ID B8R4J5_9MYCO Unreviewed; 200 AA.
AC B8R4J5;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=3,4-dihydroxy-2-butanone-4-phosphate synthase {ECO:0000256|ARBA:ARBA00012153};
DE EC=4.1.99.12 {ECO:0000256|ARBA:ARBA00012153};
OS Mycolicibacterium brisbanense.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=146020 {ECO:0000313|EMBL:ACL11825.1};
RN [1] {ECO:0000313|EMBL:ACL11825.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=JK1 {ECO:0000313|EMBL:ACL11825.1};
RX PubMed=19000034; DOI=10.1042/BJ20081488;
RA Khurana J.L., Jackson C.J., Scott C., Pandey G., Horne I., Russell R.J.,
RA Herlt A., Easton C.J., Oakeshott J.G.;
RT "Characterization of the phenylurea hydrolases A and B: founding members of
RT a novel amidohydrolase subgroup.";
RL Biochem. J. 418:431-441(2009).
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}.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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}.
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DR EMBL; EU851876; ACL11825.1; -; Genomic_DNA.
DR AlphaFoldDB; B8R4J5; -.
DR UniPathway; UPA00275; UER00399.
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 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 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Riboflavin biosynthesis {ECO:0000256|ARBA:ARBA00022619}.
SQ SEQUENCE 200 AA; 20922 MW; 7E5CA5839AC895F8 CRC64;
MNASLAAVPT AREVSAALRG HRPVVVLTST SAILAFSASA ASTALVAFAV RHSTGMLFAL
TASERLDRLR IPDQPTLDSE HGSCRVTVAV DAAAGISTGI SARDRARTLR TLGDVRSVAT
DLIRPGHILP VRCGEPGDAP ELWARVRRII VEATGDEVAG ACHLVDRAGD IMDPVGGRSF
AAEHDLLIVP VESADRLSFG
//
