ID D2QU60_SPILD Unreviewed; 432 AA. AC D2QU60; DT 02-MAR-2010, integrated into UniProtKB/TrEMBL. DT 02-MAR-2010, sequence version 1. DT 06-MAR-2013, entry version 25. DE SubName: Full=3,4-dihydroxy-2-butanone 4-phosphate synthase; GN OrderedLocusNames=Slin_6384; OS Spirosoma linguale (strain ATCC 33905 / DSM 74 / LMG 10896). OC Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Cytophagaceae; OC Spirosoma. OX NCBI_TaxID=504472; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33905 / DSM 74 / LMG 10896; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., RA Mikhailova N., Ovchinnikova G., Saunders E., Brettin T., Detter J.C., RA Han C., Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., RA Hugenholtz P., Woyke T., Wu D., Tindal B., Schutze A., Schneider S., RA Goker M., Klenk H.-P., Eisen J.A.; RT "The complete chromosome of Spirosoma linguale DSM 74."; RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases. 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; CP001769; ADB42342.1; -; Genomic_DNA. DR RefSeq; YP_003391141.1; NC_013730.1. DR GeneID; 8730168; -. DR GenomeReviews; CP001769_GR; Slin_6384. DR KEGG; sli:Slin_6384; -. DR PATRIC; 32442695; VBISpiLin97822_6349. DR HOGENOM; HOG000115440; -. DR KO; K14652; -. DR OMA; NIDPFIS; -. DR BioCyc; SLIN504472:GHKB-6871-MONOMER; -. 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:InterPro. 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; -; 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 432 AA; 47621 MW; 2103DF9F08ED4892 CRC64; MMSNNSTNSE INSANEENPA ESNPIRLDRI EDAIADIKAG KIVLVVDDED RENEGDMICA AEMITPEMVN FMVREARGLM CAPLTQERCD ELGLDMMVTS NTSVHTTPFT VSVDLLGNGC TTGISASDRS KTIQALVDPN TTPDDLGRPG HIFPLRAVEG GVIRRAGHTE AAVDLAKLAG LSPVGVLIEV LNEDGTMARL PELRVLADRF GMRLVSIQDL IAYRLRTETL IRREIGVDMP TQWGHFDLIA YKQSNTGDTH LALVKGTWEP NEPVMVRVHS SCVTGDIFGS CRCDCGPQLH AAMELVEKEG KGVVVYMFQE GRGIGLINKL KAYKLQEMGR DTVEANLDLG LPMDARDYGV GAQILRDLGI RKLRLISNNP KKRAGLMGYG LEIVDTVPLE IKSNPHNERY LRTKRDKMGH TIMNEPVNEE QE //