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Database: UniProt
Entry: A0A0N8KRE4_9EURY
LinkDB: A0A0N8KRE4_9EURY
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ID   A0A0N8KRE4_9EURY        Unreviewed;       222 AA.
AC   A0A0N8KRE4;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=3,4-dihydroxy-2-butanone 4-phosphate synthase {ECO:0000256|RuleBase:RU003843};
DE            Short=DHBP synthase {ECO:0000256|RuleBase:RU003843};
DE            EC=4.1.99.12 {ECO:0000256|RuleBase:RU003843};
GN   ORFNames=MPEBLZ_00725 {ECO:0000313|EMBL:KPQ44706.1};
OS   Candidatus Methanoperedens sp. BLZ1.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Candidatus Methanoperedenaceae; Methanoperedens.
OX   NCBI_TaxID=1719120 {ECO:0000313|EMBL:KPQ44706.1, ECO:0000313|Proteomes:UP000050360};
RN   [1] {ECO:0000313|EMBL:KPQ44706.1, ECO:0000313|Proteomes:UP000050360}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Arshad A., Speth D.R., De Graaf R.M., Op Den Camp H.J., Jetten M.S.,
RA   Welte C.U.;
RT   "A metagenomics-based metabolic model of nitrate-dependent anaerobic
RT   oxidation of methane by Methanoperedens-like archaea.";
RL   Submitted (SEP-2015) 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|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|RuleBase:RU003843};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|RuleBase:RU003843};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|RuleBase:RU003843};
CC       Note=Binds 2 divalent metal cations per subunit. Magnesium or
CC       manganese. {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|RuleBase:RU003843}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|RuleBase:RU003843}.
CC   -!- SIMILARITY: Belongs to the DHBP synthase family.
CC       {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:KPQ44706.1}.
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DR   EMBL; LKCM01000062; KPQ44706.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0N8KRE4; -.
DR   PATRIC; fig|1719120.3.peg.792; -.
DR   UniPathway; UPA00275; UER00399.
DR   Proteomes; UP000050360; Unassembled WGS sequence.
DR   GO; GO:0008686; F:3,4-dihydroxy-2-butanone-4-phosphate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009231; P:riboflavin biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.90.870.10; DHBP synthase; 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:SF46; 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|RuleBase:RU003843, ECO:0000313|EMBL:KPQ44706.1};
KW   Magnesium {ECO:0000256|RuleBase:RU003843};
KW   Manganese {ECO:0000256|RuleBase:RU003843};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU003843};
KW   Riboflavin biosynthesis {ECO:0000256|ARBA:ARBA00022619,
KW   ECO:0000256|RuleBase:RU003843}.
SQ   SEQUENCE   222 AA;  24250 MW;  FC92119E822D36F2 CRC64;
     MSLDSAIDAL RNGKMILLFD AEDREGETDL VIPAICITPS DVALMRRDGG GLICVAIYGK
     AADSLGLPFM SDILRSVSKN GHKSLISLVE KKGDIPYDSR SSFSLWVNHR ETFTGITDND
     RALTIRKVGE TVDKVMKGEK IDFGDEFRSP GHVALLRAAA GLLTERRGQT ELSIELALKA
     GISPSMVVCE MLDDKTGKAL TKEDAIKYSK EKNMPFIEGK DL
//
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