RIBB_PHOLE
ID RIBB_PHOLE Reviewed; 364 AA.
AC Q02008;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 92.
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 leiognathi.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=553611;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 25521 / DSM 21260 / CIP 66.5 / NCIMB 2193 / L1;
RX PubMed=1339274; DOI=10.1016/0006-291x(92)90802-r;
RA Lee C.Y., Meighen E.A.;
RT "The lux genes in Photobacterium leiognathi are closely linked with genes
RT corresponding in sequence to riboflavin synthesis genes.";
RL Biochem. Biophys. Res. Commun. 186:690-697(1992).
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; M90094; AAA73229.1; -; Genomic_DNA.
DR PIR; JC1188; JC1188.
DR AlphaFoldDB; Q02008; -.
DR SMR; Q02008; -.
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..364
FT /note="3,4-dihydroxy-2-butanone 4-phosphate synthase"
FT /id="PRO_0000151821"
FT REGION 1..201
FT /note="DHBP synthase"
FT REGION 202..364
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 364 AA; 39948 MW; 168E5BF3609534D5 CRC64;
MALSSAKEII DDIRQGRMVI LMDDESRENE GDLIIASEMV TPEAINFMAT HGRGLICLTL
SKARCKTLNL PLMVQGNNDN FSTPFTISIE AAKYVTTGIS ASDRAKTVLA AVAPNAKSTD
IVMPGHIFPL MAQDGGVLIR AGHTEAGCDV ARLAGLEPSS VIVEILNEDG SMARRPQLEI
FAEKHGLKLG TIADLIEYRT QQESHIERIS EYELNTEYGI FTLVTYRDTI DNQAHFALCK
GEIQAKAATL VRVHVKDTLK DILQVGLSQW SLEAAMQRIQ TEDGVLVIIS QQESPKTLFE
KLDMYAKEQP NSPHSGIVQS RNIGLGSQIL ADLGVKKIRL LSNSNQGYRA LSGFGLEVVE
YIYD
