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Database: UniProt
Entry: A0A069Q2E7_9BURK
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ID   A0A069Q2E7_9BURK        Unreviewed;       215 AA.
AC   A0A069Q2E7;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 45.
DE   RecName: Full=3,4-dihydroxy-2-butanone 4-phosphate synthase {ECO:0000256|ARBA:ARBA00018836, ECO:0000256|HAMAP-Rule:MF_00180};
DE            Short=DHBP synthase {ECO:0000256|HAMAP-Rule:MF_00180, ECO:0000256|RuleBase:RU003843};
DE            EC=4.1.99.12 {ECO:0000256|ARBA:ARBA00012153, ECO:0000256|HAMAP-Rule:MF_00180};
GN   Name=ribB {ECO:0000256|HAMAP-Rule:MF_00180};
GN   ORFNames=BG61_24785 {ECO:0000313|EMBL:KDR43961.1};
OS   Caballeronia glathei.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Caballeronia.
OX   NCBI_TaxID=60547 {ECO:0000313|EMBL:KDR43961.1, ECO:0000313|Proteomes:UP000027466};
RN   [1] {ECO:0000313|EMBL:KDR43961.1, ECO:0000313|Proteomes:UP000027466}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 50014 {ECO:0000313|EMBL:KDR43961.1,
RC   ECO:0000313|Proteomes:UP000027466};
RA   Liu X.Y., Li C.X., Xu J.H.;
RT   "Draft Genome Sequences of Four Burkholderia Strains.";
RL   Submitted (MAR-2014) 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       ECO:0000256|RuleBase:RU003843}.
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|HAMAP-Rule:MF_00180,
CC         ECO:0000256|RuleBase:RU003843};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00180,
CC         ECO:0000256|RuleBase:RU003843};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00180,
CC         ECO:0000256|RuleBase:RU003843};
CC       Note=Binds 2 divalent metal cations per subunit. Magnesium or
CC       manganese. {ECO:0000256|HAMAP-Rule:MF_00180,
CC       ECO:0000256|RuleBase:RU003843};
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       ECO:0000256|RuleBase:RU003843}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00180,
CC       ECO:0000256|RuleBase:RU003843}.
CC   -!- SIMILARITY: Belongs to the DHBP synthase family. {ECO:0000256|HAMAP-
CC       Rule:MF_00180, ECO:0000256|RuleBase:RU003843}.
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:KDR43961.1}.
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DR   EMBL; JFHC01000004; KDR43961.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A069Q2E7; -.
DR   STRING; 60547.GCA_000751215_01120; -.
DR   UniPathway; UPA00275; UER00399.
DR   Proteomes; UP000027466; Unassembled WGS sequence.
DR   GO; GO:0008686; F:3,4-dihydroxy-2-butanone-4-phosphate synthase 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:0009231; P:riboflavin biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.90.870.10; DHBP synthase; 1.
DR   HAMAP; MF_00180; RibB; 1.
DR   InterPro; IPR017945; DHBP_synth_RibB-like_a/b_dom.
DR   InterPro; IPR000422; DHBP_synthase_RibB.
DR   NCBIfam; TIGR00506; ribB; 1.
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   SUPFAM; SSF55821; YrdC/RibB; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00180, ECO:0000256|RuleBase:RU003843};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00180, ECO:0000256|RuleBase:RU003843};
KW   Manganese {ECO:0000256|HAMAP-Rule:MF_00180, ECO:0000256|RuleBase:RU003843};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00180}; Reference proteome {ECO:0000313|Proteomes:UP000027466};
KW   Riboflavin biosynthesis {ECO:0000256|ARBA:ARBA00022619, ECO:0000256|HAMAP-
KW   Rule:MF_00180}.
FT   BINDING         27..28
FT                   /ligand="D-ribulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58121"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00180"
FT   BINDING         28
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00180"
FT   BINDING         28
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00180"
FT   BINDING         32
FT                   /ligand="D-ribulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58121"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00180"
FT   BINDING         140..144
FT                   /ligand="D-ribulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58121"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00180"
FT   BINDING         143
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00180"
FT   SITE            126
FT                   /note="Essential for catalytic activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00180"
FT   SITE            164
FT                   /note="Essential for catalytic activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00180"
SQ   SEQUENCE   215 AA;  22946 MW;  4D227E5FBD8AA252 CRC64;
     MSIDRIEDAL AAMAQGALVV VVDDEDRENE GDLIMAAEMA TPEAIAFMVR YTSGVLCVAL
     PGARLDALRL PLMVPGGHDS MQTAFTVSVD YRHGTTTGIS AADRATTVRA LVDPQAHADD
     FNRPGHLFPL RAVADGVLRR PGHTEAAVDL CRLAGLREGG VLAEIVNDDG SMARLPQLAA
     FARLHGLPIV TIRDLIAYRT HTETTARVDR EAVAA
//
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