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Database: UniProt
Entry: RIBB_HELHP
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ID   RIBB_HELHP              Reviewed;         355 AA.
AC   Q7VJN5;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   27-MAR-2024, entry version 113.
DE   RecName: Full=3,4-dihydroxy-2-butanone 4-phosphate synthase;
DE            Short=DHBP synthase;
DE            EC=4.1.99.12;
GN   Name=ribB; OrderedLocusNames=HH_0208;
OS   Helicobacter hepaticus (strain ATCC 51449 / 3B1).
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=235279;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51449 / 3B1;
RX   PubMed=12810954; DOI=10.1073/pnas.1332093100;
RA   Suerbaum S., Josenhans C., Sterzenbach T., Drescher B., Brandt P., Bell M.,
RA   Droege M., Fartmann B., Fischer H.-P., Ge Z., Hoerster A., Holland R.,
RA   Klein K., Koenig J., Macko L., Mendz G.L., Nyakatura G., Schauer D.B.,
RA   Shen Z., Weber J., Frosch M., Fox J.G.;
RT   "The complete genome sequence of the carcinogenic bacterium Helicobacter
RT   hepaticus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:7901-7906(2003).
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; AE017125; AAP76805.1; -; Genomic_DNA.
DR   RefSeq; WP_011115051.1; NC_004917.1.
DR   AlphaFoldDB; Q7VJN5; -.
DR   SMR; Q7VJN5; -.
DR   STRING; 235279.HH_0208; -.
DR   GeneID; 82134835; -.
DR   KEGG; hhe:HH_0208; -.
DR   eggNOG; COG0108; Bacteria.
DR   HOGENOM; CLU_020273_1_2_7; -.
DR   OrthoDB; 9793111at2; -.
DR   UniPathway; UPA00275; UER00399.
DR   Proteomes; UP000002495; 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   Gene3D; 3.90.870.10; DHBP synthase; 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   NCBIfam; TIGR00506; ribB; 1.
DR   PANTHER; PTHR21327; GTP CYCLOHYDROLASE II-RELATED; 1.
DR   PANTHER; PTHR21327:SF48; RIBOFLAVIN BIOSYNTHESIS PROTEIN RIBBA; 1.
DR   Pfam; PF00926; DHBP_synthase; 1.
DR   Pfam; PF00925; GTP_cyclohydro2; 1.
DR   PIRSF; PIRSF001259; RibA; 1.
DR   SUPFAM; SSF142695; RibA-like; 1.
DR   SUPFAM; SSF55821; YrdC/RibB; 1.
PE   3: Inferred from homology;
KW   Lyase; Magnesium; Manganese; Metal-binding; Reference proteome;
KW   Riboflavin biosynthesis.
FT   CHAIN           1..355
FT                   /note="3,4-dihydroxy-2-butanone 4-phosphate synthase"
FT                   /id="PRO_0000151801"
FT   REGION          1..202
FT                   /note="DHBP synthase"
FT   REGION          203..355
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         139..143
FT                   /ligand="D-ribulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58121"
FT                   /evidence="ECO:0000250"
FT   BINDING         142
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         163
FT                   /ligand="D-ribulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58121"
FT                   /evidence="ECO:0000250"
FT   SITE            125
FT                   /note="Essential for catalytic activity"
FT                   /evidence="ECO:0000250"
FT   SITE            163
FT                   /note="Essential for catalytic activity"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   355 AA;  39765 MW;  015FC059512229C3 CRC64;
     MYHKRIKEAI EAIKQGEMII IMDDEDRENE GDLVMAGIFS SPQKINFMAQ EARGLICVSI
     TQELAQKLDL PPMVQKNDSN HETAFTISID AKEAKTGISA FERDMTIRLM CESNTKPSDF
     VRPGHIFPLI AKEGGVLVRT GHTEASVDIC RLAGVAPISV ICEIMKKDGT MAGRGDKFLL
     DFASQHHLKI LYVSDIIQYR LNFENLLREI TRESAVFMGV ECEKITFIDH LEREHIVFGF
     PHKGSSSNEP KPLIRFHNVR SDLELLQNAQ EWNALLKSIE CLKEKGGYLV FLNTHSEYAN
     SSKTCGDIKD FGIGAQILKR LGIEDFVLLS SCGGSKGEYN ALSGFNLHLV EKIEV
//
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