RIBB_SALTY
ID RIBB_SALTY Reviewed; 217 AA.
AC P66032; Q8XES0;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 95.
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=STM3195;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
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; AE006468; AAL22069.1; -; Genomic_DNA.
DR RefSeq; NP_462110.1; NC_003197.2.
DR RefSeq; WP_001076978.1; NC_003197.2.
DR PDB; 3LQU; X-ray; 2.52 A; A/B=1-217.
DR PDB; 3LRJ; X-ray; 2.80 A; A/B/C/D=1-217.
DR PDB; 3LS6; X-ray; 1.86 A; A/B=1-217.
DR PDBsum; 3LQU; -.
DR PDBsum; 3LRJ; -.
DR PDBsum; 3LS6; -.
DR AlphaFoldDB; P66032; -.
DR SMR; P66032; -.
DR STRING; 99287.STM3195; -.
DR PaxDb; P66032; -.
DR EnsemblBacteria; AAL22069; AAL22069; STM3195.
DR GeneID; 1254718; -.
DR KEGG; stm:STM3195; -.
DR PATRIC; fig|99287.12.peg.3389; -.
DR HOGENOM; CLU_020273_3_0_6; -.
DR OMA; DAGGLIC; -.
DR PhylomeDB; P66032; -.
DR BioCyc; SENT99287:STM3195-MON; -.
DR BRENDA; 4.1.99.12; 5542.
DR UniPathway; UPA00275; UER00399.
DR EvolutionaryTrace; P66032; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0008686; F:3,4-dihydroxy-2-butanone-4-phosphate synthase activity; IBA:GO_Central.
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; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Lyase; Magnesium; Manganese; Metal-binding;
KW Reference proteome; Riboflavin biosynthesis.
FT CHAIN 1..217
FT /note="3,4-dihydroxy-2-butanone 4-phosphate synthase"
FT /id="PRO_0000151810"
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"
FT HELIX 12..24
FT /evidence="ECO:0007829|PDB:3LS6"
FT STRAND 29..32
FT /evidence="ECO:0007829|PDB:3LS6"
FT TURN 35..38
FT /evidence="ECO:0007829|PDB:3LS6"
FT STRAND 41..46
FT /evidence="ECO:0007829|PDB:3LS6"
FT TURN 47..49
FT /evidence="ECO:0007829|PDB:3LS6"
FT HELIX 52..61
FT /evidence="ECO:0007829|PDB:3LS6"
FT STRAND 67..70
FT /evidence="ECO:0007829|PDB:3LS6"
FT HELIX 72..77
FT /evidence="ECO:0007829|PDB:3LS6"
FT STRAND 99..104
FT /evidence="ECO:0007829|PDB:3LS6"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:3LS6"
FT HELIX 111..122
FT /evidence="ECO:0007829|PDB:3LS6"
FT HELIX 128..130
FT /evidence="ECO:0007829|PDB:3LS6"
FT STRAND 131..141
FT /evidence="ECO:0007829|PDB:3LS6"
FT HELIX 146..148
FT /evidence="ECO:0007829|PDB:3LS6"
FT HELIX 153..164
FT /evidence="ECO:0007829|PDB:3LS6"
FT STRAND 170..176
FT /evidence="ECO:0007829|PDB:3LS6"
FT STRAND 180..182
FT /evidence="ECO:0007829|PDB:3LS6"
FT HELIX 185..194
FT /evidence="ECO:0007829|PDB:3LS6"
FT STRAND 198..201
FT /evidence="ECO:0007829|PDB:3LS6"
FT HELIX 202..210
FT /evidence="ECO:0007829|PDB:3LS6"
SQ SEQUENCE 217 AA; 23310 MW; EE07D4C93C3F4EB7 CRC64;
MNQTLLSSFG TPFERVELAL DALREGRGVM VLDDEDRENE GDMIFPAETM TVEQMALTIR
HGSGIVCLCI TEDRRKQLDL PMMVENNTSA YGTGFTVTIE AAEGVTTGVS AADRVTTVRA
AIKDGAKPSD LNRPGHVFPL RAQAGGVLTR GGHTEATIDL MTLAGFKPAG VLCELTNDDG
TMARAPECIA FAGQHNMAVV TIEDLVAYRQ AHERKAS
