ID   T0VHR7_LACLC            Unreviewed;       398 AA.
AC   T0VHR7;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   22-FEB-2023, entry version 60.
DE   RecName: Full=Riboflavin biosynthesis protein RibBA {ECO:0000256|HAMAP-Rule:MF_01283};
DE   Includes:
DE     RecName: Full=3,4-dihydroxy-2-butanone 4-phosphate synthase {ECO:0000256|HAMAP-Rule:MF_01283};
DE              Short=DHBP synthase {ECO:0000256|HAMAP-Rule:MF_01283};
DE              EC=4.1.99.12 {ECO:0000256|HAMAP-Rule:MF_01283};
DE   Includes:
DE     RecName: Full=GTP cyclohydrolase-2 {ECO:0000256|HAMAP-Rule:MF_01283};
DE              EC=3.5.4.25 {ECO:0000256|HAMAP-Rule:MF_01283};
DE     AltName: Full=GTP cyclohydrolase II {ECO:0000256|HAMAP-Rule:MF_01283};
GN   Name=ribBA {ECO:0000256|HAMAP-Rule:MF_01283};
GN   ORFNames=LLT3_01360 {ECO:0000313|EMBL:EQC95357.1};
OS   Lactococcus lactis subsp. cremoris TIFN3.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus; Lactococcus cremoris subsp. cremoris.
OX   NCBI_TaxID=1234873 {ECO:0000313|EMBL:EQC95357.1, ECO:0000313|Proteomes:UP000015664};
RN   [1] {ECO:0000313|EMBL:EQC95357.1, ECO:0000313|Proteomes:UP000015664}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TIFN3 {ECO:0000313|EMBL:EQC95357.1,
RC   ECO:0000313|Proteomes:UP000015664};
RX   PubMed=23823494; DOI=10.1038/ismej.2013.108;
RA   Erkus O., de Jager V.C., Spus M., van Alen-Boerrigter I.J.,
RA   van Rijswijck I.M., Hazelwood L., Janssen P.W., van Hijum S.A.,
RA   Kleerebezem M., Smid E.J.;
RT   "Multifactorial diversity sustains microbial community stability.";
RL   ISME J. 7:2126-2136(2013).
CC   -!- FUNCTION: Catalyzes the conversion of D-ribulose 5-phosphate to formate
CC       and 3,4-dihydroxy-2-butanone 4-phosphate.
CC       {ECO:0000256|ARBA:ARBA00002284, ECO:0000256|HAMAP-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:0000256|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:0000256|ARBA:ARBA00000141,
CC         ECO:0000256|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:0000256|ARBA:ARBA00029293, ECO:0000256|HAMAP-
CC         Rule:MF_01283};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01283};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01283};
CC       Note=Binds 2 divalent metal cations per subunit. Magnesium or
CC       manganese. {ECO:0000256|HAMAP-Rule:MF_01283};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01283};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|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:0000256|ARBA:ARBA00004904, ECO:0000256|HAMAP-Rule:MF_01283}.
CC   -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-
CC       ribitylamino)uracil from GTP: step 1/4. {ECO:0000256|ARBA:ARBA00004853,
CC       ECO:0000256|HAMAP-Rule:MF_01283}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the GTP
CC       cyclohydrolase II family. {ECO:0000256|HAMAP-Rule:MF_01283}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the DHBP synthase
CC       family. {ECO:0000256|ARBA:ARBA00005520, ECO:0000256|HAMAP-
CC       Rule:MF_01283}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EQC95357.1}.
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DR   EMBL; ATBE01000178; EQC95357.1; -; Genomic_DNA.
DR   RefSeq; WP_021165199.1; NZ_ATBE01000178.1.
DR   AlphaFoldDB; T0VHR7; -.
DR   EnsemblBacteria; EQC95357; EQC95357; LLT3_01360.
DR   PATRIC; fig|1234873.3.peg.1086; -.
DR   UniPathway; UPA00275; UER00399.
DR   Proteomes; UP000015664; Unassembled WGS sequence.
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; 3.90.870.10; DHBP synthase; 1.
DR   Gene3D; 3.40.50.10990; GTP cyclohydrolase II; 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   PANTHER; PTHR21327:SF18; 3,4-DIHYDROXY-2-BUTANONE 4-PHOSPHATE SYNTHASE; 1.
DR   PANTHER; PTHR21327; GTP CYCLOHYDROLASE II-RELATED; 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.
DR   TIGRFAMs; TIGR00505; ribA; 1.
DR   TIGRFAMs; TIGR00506; ribB; 1.
PE   3: Inferred from homology;
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW   Rule:MF_01283};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01283};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_01283};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01283};
KW   Manganese {ECO:0000256|HAMAP-Rule:MF_01283};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_01283}; Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_01283};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_01283};
KW   Riboflavin biosynthesis {ECO:0000256|ARBA:ARBA00022619, ECO:0000256|HAMAP-
KW   Rule:MF_01283}; Zinc {ECO:0000256|HAMAP-Rule:MF_01283}.
FT   DOMAIN          208..373
FT                   /note="GTP cyclohydrolase II"
FT                   /evidence="ECO:0000259|Pfam:PF00925"
FT   REGION          1..201
FT                   /note="DHBP synthase"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01283"
FT   REGION          202..398
FT                   /note="GTP cyclohydrolase II"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01283"
FT   ACT_SITE        329
FT                   /note="Proton acceptor; for GTP cyclohydrolase activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01283"
FT   ACT_SITE        331
FT                   /note="Nucleophile; for GTP cyclohydrolase activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01283"
FT   BINDING         28..29
FT                   /ligand="D-ribulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58121"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01283"
FT   BINDING         29
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01283"
FT   BINDING         29
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01283"
FT   BINDING         33
FT                   /ligand="D-ribulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58121"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01283"
FT   BINDING         140..144
FT                   /ligand="D-ribulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58121"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01283"
FT   BINDING         143
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01283"
FT   BINDING         164
FT                   /ligand="D-ribulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58121"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01283"
FT   BINDING         252..256
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01283"
FT   BINDING         257
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01283"
FT   BINDING         268
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01283"
FT   BINDING         270
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01283"
FT   BINDING         273
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01283"
FT   BINDING         295..297
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01283"
FT   BINDING         317
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01283"
FT   BINDING         352
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01283"
FT   BINDING         357
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01283"
FT   SITE            126
FT                   /note="Essential for DHBP synthase activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01283"
FT   SITE            164
FT                   /note="Essential for DHBP synthase activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01283"
SQ   SEQUENCE   398 AA;  44552 MW;  1A796E4074068ED6 CRC64;
     MFQYNTVEEA LTALKAGEMI IVTDDENREN EGDLICAAEM ISPEKINFMA SQAKGLICSP
     MSEKYAKSLH LSAMTERNTD NHGTAFTVSV DHVETSTGVS AFDRSLTIRK LADEESSVED
     FRRPGHVFPL IAKKNGVLER NGHTEATVDL LRLAGLKEVG VCVEIMAEDG SMMRTEELQE
     KAKEWDLNFI TIKAIQEYRK QNEQLVEQVT RAKLPTKYGY FEIFGFVNKI NGEHHVALVK
     GDIGEGEAVL CRVHSECLTG DAFGSMKCDC GEQLEQALTQ INAEGRGVLL YLRQEGRGIG
     LINKLRAYSL QDEGLDTIEA NLALGFEEDA REYSIGAQIL KTLGVKSLRL MTNNPQKIND
     FSKYGLPVKE RVPIQIKENE FDQDYLKVKQ NKMGHLFD
//