RIBB_PHOPO
ID RIBB_PHOPO Reviewed; 363 AA.
AC P51962;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=3,4-dihydroxy-2-butanone 4-phosphate synthase;
DE Short=DHBP synthase;
DE EC=4.1.99.12;
GN Name=ribB;
OS Photobacterium phosphoreum.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=659;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DSM 2167 / CIP 104260 / LMG 4231 / NCIMB 844;
RX PubMed=8144477; DOI=10.1128/jb.176.7.2100-2104.1994;
RA Lee C.Y., O'Kane D.J., Meighen E.A.;
RT "Riboflavin synthesis genes are linked with the lux operon of
RT Photobacterium phosphoreum.";
RL J. Bacteriol. 176:2100-2104(1994).
CC -!- FUNCTION: Catalyzes the conversion of D-ribulose 5-phosphate to formate
CC and 3,4-dihydroxy-2-butanone 4-phosphate. {ECO:0000250}.
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;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 2 divalent metal cations per subunit. Magnesium or
CC manganese. {ECO:0000250};
CC -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 2-hydroxy-3-
CC oxobutyl phosphate from D-ribulose 5-phosphate: step 1/1.
CC -!- SIMILARITY: In the N-terminal section; belongs to the DHBP synthase
CC family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the GTP
CC cyclohydrolase II family. {ECO:0000305}.
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DR EMBL; L11391; AAA25629.1; -; Genomic_DNA.
DR AlphaFoldDB; P51962; -.
DR SMR; P51962; -.
DR STRING; 659.AYY26_10960; -.
DR UniPathway; UPA00275; UER00399.
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 Gene3D; 3.40.50.10990; -; 1.
DR HAMAP; MF_00180; RibB; 1.
DR InterPro; IPR017945; DHBP_synth_RibB-like_a/b_dom.
DR InterPro; IPR000422; DHBP_synthase_RibB.
DR InterPro; IPR032677; GTP_cyclohydro_II.
DR InterPro; IPR036144; RibA-like_sf.
DR Pfam; PF00926; DHBP_synthase; 1.
DR Pfam; PF00925; GTP_cyclohydro2; 1.
DR SUPFAM; SSF142695; SSF142695; 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..363
FT /note="3,4-dihydroxy-2-butanone 4-phosphate synthase"
FT /id="PRO_0000151822"
FT REGION 1..201
FT /note="DHBP synthase"
FT REGION 202..363
FT /note="GTP cyclohydrolase II-like"
FT BINDING 27..28
FT /ligand="D-ribulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:58121"
FT /evidence="ECO:0000250"
FT BINDING 28
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 28
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 32
FT /ligand="D-ribulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:58121"
FT /evidence="ECO:0000250"
FT BINDING 140..144
FT /ligand="D-ribulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:58121"
FT /evidence="ECO:0000250"
FT BINDING 143
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 164
FT /ligand="D-ribulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:58121"
FT /evidence="ECO:0000250"
FT SITE 126
FT /note="Essential for catalytic activity"
FT /evidence="ECO:0000250"
FT SITE 164
FT /note="Essential for catalytic activity"
FT /evidence="ECO:0000250"
SQ SEQUENCE 363 AA; 40065 MW; 668F89CE296A3CD9 CRC64;
MTLSTAQEII EDIHQGKMVI LMDDEDRENE GDLIIASDKV TPEAINFMAT YGRGLICLTL
NKERCLQLEL PMMVKSNTDK FATPFTISIE AASGVTTGIS VNDRARTVQA AIAATATAKD
IVMPGHIFPL MAQDGGVLAR AGHTEAGCDV ARLAGLEPSS VIVEILNDDG TMARRPQLEV
FAKKHGLKLG TVADLIEYRN KYETMIERIS ECKLNTEFGE FDMITYRDKI NHQIHYALQK
GNIEPNSQTL VRVHLQDTFK DILQTGSTRW TLPAAMERIS SENGVLVIVT KQEDPEMVIS
KIQNLALENK ETPVVNSQSR QVGLGSQILS DLGIRKMRLL SSSSHLYHSL SGFGLEIVEY
VCS
