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RIBBA_BACMK
ID   RIBBA_BACMK             Reviewed;         397 AA.
AC   A9VG50;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Riboflavin biosynthesis protein RibBA {ECO:0000255|HAMAP-Rule:MF_01283};
DE   Includes:
DE     RecName: Full=3,4-dihydroxy-2-butanone 4-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_01283};
DE              Short=DHBP synthase {ECO:0000255|HAMAP-Rule:MF_01283};
DE              EC=4.1.99.12 {ECO:0000255|HAMAP-Rule:MF_01283};
DE   Includes:
DE     RecName: Full=GTP cyclohydrolase-2 {ECO:0000255|HAMAP-Rule:MF_01283};
DE              EC=3.5.4.25 {ECO:0000255|HAMAP-Rule:MF_01283};
DE     AltName: Full=GTP cyclohydrolase II {ECO:0000255|HAMAP-Rule:MF_01283};
GN   Name=ribBA {ECO:0000255|HAMAP-Rule:MF_01283};
GN   OrderedLocusNames=BcerKBAB4_3943;
OS   Bacillus mycoides (strain KBAB4) (Bacillus weihenstephanensis).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=315730;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KBAB4;
RX   PubMed=17434157; DOI=10.1016/j.cbi.2007.03.003;
RA   Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C.,
RA   Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., Sanchis V.,
RA   Nguen-the C., Lereclus D., Richardson P., Wincker P., Weissenbach J.,
RA   Ehrlich S.D., Sorokin A.;
RT   "Extending the Bacillus cereus group genomics to putative food-borne
RT   pathogens of different toxicity.";
RL   Chem. Biol. Interact. 171:236-249(2008).
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_01283}.
CC   -!- FUNCTION: Catalyzes the conversion of GTP to 2,5-diamino-6-
CC       ribosylamino-4(3H)-pyrimidinone 5'-phosphate (DARP), formate and
CC       pyrophosphate. {ECO:0000255|HAMAP-Rule:MF_01283}.
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_01283};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GTP + 4 H2O = 2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)-
CC         pyrimidine + formate + 3 H(+) + 2 phosphate; Xref=Rhea:RHEA:23704,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15740,
CC         ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58614; EC=3.5.4.25;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01283};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01283};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01283};
CC       Note=Binds 2 divalent metal cations per subunit. Magnesium or
CC       manganese. {ECO:0000255|HAMAP-Rule:MF_01283};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01283};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01283};
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_01283}.
CC   -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-
CC       ribitylamino)uracil from GTP: step 1/4. {ECO:0000255|HAMAP-
CC       Rule:MF_01283}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the DHBP synthase
CC       family. {ECO:0000255|HAMAP-Rule:MF_01283}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the GTP
CC       cyclohydrolase II family. {ECO:0000255|HAMAP-Rule:MF_01283}.
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DR   EMBL; CP000903; ABY45110.1; -; Genomic_DNA.
DR   RefSeq; WP_002033864.1; NC_010184.1.
DR   AlphaFoldDB; A9VG50; -.
DR   SMR; A9VG50; -.
DR   STRING; 315730.BcerKBAB4_3943; -.
DR   EnsemblBacteria; ABY45110; ABY45110; BcerKBAB4_3943.
DR   KEGG; bwe:BcerKBAB4_3943; -.
DR   eggNOG; COG0108; Bacteria.
DR   eggNOG; COG0807; Bacteria.
DR   HOGENOM; CLU_020273_1_2_9; -.
DR   OMA; ECRGLIC; -.
DR   UniPathway; UPA00275; UER00399.
DR   UniPathway; UPA00275; UER00400.
DR   Proteomes; UP000002154; Chromosome.
DR   GO; GO:0008686; F:3,4-dihydroxy-2-butanone-4-phosphate synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003935; F:GTP cyclohydrolase II 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:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009231; P:riboflavin biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd00641; GTP_cyclohydro2; 1.
DR   Gene3D; 3.40.50.10990; -; 1.
DR   HAMAP; MF_00179; RibA; 1.
DR   HAMAP; MF_00180; RibB; 1.
DR   HAMAP; MF_01283; RibBA; 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; IPR000926; RibA.
DR   InterPro; IPR036144; RibA-like_sf.
DR   InterPro; IPR016299; Riboflavin_synth_RibBA.
DR   Pfam; PF00926; DHBP_synthase; 1.
DR   Pfam; PF00925; GTP_cyclohydro2; 1.
DR   SUPFAM; SSF142695; SSF142695; 1.
DR   SUPFAM; SSF55821; SSF55821; 1.
DR   TIGRFAMs; TIGR00505; ribA; 1.
DR   TIGRFAMs; TIGR00506; ribB; 1.
PE   3: Inferred from homology;
KW   GTP-binding; Hydrolase; Lyase; Magnesium; Manganese; Metal-binding;
KW   Multifunctional enzyme; Nucleotide-binding; Riboflavin biosynthesis; Zinc.
FT   CHAIN           1..397
FT                   /note="Riboflavin biosynthesis protein RibBA"
FT                   /id="PRO_1000140364"
FT   REGION          1..199
FT                   /note="DHBP synthase"
FT   REGION          200..397
FT                   /note="GTP cyclohydrolase II"
FT   ACT_SITE        327
FT                   /note="Proton acceptor; for GTP cyclohydrolase activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01283"
FT   ACT_SITE        329
FT                   /note="Nucleophile; for GTP cyclohydrolase activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01283"
FT   BINDING         26..27
FT                   /ligand="D-ribulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58121"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01283"
FT   BINDING         27
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01283"
FT   BINDING         27
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01283"
FT   BINDING         31
FT                   /ligand="D-ribulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58121"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01283"
FT   BINDING         138..142
FT                   /ligand="D-ribulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58121"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01283"
FT   BINDING         141
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01283"
FT   BINDING         162
FT                   /ligand="D-ribulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58121"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01283"
FT   BINDING         250..254
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01283"
FT   BINDING         255
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01283"
FT   BINDING         266
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01283"
FT   BINDING         268
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01283"
FT   BINDING         271
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01283"
FT   BINDING         293..295
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01283"
FT   BINDING         315
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01283"
FT   BINDING         350
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01283"
FT   BINDING         355
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01283"
FT   SITE            124
FT                   /note="Essential for DHBP synthase activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01283"
FT   SITE            162
FT                   /note="Essential for DHBP synthase activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01283"
SQ   SEQUENCE   397 AA;  43955 MW;  D0D177DAAE8C058F CRC64;
     MFHRIEEALE DLKQGKVVIV CDDENRENEG DFIALAEYIT PETINFMITH GRGLVCVPIT
     EEYAERLQLE PMVSHNTDSH HTAFTVSIDH VSTTTGISAH ERATTIQELL NPASKGSDFN
     RPGHIFPLIA KEGGVLRRAG HTEAAVDLAK LCGAEPAGVI CEIINEDGTM ARVPDLLECA
     KQFDIKMITI EDLIAYRRHH ETLVTREVEI TLPTDFGTFH AIGYSNSLDM KEHIALVKGD
     ISTGEPVLVR VHSECLTGDV FGSCRCDCGP QLHAALAQIE REGKGVLLYM RQEGRGIGLL
     NKLRAYKLQE EGLDTVEANE KLGFPADLRD YGIGAQILKD LGLQSLRLLT NNPRKIAGLQ
     GYDLEVTERV PLQMPTKEEN KTYLQTKASK LGHLLNL
 
 
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