ID C9MUK6_9FUSO Unreviewed; 145 AA.
AC C9MUK6;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 24-JAN-2024, entry version 47.
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};
GN ORFNames=GCWU000323_00225 {ECO:0000313|EMBL:EEX75626.1};
OS Leptotrichia hofstadii F0254.
OC Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Leptotrichiaceae;
OC Leptotrichia.
OX NCBI_TaxID=634994 {ECO:0000313|EMBL:EEX75626.1, ECO:0000313|Proteomes:UP000006233};
RN [1] {ECO:0000313|EMBL:EEX75626.1, ECO:0000313|Proteomes:UP000006233}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0254 {ECO:0000313|EMBL:EEX75626.1,
RC ECO:0000313|Proteomes:UP000006233};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (SEP-2009) 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}.
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}.
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:EEX75626.1}.
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DR EMBL; ACVB02000006; EEX75626.1; -; Genomic_DNA.
DR AlphaFoldDB; C9MUK6; -.
DR STRING; 634994.GCWU000323_00225; -.
DR eggNOG; COG0108; Bacteria.
DR HOGENOM; CLU_020273_3_0_0; -.
DR UniPathway; UPA00275; UER00399.
DR Proteomes; UP000006233; 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 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 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000006233};
KW Riboflavin biosynthesis {ECO:0000256|ARBA:ARBA00022619}.
SQ SEQUENCE 145 AA; 16279 MW; 2B567B491BEF79FD CRC64;
MSKKRAEELE LDPMVQHNTD YYGTAFTVSV DSLEGTTTGI SAGDRLKTIK DLANPLKTAK
DFRKPGHIFP LIAREGGVLE RKGHTEAAVE LSRLAGFSDI GVIMEILRED GEMARRNDLF
EFCQKHNLKL ITIDDLIVYI KKTKN
//
