ID A0A1E9HN18_9MICO Unreviewed; 432 AA. AC A0A1E9HN18; DT 18-JAN-2017, integrated into UniProtKB/TrEMBL. DT 18-JAN-2017, sequence version 1. DT 05-DEC-2018, entry version 13. 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; OC 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 CC formate and 3,4-dihydroxy-2-butanone 4-phosphate. CC {ECO:0000256|HAMAP-Rule:MF_00180}. CC -!- CATALYTIC ACTIVITY: CC Reaction=D-ribulose 5-phosphate = (2S)-2-hydroxy-3-oxobutyl CC phosphate + formate + H(+); Xref=Rhea:RHEA:18457, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15740, ChEBI:CHEBI:58121, CC ChEBI:CHEBI:58830; EC=4.1.99.12; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00180}; CC -!- CATALYTIC ACTIVITY: CC Reaction=GTP + 3 H2O = 2,5-diamino-6-hydroxy-4-(5- CC phosphoribosylamino)-pyrimidine + diphosphate + formate + 2 CC H(+); Xref=Rhea:RHEA:23704, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15740, ChEBI:CHEBI:33019, CC ChEBI:CHEBI:37565, ChEBI:CHEBI:58614; EC=3.5.4.25; CC Evidence={ECO:0000256|SAAS:SAAS00711742}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00180}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000256|HAMAP- CC 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|SAAS:SAAS00711674}; 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_00180}. CC -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino- CC 6-(D-ribitylamino)uracil from GTP: step 1/4. CC {ECO:0000256|SAAS:SAAS00711724}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00180}. CC -!- SIMILARITY: Belongs to the DHBP synthase family. CC {ECO:0000256|HAMAP-Rule:MF_00180}. CC -!- SIMILARITY: In the C-terminal section; belongs to the GTP CC cyclohydrolase II family. {ECO:0000256|SAAS:SAAS00789992}. CC -!- SIMILARITY: In the N-terminal section; belongs to the DHBP CC synthase family. {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: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 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:InterPro. 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; 3.40.50.10990; -; 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 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:UP000242868}; KW GTP-binding {ECO:0000256|SAAS:SAAS00711691}; KW Hydrolase {ECO:0000256|SAAS:SAAS01033620, KW 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|HAMAP-Rule:MF_00180, KW ECO:0000256|SAAS:SAAS00037896}; KW Nucleotide-binding {ECO:0000256|SAAS:SAAS00711707}; KW Riboflavin biosynthesis {ECO:0000256|HAMAP-Rule:MF_00180, KW ECO:0000256|SAAS:SAAS00037880}; Zinc {ECO:0000256|SAAS:SAAS00711685}. FT DOMAIN 246 402 GTP_cyclohydro2. {ECO:0000259|Pfam: FT PF00925}. FT REGION 29 30 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_00180}. FT REGION 142 146 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_00180}. FT METAL 30 30 Magnesium or manganese 1. FT {ECO:0000256|HAMAP-Rule:MF_00180}. FT METAL 30 30 Magnesium or manganese 2. FT {ECO:0000256|HAMAP-Rule:MF_00180}. FT METAL 145 145 Magnesium or manganese 2. FT {ECO:0000256|HAMAP-Rule:MF_00180}. FT BINDING 34 34 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00180}. FT BINDING 166 166 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00180}. FT SITE 128 128 Essential for catalytic activity. FT {ECO:0000256|HAMAP-Rule:MF_00180}. FT SITE 166 166 Essential for catalytic activity. FT {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 //