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RIBBA_CLONN
ID   RIBBA_CLONN             Reviewed;         414 AA.
AC   A0Q3H7;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 94.
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=NT01CX_0713;
OS   Clostridium novyi (strain NT).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=386415;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NT;
RX   PubMed=17115055; DOI=10.1038/nbt1256;
RA   Bettegowda C., Huang X., Lin J., Cheong I., Kohli M., Szabo S.A., Zhang X.,
RA   Diaz L.A. Jr., Velculescu V.E., Parmigiani G., Kinzler K.W., Vogelstein B.,
RA   Zhou S.;
RT   "The genome and transcriptomes of the anti-tumor agent Clostridium novyi-
RT   NT.";
RL   Nat. Biotechnol. 24:1573-1580(2006).
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; CP000382; ABK61746.1; -; Genomic_DNA.
DR   RefSeq; WP_011723157.1; NC_008593.1.
DR   AlphaFoldDB; A0Q3H7; -.
DR   SMR; A0Q3H7; -.
DR   STRING; 386415.NT01CX_0713; -.
DR   EnsemblBacteria; ABK61746; ABK61746; NT01CX_0713.
DR   KEGG; cno:NT01CX_0713; -.
DR   PATRIC; fig|386415.7.peg.2218; -.
DR   eggNOG; COG0108; Bacteria.
DR   eggNOG; COG0807; Bacteria.
DR   HOGENOM; CLU_020273_1_2_9; -.
DR   OMA; ECRGLIC; -.
DR   OrthoDB; 900513at2; -.
DR   UniPathway; UPA00275; UER00399.
DR   UniPathway; UPA00275; UER00400.
DR   Proteomes; UP000008220; 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; Reference proteome;
KW   Riboflavin biosynthesis; Zinc.
FT   CHAIN           1..414
FT                   /note="Riboflavin biosynthesis protein RibBA"
FT                   /id="PRO_1000073187"
FT   REGION          1..203
FT                   /note="DHBP synthase"
FT   REGION          204..414
FT                   /note="GTP cyclohydrolase II"
FT   ACT_SITE        331
FT                   /note="Proton acceptor; for GTP cyclohydrolase activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01283"
FT   ACT_SITE        333
FT                   /note="Nucleophile; for GTP cyclohydrolase activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01283"
FT   BINDING         30..31
FT                   /ligand="D-ribulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58121"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01283"
FT   BINDING         31
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01283"
FT   BINDING         31
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01283"
FT   BINDING         35
FT                   /ligand="D-ribulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58121"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01283"
FT   BINDING         142..146
FT                   /ligand="D-ribulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58121"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01283"
FT   BINDING         145
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01283"
FT   BINDING         166
FT                   /ligand="D-ribulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58121"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01283"
FT   BINDING         254..258
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01283"
FT   BINDING         259
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01283"
FT   BINDING         270
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01283"
FT   BINDING         272
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01283"
FT   BINDING         275
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01283"
FT   BINDING         297..299
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01283"
FT   BINDING         319
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01283"
FT   BINDING         354
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01283"
FT   BINDING         359
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01283"
FT   SITE            128
FT                   /note="Essential for DHBP synthase activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01283"
FT   SITE            166
FT                   /note="Essential for DHBP synthase activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01283"
SQ   SEQUENCE   414 AA;  46198 MW;  79F6FA3898C24B71 CRC64;
     MEQFKFNTIE EAIEDIKNGK MVVVVDDEDR ENEGDLLMAA EKVTPEAINF MAKYARGLIC
     MPMTEEKLKE LDLYQMVINN TDTKETAFTV SIDSVETTTG ISAFERALTI TKAVEKGAKA
     KDFQRPGHIF PLRARKGGVL KRAGHTEAAV DLATLAGLTP AGTICEIMNE DGTMARVPDL
     MKYVKVHNLK IVTIADLIEY RRKTESFIER QGSASLPTKY GEFEIIGYED KLTGKEHVAL
     VKGDIKNGEP VLIRVHSECL TGDVLGSLRC DCGDQLAQAL RQINKEGRGA LLYMRQEGRG
     IGLINKIKAY KLQDNGMDTV DANLALGFPE DLRDYGIGAQ ILKDLGVEKV RLMTNNPKKV
     SGISGYGIEI VERVPIEIEC NKKNEFYLRT KKERMGHILN FKNIKKYDKS IKEA
 
 
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