ID   RIBX_NOSP7              Reviewed;         156 AA.
AC   B2J4E5;
DT   16-SEP-2015, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   25-MAY-2022, entry version 54.
DE   RecName: Full=N-glycosidase Npun_R5314 {ECO:0000305|PubMed:25431972};
DE            EC=3.2.2.- {ECO:0000269|PubMed:25431972};
DE   AltName: Full=Riboflavin biosynthesis intermediates N-glycosidase {ECO:0000305|PubMed:25431972};
GN   OrderedLocusNames=Npun_R5314 {ECO:0000312|EMBL:ACC83635.1};
OS   Nostoc punctiforme (strain ATCC 29133 / PCC 73102).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=63737;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29133 / PCC 73102;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Meeks J.C., Elhai J.,
RA   Campbell E.L., Thiel T., Longmire J., Potts M., Atlas R.;
RT   "Complete sequence of chromosome of Nostoc punctiforme ATCC 29133.";
RL   Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY.
RX   PubMed=25431972; DOI=10.1042/bj20141237;
RA   Frelin O., Huang L., Hasnain G., Jeffryes J.G., Ziemak M.J., Rocca J.R.,
RA   Wang B., Rice J., Roje S., Yurgel S.N., Gregory J.F. III, Edison A.S.,
RA   Henry C.S., de Crecy-Lagard V., Hanson A.D.;
RT   "A directed-overflow and damage-control N-glycosidase in riboflavin
RT   biosynthesis.";
RL   Biochem. J. 466:137-145(2015).
CC   -!- FUNCTION: Catalyzes the hydrolysis of the N-glycosidic bond in the
CC       first two intermediates of riboflavin biosynthesis, which are highly
CC       reactive metabolites, yielding relatively innocuous products. Thus, can
CC       divert a surplus of harmful intermediates into relatively harmless
CC       products and pre-empt the damage these intermediates would otherwise
CC       do. May act on other substrates in vivo. Has no activity against GTP,
CC       nucleoside monophosphates or ADP-ribose. {ECO:0000269|PubMed:25431972}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)-pyrimidine +
CC         H2O = 2,5,6-triamino-4-hydroxypyrimidine + D-ribose 5-phosphate;
CC         Xref=Rhea:RHEA:23436, ChEBI:CHEBI:15377, ChEBI:CHEBI:58614,
CC         ChEBI:CHEBI:78346, ChEBI:CHEBI:137796;
CC         Evidence={ECO:0000269|PubMed:25431972};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-amino-6-(5-phospho-D-ribosylamino)uracil + H2O = 5,6-
CC         diaminouracil + D-ribose 5-phosphate; Xref=Rhea:RHEA:55020,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:46252, ChEBI:CHEBI:58453,
CC         ChEBI:CHEBI:78346; Evidence={ECO:0000269|PubMed:25431972};
CC   -!- SIMILARITY: Belongs to the YbiA family. {ECO:0000305}.
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DR   EMBL; CP001037; ACC83635.1; -; Genomic_DNA.
DR   RefSeq; WP_012411586.1; NC_010628.1.
DR   AlphaFoldDB; B2J4E5; -.
DR   SMR; B2J4E5; -.
DR   STRING; 63737.Npun_R5314; -.
DR   EnsemblBacteria; ACC83635; ACC83635; Npun_R5314.
DR   KEGG; npu:Npun_R5314; -.
DR   eggNOG; COG3236; Bacteria.
DR   HOGENOM; CLU_084247_3_1_3; -.
DR   OMA; YFWGCGA; -.
DR   OrthoDB; 1726046at2; -.
DR   PhylomeDB; B2J4E5; -.
DR   Proteomes; UP000001191; Chromosome.
DR   GO; GO:0016799; F:hydrolase activity, hydrolyzing N-glycosyl compounds; IDA:UniProtKB.
DR   GO; GO:1901135; P:carbohydrate derivative metabolic process; IDA:UniProtKB.
DR   CDD; cd15457; NADAR; 1.
DR   Gene3D; 1.10.357.40; -; 1.
DR   InterPro; IPR012816; NADAR.
DR   InterPro; IPR037238; YbiA-like_sf.
DR   Pfam; PF08719; NADAR; 1.
DR   SUPFAM; SSF143990; SSF143990; 1.
DR   TIGRFAMs; TIGR02464; ribofla_fusion; 1.
PE   1: Evidence at protein level;
KW   Glycosidase; Hydrolase; Reference proteome.
FT   CHAIN           1..156
FT                   /note="N-glycosidase Npun_R5314"
FT                   /id="PRO_0000433625"
SQ   SEQUENCE   156 AA;  17748 MW;  0BB2909133D7DDE4 CRC64;
     MTIYFYKVWQ PYGCFSNFSP HGIHIQDTYW ATVEHYYQAQ KFVGSKDAAI IPLIHAAATP
     EEAAALGRCS TRQLRRDWDL VKTQIMREAV LKKFLTHADI REVLLKTGDE LLVENSPTDS
     FWGCGANKAG LNHLGKTLMS VREEIRNLLS LTGIYE