ID   RIBX_SHIFL              Reviewed;         160 AA.
AC   Q83LU8; Q7C2G6;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 99.
DE   RecName: Full=N-glycosidase YbiA;
DE            EC=3.2.2.-;
DE   AltName: Full=Riboflavin biosynthesis intermediates N-glycosidase;
GN   Name=ybiA; OrderedLocusNames=SF0749, S0789;
OS   Shigella flexneri.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=301 / Serotype 2a;
RX   PubMed=12384590; DOI=10.1093/nar/gkf566;
RA   Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA   Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA   Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA   Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT   "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT   through comparison with genomes of Escherichia coli K12 and O157.";
RL   Nucleic Acids Res. 30:4432-4441(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX   PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA   Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA   Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA   Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT   "Complete genome sequence and comparative genomics of Shigella flexneri
RT   serotype 2a strain 2457T.";
RL   Infect. Immun. 71:2775-2786(2003).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE005674; AAN42383.1; -; Genomic_DNA.
DR   EMBL; AE014073; AAP16260.1; -; Genomic_DNA.
DR   RefSeq; NP_706676.1; NC_004337.2.
DR   RefSeq; WP_001145124.1; NZ_WPGW01000030.1.
DR   AlphaFoldDB; Q83LU8; -.
DR   SMR; Q83LU8; -.
DR   STRING; 198214.SF0749; -.
DR   EnsemblBacteria; AAN42383; AAN42383; SF0749.
DR   EnsemblBacteria; AAP16260; AAP16260; S0789.
DR   GeneID; 1023696; -.
DR   KEGG; sfl:SF0749; -.
DR   KEGG; sfx:S0789; -.
DR   PATRIC; fig|198214.7.peg.869; -.
DR   HOGENOM; CLU_084247_3_1_6; -.
DR   OMA; WWPTSEH; -.
DR   Proteomes; UP000001006; Chromosome.
DR   Proteomes; UP000002673; 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; Reference proteome.
FT   CHAIN           1..160
FT                   /note="N-glycosidase YbiA"
FT                   /id="PRO_0000287339"
SQ   SEQUENCE   160 AA;  18629 MW;  AB0015667247722A CRC64;
     MPVRAQRIQH VMQDTIINFY STSDDYGDFS NFAARPIKVD GNTWPTSEHY FQAQKFLDEK
     YREEIRRVSS PMVAARMGRN RSKPLRKNWE SVKEQVMRKA LRAKFEQHAE LRVLLLATAP
     AKLVEHTEND AYWGDGGNGK GKNRLGYLLM ELREQLAIEK