RIBB_SHELP
ID RIBB_SHELP Reviewed; 217 AA.
AC A3Q8W5;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 96.
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=Shew_0040;
OS Shewanella loihica (strain ATCC BAA-1088 / PV-4).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=323850;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1088 / PV-4;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Romine M.F., Serres G.,
RA Fredrickson J., Tiedje J., Richardson P.;
RT "Complete sequence of Shewanella loihica PV-4.";
RL Submitted (MAR-2007) 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. {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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000606; ABO21913.1; -; Genomic_DNA.
DR RefSeq; WP_011863850.1; NC_009092.1.
DR AlphaFoldDB; A3Q8W5; -.
DR SMR; A3Q8W5; -.
DR STRING; 323850.Shew_0040; -.
DR EnsemblBacteria; ABO21913; ABO21913; Shew_0040.
DR KEGG; slo:Shew_0040; -.
DR eggNOG; COG0108; Bacteria.
DR HOGENOM; CLU_020273_3_0_6; -.
DR OMA; DAGGLIC; -.
DR OrthoDB; 900513at2; -.
DR UniPathway; UPA00275; UER00399.
DR Proteomes; UP000001558; 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; Reference proteome;
KW Riboflavin biosynthesis.
FT CHAIN 1..217
FT /note="3,4-dihydroxy-2-butanone 4-phosphate synthase"
FT /id="PRO_1000040628"
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; 23316 MW; 257FFFFA18E35BF9 CRC64;
MNQSLLSPFG DAITRVEAAL TALRAGQGVL VVDDEDRENE GDLIYSAEHL TQEQMALLIR
ECSGIVCLCL TDERVKQLEL PPMVEDNSSQ YGTAFTVSIE AKVGVTTGVS AADRVTTIKA
AIADDAKPSD LARPGHVYPL RAQPGGVLTR RGHTEGTIDL MKLAGLKPAG VLCEVTNVNG
TMARLPEIIA FGEQHKMPVL TIEDIVCYRK SLLEKAS
