ID A0A2A7H4I0_9BACI Unreviewed; 397 AA. AC A0A2A7H4I0; DT 20-DEC-2017, integrated into UniProtKB/TrEMBL. DT 20-DEC-2017, sequence version 1. DT 28-FEB-2018, entry version 3. DE RecName: Full=Riboflavin biosynthesis protein RibBA {ECO:0000256|HAMAP-Rule:MF_01283}; DE Includes: DE RecName: Full=GTP cyclohydrolase-2 {ECO:0000256|HAMAP-Rule:MF_01283}; DE EC=3.5.4.25 {ECO:0000256|HAMAP-Rule:MF_01283}; DE AltName: Full=GTP cyclohydrolase II {ECO:0000256|HAMAP-Rule:MF_01283}; DE Includes: DE RecName: Full=3,4-dihydroxy-2-butanone 4-phosphate synthase {ECO:0000256|HAMAP-Rule:MF_01283}; DE Short=DHBP synthase {ECO:0000256|HAMAP-Rule:MF_01283}; DE EC=4.1.99.12 {ECO:0000256|HAMAP-Rule:MF_01283}; GN Name=ribBA {ECO:0000256|HAMAP-Rule:MF_01283}; GN ORFNames=COO03_08555 {ECO:0000313|EMBL:PEB53210.1}; OS Bacillus sp. AFS098217. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=2033868 {ECO:0000313|EMBL:PEB53210.1, ECO:0000313|Proteomes:UP000220707}; RN [1] {ECO:0000313|EMBL:PEB53210.1, ECO:0000313|Proteomes:UP000220707} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AFS098217 {ECO:0000313|EMBL:PEB53210.1, RC ECO:0000313|Proteomes:UP000220707}; RG Agbiome Team Llc; RA Bleich R.M., Grubbs K.J., Santa Maria K.C., Allen S.E., Farag S., RA Shank E.A., Bowers A.; RT "Large-scale bioinformatics analysis of Bacillus genomes uncovers RT conserved roles of natural products in bacterial physiology."; RL Submitted (SEP-2017) 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. CC {ECO:0000256|HAMAP-Rule:MF_01283, ECO:0000256|SAAS:SAAS00739193}. CC -!- FUNCTION: Catalyzes the conversion of GTP to 2,5-diamino-6- CC ribosylamino-4(3H)-pyrimidinone 5'-phosphate (DARP), formate and CC pyrophosphate. {ECO:0000256|HAMAP-Rule:MF_01283}. CC -!- CATALYTIC ACTIVITY: D-ribulose 5-phosphate = formate + L-3,4- CC dihydroxybutan-2-one 4-phosphate. {ECO:0000256|HAMAP- CC Rule:MF_01283}. CC -!- CATALYTIC ACTIVITY: GTP + 3 H(2)O = formate + 2,5-diamino-6- CC hydroxy-4-(5-phospho-D-ribosylamino)pyrimidine + diphosphate. CC {ECO:0000256|HAMAP-Rule:MF_01283, ECO:0000256|SAAS:SAAS00711742}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01283}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01283}; CC Note=Binds 2 divalent metal cations per subunit. Magnesium or CC manganese. {ECO:0000256|HAMAP-Rule:MF_01283}; CC -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 2- CC hydroxy-3-oxobutyl phosphate from D-ribulose 5-phosphate: step CC 1/1. {ECO:0000256|HAMAP-Rule:MF_01283}. CC -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino- CC 6-(D-ribitylamino)uracil from GTP: step 1/4. CC {ECO:0000256|SAAS:SAAS00711724}. CC -!- SIMILARITY: In the C-terminal section; belongs to the GTP CC cyclohydrolase II family. {ECO:0000256|HAMAP-Rule:MF_01283, CC ECO:0000256|SAAS:SAAS00789992}. CC -!- SIMILARITY: In the N-terminal section; belongs to the DHBP CC synthase family. {ECO:0000256|HAMAP-Rule:MF_01283, CC ECO:0000256|SAAS:SAAS00534513}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:PEB53210.1}. 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; NVPR01000032; PEB53210.1; -; Genomic_DNA. DR UniPathway; UPA00275; UER00399. DR Proteomes; UP000220707; Unassembled WGS sequence. DR GO; GO:0008686; F:3,4-dihydroxy-2-butanone-4-phosphate synthase activity; IEA:UniProtKB-UniRule. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0003935; F:GTP cyclohydrolase II activity; IEA:UniProtKB-UniRule. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0009231; P:riboflavin biosynthetic process; IEA:UniProtKB-UniRule. DR CDD; cd00641; GTP_cyclohydro2; 1. 