ID A0A1V4AJZ3_9BACT Unreviewed; 399 AA. AC A0A1V4AJZ3; DT 07-JUN-2017, integrated into UniProtKB/TrEMBL. DT 07-JUN-2017, sequence version 1. DT 29-SEP-2021, entry version 23. DE RecName: Full=Riboflavin biosynthesis protein RibBA {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}; 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}; GN Name=ribBA {ECO:0000256|HAMAP-Rule:MF_01283}; GN ORFNames=B0D78_05955 {ECO:0000313|EMBL:OON89001.1}; OS Pyramidobacter sp. C12-8. OC Bacteria; Synergistetes; Synergistia; Synergistales; Synergistaceae; OC Pyramidobacter; unclassified Pyramidobacter. OX NCBI_TaxID=1943580 {ECO:0000313|EMBL:OON89001.1, ECO:0000313|Proteomes:UP000190264}; RN [1] {ECO:0000313|EMBL:OON89001.1, ECO:0000313|Proteomes:UP000190264} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C12-8 {ECO:0000313|EMBL:OON89001.1, RC ECO:0000313|Proteomes:UP000190264}; RA Kang S.; RT "Fluoroacetate degrading rumen bacteria."; RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the conversion of D-ribulose 5-phosphate to formate CC and 3,4-dihydroxy-2-butanone 4-phosphate. CC {ECO:0000256|ARBA:ARBA00002284, ECO:0000256|HAMAP-Rule:MF_01283}. 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: CC Reaction=D-ribulose 5-phosphate = (2S)-2-hydroxy-3-oxobutyl phosphate + CC formate + H(+); Xref=Rhea:RHEA:18457, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:15740, ChEBI:CHEBI:58121, ChEBI:CHEBI:58830; CC EC=4.1.99.12; Evidence={ECO:0000256|ARBA:ARBA00000141, CC ECO:0000256|HAMAP-Rule:MF_01283}; CC -!- CATALYTIC ACTIVITY: CC Reaction=GTP + 3 H2O = 2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)- CC pyrimidine + diphosphate + formate + 2 H(+); Xref=Rhea:RHEA:23704, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15740, CC ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:58614; EC=3.5.4.25; CC Evidence={ECO:0000256|ARBA:ARBA00000698, ECO:0000256|HAMAP- CC Rule:MF_01283}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01283}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01283}; CC Note=Binds 2 divalent metal cations per subunit. Magnesium or CC manganese. {ECO:0000256|HAMAP-Rule:MF_01283}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01283}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01283}; CC -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D- CC ribitylamino)uracil from GTP: step 1/4. {ECO:0000256|ARBA:ARBA00004853, CC ECO:0000256|HAMAP-Rule:MF_01283}. CC -!- SIMILARITY: In the C-terminal section; belongs to the GTP CC cyclohydrolase II family. {ECO:0000256|HAMAP-Rule:MF_01283}. CC -!- SIMILARITY: In the N-terminal section; belongs to the DHBP synthase CC family. {ECO:0000256|ARBA:ARBA00005520, ECO:0000256|HAMAP- CC Rule:MF_01283}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:OON89001.1}. 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; MUHX01000011; OON89001.1; -; Genomic_DNA. DR EnsemblBacteria; OON89001; OON89001; B0D78_05955. DR UniPathway; UPA00275; UER00400. DR Proteomes; UP000190264; 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; 3.40.50.10990; -; 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 GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP- KW Rule:MF_01283}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01283}; KW Lyase {ECO:0000256|HAMAP-Rule:MF_01283}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01283}; KW Manganese {ECO:0000256|HAMAP-Rule:MF_01283}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_01283}; Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_01283}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_01283}; KW Riboflavin biosynthesis {ECO:0000256|ARBA:ARBA00022619, ECO:0000256|HAMAP- KW Rule:MF_01283}; Zinc {ECO:0000256|HAMAP-Rule:MF_01283}. FT DOMAIN 208..373 FT /note="GTP_cyclohydro2" FT /evidence="ECO:0000259|Pfam:PF00925" FT NP_BIND 252..256 FT /note="GTP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT NP_BIND 295..297 FT /note="GTP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT REGION 1..201 FT /note="DHBP synthase" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT REGION 28..29 FT /note="D-ribulose 5-phosphate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT REGION 140..144 FT /note="D-ribulose 5-phosphate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT REGION 202..399 FT /note="GTP cyclohydrolase II" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT ACT_SITE 329 FT /note="Proton acceptor; for GTP cyclohydrolase activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT ACT_SITE 331 FT /note="Nucleophile; for GTP cyclohydrolase activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT METAL 29 FT /note="Magnesium or manganese 1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT METAL 29 FT /note="Magnesium or manganese 2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT METAL 143 FT /note="Magnesium or manganese 2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT METAL 257 FT /note="Zinc; catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT METAL 268 FT /note="Zinc; catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT METAL 270 FT /note="Zinc; catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT BINDING 33 FT /note="D-ribulose 5-phosphate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT BINDING 164 FT /note="D-ribulose 5-phosphate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT BINDING 273 FT /note="GTP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT BINDING 317 FT /note="GTP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT BINDING 352 FT /note="GTP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT BINDING 357 FT /note="GTP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT SITE 126 FT /note="Essential for DHBP synthase activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT SITE 164 FT /note="Essential for DHBP synthase activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" SQ SEQUENCE 399 AA; 44326 MW; 401BC096797ABF12 CRC64; MIQYNTVEEA AAELRAGKIV LVADDENREN EGDMICAAQF AGTENVNFMA RFARGLICMP MSAAYVKRLG LPQMVESNTD NHYTAFTVSI DHISTATGIS AVERGVTARA CVGDDAKPED FRRPGHMFPL LARPNGVLER NGHTEATVDL LRLAGLKECG LCCEVMRDDG GMMRAPELAE KAKEWGLKFI TIRAIQEYRK RHETFVERVA TTKMPTKYGF FTAYGYRNRL NGEHHVALVM GDVGDGRDVL CRVHSECLTG DTFGSLRCDC GQQFAAAMTQ IAAEGRGVML YLRQEGRGIG LLNKLRAYAL QDRGLDTVEA NLALGFEEDQ REYYIGAQIL RDLGVRTLRL LTNNPKKIEG LADFGLEIAA RVPIQMPATA NDLFYLQTKE HKMGHLVTY //