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RIBB_AERS4
ID   RIBB_AERS4              Reviewed;         217 AA.
AC   A4SKH7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=3,4-dihydroxy-2-butanone 4-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00180};
DE            Short=DHBP synthase {ECO:0000255|HAMAP-Rule:MF_00180};
DE            EC=4.1.99.12 {ECO:0000255|HAMAP-Rule:MF_00180};
GN   Name=ribB {ECO:0000255|HAMAP-Rule:MF_00180}; OrderedLocusNames=ASA_1293;
OS   Aeromonas salmonicida (strain A449).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=382245;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A449;
RX   PubMed=18801193; DOI=10.1186/1471-2164-9-427;
RA   Reith M.E., Singh R.K., Curtis B., Boyd J.M., Bouevitch A., Kimball J.,
RA   Munholland J., Murphy C., Sarty D., Williams J., Nash J.H., Johnson S.C.,
RA   Brown L.L.;
RT   "The genome of Aeromonas salmonicida subsp. salmonicida A449: insights into
RT   the evolution of a fish pathogen.";
RL   BMC Genomics 9:427-427(2008).
CC   -!- FUNCTION: Catalyzes the conversion of D-ribulose 5-phosphate to formate
CC       and 3,4-dihydroxy-2-butanone 4-phosphate. {ECO:0000255|HAMAP-
CC       Rule:MF_00180}.
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:0000255|HAMAP-Rule:MF_00180};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00180};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00180};
CC       Note=Binds 2 divalent metal cations per subunit. Magnesium or
CC       manganese. {ECO:0000255|HAMAP-Rule:MF_00180};
CC   -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 2-hydroxy-3-
CC       oxobutyl phosphate from D-ribulose 5-phosphate: step 1/1.
CC       {ECO:0000255|HAMAP-Rule:MF_00180}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00180}.
CC   -!- SIMILARITY: Belongs to the DHBP synthase family. {ECO:0000255|HAMAP-
CC       Rule:MF_00180}.
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DR   EMBL; CP000644; ABO89399.1; -; Genomic_DNA.
DR   RefSeq; WP_005316761.1; NC_009348.1.
DR   AlphaFoldDB; A4SKH7; -.
DR   SMR; A4SKH7; -.
DR   STRING; 382245.ASA_1293; -.
DR   EnsemblBacteria; ABO89399; ABO89399; ASA_1293.
DR   KEGG; asa:ASA_1293; -.
DR   eggNOG; COG0108; Bacteria.
DR   HOGENOM; CLU_020273_3_0_6; -.
DR   OMA; DAGGLIC; -.
DR   OrthoDB; 900513at2; -.
DR   UniPathway; UPA00275; UER00399.
DR   Proteomes; UP000000225; Chromosome.
DR   GO; GO:0008686; F:3,4-dihydroxy-2-butanone-4-phosphate synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009231; P:riboflavin biosynthetic process; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00180; RibB; 1.
DR   InterPro; IPR017945; DHBP_synth_RibB-like_a/b_dom.
DR   InterPro; IPR000422; DHBP_synthase_RibB.
DR   Pfam; PF00926; DHBP_synthase; 1.
DR   SUPFAM; SSF55821; SSF55821; 1.
DR   TIGRFAMs; TIGR00506; ribB; 1.
PE   3: Inferred from homology;
KW   Lyase; Magnesium; Manganese; Metal-binding; Riboflavin biosynthesis.
FT   CHAIN           1..217
FT                   /note="3,4-dihydroxy-2-butanone 4-phosphate synthase"
FT                   /id="PRO_1000040595"
FT   BINDING         37..38
FT                   /ligand="D-ribulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58121"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00180"
FT   BINDING         38
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00180"
FT   BINDING         38
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00180"
FT   BINDING         42
FT                   /ligand="D-ribulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58121"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00180"
FT   BINDING         150..154
FT                   /ligand="D-ribulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58121"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00180"
FT   BINDING         153
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00180"
FT   BINDING         174
FT                   /ligand="D-ribulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58121"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00180"
FT   SITE            136
FT                   /note="Essential for catalytic activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00180"
FT   SITE            174
FT                   /note="Essential for catalytic activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00180"
SQ   SEQUENCE   217 AA;  23535 MW;  91933A34329937A8 CRC64;
     MNQSLLSEFG DPLARVEAAL AALRAGRGVL VADDEDRENE GDLIFAAQTM TNEQMAMMIR
     ECSGIVCLCL TDERVRQLAL PMMVEANSSH YQTAFTVTIE AAQGVTTGVS AADRITTIRA
     AIADGAKPSD LHRPGHVFPL RARTGGVLTR RGHTEATVDL MQLAGLKPFG VLCELTKEDG
     SMARLPDLVA FGRLHQMPVL TIEDLVQYRQ LLSERSA
 
 
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