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; IPR032677; GTP_cyclohydro_II. DR InterPro; IPR000926; RibA. DR InterPro; IPR036144; RibA-like_sf. DR InterPro; IPR016299; Riboflavin_synth_RibBA. DR Pfam; PF00926; DHBP_synthase; 1. DR Pfam; PF00925; GTP_cyclohydro2; 1. DR SUPFAM; SSF142695; SSF142695; 1. DR SUPFAM; SSF55821; SSF55821; 1. DR TIGRFAMs; TIGR00505; ribA; 1. DR TIGRFAMs; TIGR00506; ribB; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000220707}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_01283, KW ECO:0000256|SAAS:SAAS00711691}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01283, KW ECO:0000313|EMBL:PEB53210.1}; KW Lyase {ECO:0000256|HAMAP-Rule:MF_01283, KW ECO:0000256|SAAS:SAAS00711664}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01283}; KW Manganese {ECO:0000256|HAMAP-Rule:MF_01283}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01283, KW ECO:0000256|SAAS:SAAS00037896}; KW Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_01283}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01283, KW ECO:0000256|SAAS:SAAS00711707}; KW Riboflavin biosynthesis {ECO:0000256|HAMAP-Rule:MF_01283, KW ECO:0000256|SAAS:SAAS00037880}; KW Zinc {ECO:0000256|HAMAP-Rule:MF_01283, ECO:0000256|SAAS:SAAS00711685}. FT DOMAIN 206 371 GTP_cyclohydro2. {ECO:0000259|Pfam: FT PF00925}. FT NP_BIND 250 254 GTP. {ECO:0000256|HAMAP-Rule:MF_01283}. FT NP_BIND 293 295 GTP. {ECO:0000256|HAMAP-Rule:MF_01283}. FT REGION 1 199 DHBP synthase. {ECO:0000256|HAMAP-Rule: FT MF_01283}. FT REGION 26 27 D-ribulose 5-phosphate binding. FT {ECO:0000256|HAMAP-Rule:MF_01283}. FT REGION 138 142 D-ribulose 5-phosphate binding. FT {ECO:0000256|HAMAP-Rule:MF_01283}. FT REGION 200 397 GTP cyclohydrolase II. FT {ECO:0000256|HAMAP-Rule:MF_01283}. FT ACT_SITE 327 327 Proton acceptor; for GTP cyclohydrolase FT activity. {ECO:0000256|HAMAP-Rule: FT MF_01283}. FT ACT_SITE 329 329 Nucleophile; for GTP cyclohydrolase FT activity. {ECO:0000256|HAMAP-Rule: FT MF_01283}. FT METAL 27 27 Magnesium or manganese 1. FT {ECO:0000256|HAMAP-Rule:MF_01283}. FT METAL 27 27 Magnesium or manganese 2. FT {ECO:0000256|HAMAP-Rule:MF_01283}. FT METAL 141 141 Magnesium or manganese 2. FT {ECO:0000256|HAMAP-Rule:MF_01283}. FT METAL 255 255 Zinc; catalytic. {ECO:0000256|HAMAP-Rule: FT MF_01283}. FT METAL 266 266 Zinc; catalytic. {ECO:0000256|HAMAP-Rule: FT MF_01283}. FT METAL 268 268 Zinc; catalytic. {ECO:0000256|HAMAP-Rule: FT MF_01283}. FT BINDING 31 31 D-ribulose 5-phosphate. FT {ECO:0000256|HAMAP-Rule:MF_01283}. FT BINDING 162 162 D-ribulose 5-phosphate. FT {ECO:0000256|HAMAP-Rule:MF_01283}. FT BINDING 271 271 GTP. {ECO:0000256|HAMAP-Rule:MF_01283}. FT BINDING 315 315 GTP. {ECO:0000256|HAMAP-Rule:MF_01283}. FT BINDING 350 350 GTP. {ECO:0000256|HAMAP-Rule:MF_01283}. FT BINDING 355 355 GTP. {ECO:0000256|HAMAP-Rule:MF_01283}. FT SITE 124 124 Essential for DHBP synthase activity. FT {ECO:0000256|HAMAP-Rule:MF_01283}. FT SITE 162 162 Essential for DHBP synthase activity. FT {ECO:0000256|HAMAP-Rule:MF_01283}. SQ SEQUENCE 397 AA; 44146 MW; 7CDA12078AC12D97 CRC64; MFHRIEEALE DLKQGKVVIV CDDENRENEG DFIALAEYIT PETINFMITH GRGLVCVPIT EQYAERLQLE PMVSHNTDSH HTAFTVSIDH ISTTTGISAH ERAATVRELL NPASKGSDFN RPGHIFPLIA KDGGVLRRAG HTEAAVDLAK LCGAEPAGVI CEIINEDGTM ARVADLFQVA KQFDIKMITI EDLIAYRRHH ETLVTREVEI TLPTDFGTFH AIGYSNSLDQ KEHIALVKGE ISTDEPVLVR VHSECLTGDV FGSCRCDCGP QLHAALAQIE REGKGVLLYM RQEGRGIGLL NKLRAYKLQE KGLDTVEANE KLGFPADLRD YGIGAQILKE LGLQKLRLLT NNPRKIAGLQ GYELEVVERV PLQMPTKEEN KTYLQTKVKK LGHLLNL //