ID   RIBX_SHISS              Reviewed;         160 AA.
AC   Q3Z3Y7;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=N-glycosidase YbiA;
DE            EC=3.2.2.-;
DE   AltName: Full=Riboflavin biosynthesis intermediates N-glycosidase;
GN   Name=ybiA; OrderedLocusNames=SSON_0777;
OS   Shigella sonnei (strain Ss046).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300269;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ss046;
RX   PubMed=16275786; DOI=10.1093/nar/gki954;
RA   Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA   Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA   Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA   Jin Q.;
RT   "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT   bacillary dysentery.";
RL   Nucleic Acids Res. 33:6445-6458(2005).
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. Helps maintain flavin levels. May act on other substrates in vivo.
CC       Has no activity against GTP, nucleoside monophosphates or ADP-ribose.
CC       Is Required for swarming motility. {ECO:0000250|UniProtKB:P30176}.
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:0000250|UniProtKB:P30176};
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:0000250|UniProtKB:P30176};
CC   -!- SIMILARITY: Belongs to the YbiA family. {ECO:0000305}.
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DR   EMBL; CP000038; AAZ87525.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q3Z3Y7; -.
DR   BMRB; Q3Z3Y7; -.
DR   SMR; Q3Z3Y7; -.
DR   EnsemblBacteria; AAZ87525; AAZ87525; SSON_0777.
DR   KEGG; ssn:SSON_0777; -.
DR   HOGENOM; CLU_084247_3_1_6; -.
DR   OMA; WWPTSEH; -.
DR   Proteomes; UP000002529; Chromosome.
DR   GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR   GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
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   3: Inferred from homology;
KW   Glycosidase; Hydrolase.
FT   CHAIN           1..160
FT                   /note="N-glycosidase YbiA"
FT                   /id="PRO_0000287341"
SQ   SEQUENCE   160 AA;  18673 MW;  FE001561074501F4 CRC64;
     MPVRAQRIQH VMQDTIINFY STSDDYGDFS NFAAWPIKVD GKTWPTSEHY FQAQKFLDEK
     YREEIRRVSS PMVAARMGRN RSKPLRKNWE SVKEQVMRKA LRAKFEQHAE LRVLLLATAP
     AKLVEHTEND AYWGDGGNGK GKNRLGYLLM ELREQLAIEK