ID A0A1E9HN18_9MICO Unreviewed; 432 AA. AC A0A1E9HN18; DT 18-JAN-2017, integrated into UniProtKB/TrEMBL. DT 18-JAN-2017, sequence version 1. DT 22-FEB-2023, entry version 30. DE RecName: Full=3,4-dihydroxy-2-butanone 4-phosphate synthase {ECO:0000256|HAMAP-Rule:MF_00180}; DE Short=DHBP synthase {ECO:0000256|HAMAP-Rule:MF_00180}; DE EC=4.1.99.12 {ECO:0000256|HAMAP-Rule:MF_00180}; GN Name=ribB {ECO:0000256|HAMAP-Rule:MF_00180}; GN ORFNames=HMPREF2757_08920 {ECO:0000313|EMBL:OFL68009.1}; OS Brevibacterium sp. HMSC063G07. OC Bacteria; Actinobacteria; Micrococcales; Brevibacteriaceae; Brevibacterium. OX NCBI_TaxID=1739261 {ECO:0000313|EMBL:OFL68009.1, ECO:0000313|Proteomes:UP000242868}; RN [1] {ECO:0000313|EMBL:OFL68009.1, ECO:0000313|Proteomes:UP000242868} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HMSC063G07 {ECO:0000313|EMBL:OFL68009.1, RC ECO:0000313|Proteomes:UP000242868}; RA Wen L., He K., Yang H.; RL Submitted (FEB-2016) 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_00180}. 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_00180}; CC -!- CATALYTIC ACTIVITY: CC Reaction=GTP + 4 H2O = 2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)- CC pyrimidine + formate + 3 H(+) + 2 phosphate; Xref=Rhea:RHEA:23704, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15740, CC ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58614; EC=3.5.4.25; CC Evidence={ECO:0000256|ARBA:ARBA00029293}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00180}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00180}; CC Note=Binds 2 divalent metal cations per subunit. Magnesium or CC manganese. {ECO:0000256|HAMAP-Rule:MF_00180}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|ARBA:ARBA00001947}; CC -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 2-hydroxy-3- CC oxobutyl phosphate from D-ribulose 5-phosphate: step 1/1. CC {ECO:0000256|ARBA:ARBA00004904, ECO:0000256|HAMAP-Rule:MF_00180}. CC -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D- CC ribitylamino)uracil from GTP: step 1/4. CC {ECO:0000256|ARBA:ARBA00004853}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00180}. CC -!- SIMILARITY: Belongs to the DHBP synthase family. {ECO:0000256|HAMAP- CC Rule:MF_00180}. CC -!- SIMILARITY: In the N-terminal section; belongs to the DHBP synthase CC family. {ECO:0000256|ARBA:ARBA00005520}. 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:OFL68009.1}. 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; LTHM01000009; OFL68009.1; -; Genomic_DNA. DR RefSeq; WP_070575623.1; NZ_KV802363.1. DR AlphaFoldDB; A0A1E9HN18; -. DR STRING; 1739261.HMPREF2757_08920; -. DR EnsemblBacteria; OFL68009; OFL68009; HMPREF2757_08920. DR OrthoDB; 9793111at2; -. DR UniPathway; UPA00275; UER00399. DR Proteomes; UP000242868; 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-EC. 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:0009231; P:riboflavin biosynthetic process; IEA:UniProtKB-UniRule. DR CDD; cd00641; GTP_cyclohydro2; 1. DR Gene3D; 3.90.870.10; DHBP synthase; 1. DR Gene3D; 3.40.50.10990; GTP cyclohydrolase II; 1. DR HAMAP; MF_00180; RibB; 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 PANTHER; PTHR21327:SF18; 3,4-DIHYDROXY-2-BUTANONE 4-PHOSPHATE SYNTHASE; 1. DR PANTHER; PTHR21327; GTP CYCLOHYDROLASE II-RELATED; 1. DR Pfam; PF00926; DHBP_synthase; 1. DR Pfam; PF00925; GTP_cyclohydro2; 1. DR PIRSF; PIRSF001259; RibA; 2. DR SUPFAM; SSF142695; RibA-like; 1. DR SUPFAM; SSF55821; YrdC/RibB; 1. DR TIGRFAMs; TIGR00505; ribA; 1. DR TIGRFAMs; TIGR00506; ribB; 1. PE 3: Inferred from homology; KW GTP-binding {ECO:0000256|ARBA:ARBA00023134}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:OFL68009.1}; KW Lyase {ECO:0000256|HAMAP-Rule:MF_00180}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00180}; KW Manganese {ECO:0000256|HAMAP-Rule:MF_00180}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_00180}; Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}; KW Riboflavin biosynthesis {ECO:0000256|ARBA:ARBA00022619, ECO:0000256|HAMAP- KW Rule:MF_00180}. FT DOMAIN 246..402 FT /note="GTP cyclohydrolase II" FT /evidence="ECO:0000259|Pfam:PF00925" FT REGION 208..240 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 209..232 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 29..30 FT /ligand="D-ribulose 5-phosphate" FT /ligand_id="ChEBI:CHEBI:58121" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00180" FT BINDING 30 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00180" FT BINDING 30 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00180" FT BINDING 34 FT /ligand="D-ribulose 5-phosphate" FT /ligand_id="ChEBI:CHEBI:58121" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00180" FT BINDING 142..146 FT /ligand="D-ribulose 5-phosphate" FT /ligand_id="ChEBI:CHEBI:58121" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00180" FT BINDING 145 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00180" FT SITE 128 FT /note="Essential for catalytic activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00180" FT SITE 166 FT /note="Essential for catalytic activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00180" SQ SEQUENCE 432 AA; 45569 MW; E23315592B1C7312 CRC64; MTTTLASIED AIQQIAAGRP IVVVDDEDRE NEGDLIMAAD AVTAEWMGFI IRYSSGVVCA PIPAQTAQRL ALPPMTADNE DPKGTAYTVS VDAKAGVTTG ISAADRSLTA RLLADPDTRT EDLTRPGHLF PLIAQDDGVL ARDGHTEAGL DFARLAGRSP AAVIAEIVHD DGSMMRFAAL AEFAREHGLA MVTIADLIAY RKANPDAPMT PVPTTSGKNQ STGPTAAQSA AAGGNTAGRR LVRGETVPLP TDFGTLTATA YTFDGTDHLV LSGPPNADST PLVRIHSECL TGDVFGSHRC DCGEQLAQAL RTVATVGGHV IYVRGHEGRG IGLAGKIAAY SLQDTGVDTV DANTRLGFAA DARKYDAVAA ILADMGLHSV RLMTNNPTKI TALQHMDIDV TRVDAEVAPR PENIAYLATK RDRMSHLLER TL //