ID A0A1C0Y757_9BACL Unreviewed; 199 AA.
AC A0A1C0Y757;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=A6M13_06350 {ECO:0000313|EMBL:OCS83019.1};
OS Caryophanon tenue.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Caryophanon.
OX NCBI_TaxID=33978 {ECO:0000313|EMBL:OCS83019.1, ECO:0000313|Proteomes:UP000093199};
RN [1] {ECO:0000313|EMBL:OCS83019.1, ECO:0000313|Proteomes:UP000093199}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14152 {ECO:0000313|EMBL:OCS83019.1,
RC ECO:0000313|Proteomes:UP000093199};
RA Verma A., Pal Y., Krishnamurthi S.;
RT "Caryophanon tenue genome sequencing.";
RL Submitted (JUL-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|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|ARBA:ARBA00000141,
CC 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 -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
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|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:OCS83019.1}.
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DR EMBL; MASJ01000039; OCS83019.1; -; Genomic_DNA.
DR RefSeq; WP_066547948.1; NZ_MASJ01000039.1.
DR AlphaFoldDB; A0A1C0Y757; -.
DR STRING; 33978.A6M13_06350; -.
DR OrthoDB; 9793111at2; -.
DR UniPathway; UPA00275; UER00399.
DR Proteomes; UP000093199; 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; GTP CYCLOHYDROLASE II-RELATED; 1.
DR PANTHER; PTHR21327:SF48; RIBOFLAVIN BIOSYNTHESIS PROTEIN RIBBA; 1.
DR Pfam; PF00926; DHBP_synthase; 1.
DR SUPFAM; SSF55821; YrdC/RibB; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|RuleBase:RU003843};
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 Reference proteome {ECO:0000313|Proteomes:UP000093199};
KW Riboflavin biosynthesis {ECO:0000256|ARBA:ARBA00022619,
KW ECO:0000256|RuleBase:RU003843}.
SQ SEQUENCE 199 AA; 21924 MW; AD54CAC0574C9EB6 CRC64;
MIEQALDVLK NGGIIIVVDD EDRENEGDFV CLAQYATPQN INFMATYGRG LICAPVSEAI
AERLALHPMV TTNTDPHGTA FTESIDFETT TTGISAFERA ETIQQLCNEH VKAHQFKRPG
HVFPLRAKAG GVIERRGHTE AGIELAKLCN STEAAVICEI LNDDGTMARR PQLEQIANQH
NLHIMTIEAL VDYVQLARV
//
