ID   T0VHR7_LACLC            Unreviewed;       398 AA.
AC   T0VHR7;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   02-DEC-2020, entry version 52.
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.
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 + 3 H2O = 2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)-
CC         pyrimidine + diphosphate + formate + 2 H(+); Xref=Rhea:RHEA:23704,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15740,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:58614; EC=3.5.4.25;
CC         Evidence={ECO:0000256|ARBA:ARBA00000698, 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; 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   EnsemblBacteria; EQC95357; EQC95357; LLT3_01360.
DR   PATRIC; fig|1234873.3.peg.1086; -.
DR   UniPathway; UPA00275; UER00400.
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; 3.40.50.10990; -; 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 {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW   Rule:MF_01283};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01283,
KW   ECO:0000313|EMBL:EQC95357.1}; 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_cyclohydro2"
FT                   /evidence="ECO:0000259|Pfam:PF00925"
FT   NP_BIND         252..256
FT                   /note="GTP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01283"
FT   NP_BIND         295..297
FT                   /note="GTP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01283"
FT   REGION          1..201
FT                   /note="DHBP synthase"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01283"
FT   REGION          28..29
FT                   /note="D-ribulose 5-phosphate binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01283"
FT   REGION          140..144
FT                   /note="D-ribulose 5-phosphate binding"
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   METAL           29
FT                   /note="Magnesium or manganese 1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01283"
FT   METAL           29
FT                   /note="Magnesium or manganese 2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01283"
FT   METAL           143
FT                   /note="Magnesium or manganese 2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01283"
FT   METAL           257
FT                   /note="Zinc; catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01283"
FT   METAL           268
FT                   /note="Zinc; catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01283"
FT   METAL           270
FT                   /note="Zinc; catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01283"
FT   BINDING         33
FT                   /note="D-ribulose 5-phosphate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01283"
FT   BINDING         164
FT                   /note="D-ribulose 5-phosphate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01283"
FT   BINDING         273
FT                   /note="GTP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01283"
FT   BINDING         317
FT                   /note="GTP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01283"
FT   BINDING         352
FT                   /note="GTP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01283"
FT   BINDING         357
FT                   /note="GTP"
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
//