPro; IPR016299; Riboflavin_synth_RibBA. DR Pfam; PF00926; DHBP_synthase; 1. DR Pfam; PF00925; GTP_cyclohydro2; 1. DR PIRSF; PIRSF001259; RibA; 1. DR SUPFAM; SSF55821; DHBP_synth_RibB-like_a/b_dom; 1. DR TIGRFAMs; TIGR00505; ribA; 1. DR TIGRFAMs; TIGR00506; ribB; 1. PE 3: Inferred from homology; KW Complete proteome; GTP-binding; Hydrolase; Lyase; Magnesium; KW Manganese; Metal-binding; Multifunctional enzyme; Nucleotide-binding; KW Riboflavin biosynthesis; Zinc. SQ SEQUENCE 407 AA; 44349 MW; F253C847500A2D21 CRC64; MTGSKIQQAL DELRAGRFVV VVDDESRERE ADLVLAAQHA TPAAINFMAR EACGLICVAM HGRRMDQLGI PPMVSPENNT SAHGTAFGVP VDAASGITTG ISAYDRAHTI RLLADPSSTP GDFIMPGHVF PLRAREGGVL ERRGHTEAAV DLMVMAGLQP VAAICEIMAP NGRMAWGEEL EEFAHRHNLM LVTVQEVADA RAAESEGTLG KVRPVKLPTS HGEFTLVAYT APDSREPHLA LIHGDPGSSP LVRLHSECFT GDVLGSERCD CGPQLDRALQ MIAAQGGILL YLRQEGRGIG LLNKLRAYAL QDEGLDTVEA NEHLGFQPDE RDYAVAAEIL RDLGVSSVRL LTNNPRKIEG LRAHGIEVVE RVPLEVPPRR HNLRYLQTKK LKLGHWLQLH PPIGEQR //