ID   RIBX_SHIF8              Reviewed;         160 AA.
AC   Q0T6G3;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   25-MAY-2022, entry version 71.
DE   RecName: Full=N-glycosidase YbiA;
DE            EC=3.2.2.-;
DE   AltName: Full=Riboflavin biosynthesis intermediates N-glycosidase;
GN   Name=ybiA; OrderedLocusNames=SFV_0782;
OS   Shigella flexneri serotype 5b (strain 8401).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=373384;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=8401;
RX   PubMed=16822325; DOI=10.1186/1471-2164-7-173;
RA   Nie H., Yang F., Zhang X., Yang J., Chen L., Wang J., Xiong Z., Peng J.,
RA   Sun L., Dong J., Xue Y., Xu X., Chen S., Yao Z., Shen Y., Jin Q.;
RT   "Complete genome sequence of Shigella flexneri 5b and comparison with
RT   Shigella flexneri 2a.";
RL   BMC Genomics 7:173-173(2006).
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; CP000266; ABF03014.1; -; Genomic_DNA.
DR   RefSeq; WP_001145124.1; NC_008258.1.
DR   AlphaFoldDB; Q0T6G3; -.
DR   SMR; Q0T6G3; -.
DR   EnsemblBacteria; ABF03014; ABF03014; SFV_0782.
DR   KEGG; sfv:SFV_0782; -.
DR   HOGENOM; CLU_084247_3_1_6; -.
DR   OMA; WWPTSEH; -.
DR   Proteomes; UP000000659; 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_0000287340"
SQ   SEQUENCE   160 AA;  18629 MW;  AB0015667247722A CRC64;
     MPVRAQRIQH VMQDTIINFY STSDDYGDFS NFAARPIKVD GNTWPTSEHY FQAQKFLDEK
     YREEIRRVSS PMVAARMGRN RSKPLRKNWE SVKEQVMRKA LRAKFEQHAE LRVLLLATAP
     AKLVEHTEND AYWGDGGNGK GKNRLGYLLM ELREQLAIEK