ID S6V7S5_PSESF Unreviewed; 103 AA.
AC S6V7S5;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=3,4-dihydroxy-2-butanone 4-phosphate synthase {ECO:0000256|ARBA:ARBA00018836};
DE EC=4.1.99.12 {ECO:0000256|ARBA:ARBA00012153};
DE Flags: Fragment;
GN ORFNames=A244_21331 {ECO:0000313|EMBL:EPN47107.1};
OS Pseudomonas syringae pv. actinidiae ICMP 18807.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX NCBI_TaxID=1194404 {ECO:0000313|EMBL:EPN47107.1, ECO:0000313|Proteomes:UP000015729};
RN [1] {ECO:0000313|EMBL:EPN47107.1, ECO:0000313|Proteomes:UP000015729}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ICMP 18807 {ECO:0000313|EMBL:EPN47107.1,
RC ECO:0000313|Proteomes:UP000015729};
RX PubMed=23935484; DOI=10.1371/journal.ppat.1003503;
RA McCann H.C., Rikkerink E.H., Bertels F., Fiers M., Lu A., Rees-George J.,
RA Andersen M.T., Gleave A.P., Haubold B., Wohlers M.W., Guttman D.S.,
RA Wang P.W., Straub C., Vanneste J.L., Rainey P.B., Templeton M.D.;
RT "Genomic analysis of the Kiwifruit pathogen Pseudomonas syringae pv.
RT actinidiae provides insight into the origins of an emergent plant
RT disease.";
RL PLoS Pathog. 9:E1003503-E1003503(2013).
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}.
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:EPN47107.1}.
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DR EMBL; AOKG01001501; EPN47107.1; -; Genomic_DNA.
DR AlphaFoldDB; S6V7S5; -.
DR PATRIC; fig|1194404.4.peg.4383; -.
DR UniPathway; UPA00275; UER00399.
DR Proteomes; UP000015729; Unassembled WGS sequence.
DR GO; GO:0008686; F:3,4-dihydroxy-2-butanone-4-phosphate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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 Hydrolase {ECO:0000313|EMBL:EPN47107.1};
KW Lyase {ECO:0000313|EMBL:EPN47107.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Riboflavin biosynthesis {ECO:0000256|ARBA:ARBA00022619}.
FT NON_TER 103
FT /evidence="ECO:0000313|EMBL:EPN47107.1"
SQ SEQUENCE 103 AA; 11177 MW; 260AB072B6AFA2FC CRC64;
MAFDRIEDII EDYRQGKMVL LVDDEDRENE GDLLLAADCC TAQAISFMAR EARGLICLTL
TDEHCKRLGL EQMVPSNGSV FATAFTVSIE ATTGVTTGIS AAD
//
