ID   T0VHR7_LACLC            Unreviewed;       398 AA.
AC   T0VHR7;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   17-FEB-2016, entry version 22.
DE   RecName: Full=Riboflavin biosynthesis protein RibBA {ECO:0000256|HAMAP-Rule:MF_01283, ECO:0000256|SAAS:SAAS00332815};
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
CC       formate and 3,4-dihydroxy-2-butanone 4-phosphate.
CC       {ECO:0000256|HAMAP-Rule:MF_01283, ECO:0000256|SAAS:SAAS00318278}.
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       ECO:0000256|SAAS:SAAS00317964}.
CC   -!- CATALYTIC ACTIVITY: D-ribulose 5-phosphate = formate + L-3,4-
CC       dihydroxybutan-2-one 4-phosphate. {ECO:0000256|HAMAP-
CC       Rule:MF_01283}.
CC   -!- CATALYTIC ACTIVITY: GTP + 3 H(2)O = formate + 2,5-diamino-6-
CC       hydroxy-4-(5-phospho-D-ribosylamino)pyrimidine + diphosphate.
CC       {ECO:0000256|HAMAP-Rule:MF_01283, ECO:0000256|SAAS:SAAS00415363}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01283, ECO:0000256|SAAS:SAAS00318265};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01283, ECO:0000256|SAAS:SAAS00318265};
CC       Note=Binds 2 divalent metal cations per subunit. Magnesium or
CC       manganese. {ECO:0000256|HAMAP-Rule:MF_01283,
CC       ECO:0000256|SAAS:SAAS00318265};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01283, ECO:0000256|SAAS:SAAS00318282};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01283, ECO:0000256|SAAS:SAAS00318282};
CC   -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 2-
CC       hydroxy-3-oxobutyl phosphate from D-ribulose 5-phosphate: step
CC       1/1. {ECO:0000256|HAMAP-Rule:MF_01283}.
CC   -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-
CC       6-(D-ribitylamino)uracil from GTP: step 1/4. {ECO:0000256|HAMAP-
CC       Rule:MF_01283, ECO:0000256|SAAS:SAAS00317943}.
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
CC       synthase family. {ECO:0000256|HAMAP-Rule:MF_01283}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {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   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-HAMAP.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003935; F:GTP cyclohydrolase II activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0009231; P:riboflavin biosynthetic process; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.90.870.10; -; 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; 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   Complete proteome {ECO:0000313|Proteomes:UP000015664};
KW   GTP-binding {ECO:0000256|HAMAP-Rule:MF_01283,
KW   ECO:0000256|SAAS:SAAS00415392};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01283,
KW   ECO:0000313|EMBL:EQC95357.1};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_01283,
KW   ECO:0000256|SAAS:SAAS00415349};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01283};
KW   Manganese {ECO:0000256|HAMAP-Rule:MF_01283};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01283,
KW   ECO:0000256|SAAS:SAAS00434439};
KW   Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_01283};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01283,
KW   ECO:0000256|SAAS:SAAS00415375};
KW   Riboflavin biosynthesis {ECO:0000256|HAMAP-Rule:MF_01283,
KW   ECO:0000256|SAAS:SAAS00434473};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_01283, ECO:0000256|SAAS:SAAS00415429}.
FT   DOMAIN      208    373       GTP_cyclohydro2. {ECO:0000259|Pfam:
FT                                PF00925}.
FT   NP_BIND     252    256       GTP. {ECO:0000256|HAMAP-Rule:MF_01283}.
FT   NP_BIND     295    297       GTP. {ECO:0000256|HAMAP-Rule:MF_01283}.
FT   REGION        1    201       DHBP synthase. {ECO:0000256|HAMAP-Rule:
FT                                MF_01283}.
FT   REGION       28     29       D-ribulose 5-phosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_01283}.
FT   REGION      140    144       D-ribulose 5-phosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_01283}.
FT   REGION      202    398       GTP cyclohydrolase II.
FT                                {ECO:0000256|HAMAP-Rule:MF_01283}.
FT   ACT_SITE    329    329       Proton acceptor; for GTP cyclohydrolase
FT                                activity. {ECO:0000256|HAMAP-Rule:
FT                                MF_01283}.
FT   ACT_SITE    331    331       Nucleophile; for GTP cyclohydrolase
FT                                activity. {ECO:0000256|HAMAP-Rule:
FT                                MF_01283}.
FT   METAL        29     29       Magnesium or manganese 1.
FT                                {ECO:0000256|HAMAP-Rule:MF_01283}.
FT   METAL        29     29       Magnesium or manganese 2.
FT                                {ECO:0000256|HAMAP-Rule:MF_01283}.
FT   METAL       143    143       Magnesium or manganese 2.
FT                                {ECO:0000256|HAMAP-Rule:MF_01283}.
FT   METAL       257    257       Zinc; catalytic. {ECO:0000256|HAMAP-Rule:
FT                                MF_01283}.
FT   METAL       268    268       Zinc; catalytic. {ECO:0000256|HAMAP-Rule:
FT                                MF_01283}.
FT   METAL       270    270       Zinc; catalytic. {ECO:0000256|HAMAP-Rule:
FT                                MF_01283}.
FT   BINDING      33     33       D-ribulose 5-phosphate.
FT                                {ECO:0000256|HAMAP-Rule:MF_01283}.
FT   BINDING     164    164       D-ribulose 5-phosphate.
FT                                {ECO:0000256|HAMAP-Rule:MF_01283}.
FT   BINDING     273    273       GTP. {ECO:0000256|HAMAP-Rule:MF_01283}.
FT   BINDING     317    317       GTP. {ECO:0000256|HAMAP-Rule:MF_01283}.
FT   BINDING     352    352       GTP. {ECO:0000256|HAMAP-Rule:MF_01283}.
FT   BINDING     357    357       GTP. {ECO:0000256|HAMAP-Rule:MF_01283}.
FT   SITE        126    126       Essential for DHBP synthase activity.
FT                                {ECO:0000256|HAMAP-Rule:MF_01283}.
FT   SITE        164    164       Essential for DHBP synthase activity.
FT                                {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
//