ID   RIBX_MIMIV              Reviewed;         170 AA.
AC   Q5UR67;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   07-OCT-2020, entry version 55.
DE   RecName: Full=N-glycosidase R617;
DE            EC=3.2.2.-;
DE   AltName: Full=Riboflavin biosynthesis intermediates N-glycosidase;
GN   OrderedLocusNames=MIMI_R617;
OS   Acanthamoeba polyphaga mimivirus (APMV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC   Imitervirales; Mimiviridae; Mimivirus.
OX   NCBI_TaxID=212035;
OH   NCBI_TaxID=5757; Acanthamoeba polyphaga (Amoeba).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Rowbotham-Bradford;
RX   PubMed=15486256; DOI=10.1126/science.1101485;
RA   Raoult D., Audic S., Robert C., Abergel C., Renesto P., Ogata H.,
RA   La Scola B., Susan M., Claverie J.-M.;
RT   "The 1.2-megabase genome sequence of Mimivirus.";
RL   Science 306:1344-1350(2004).
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.
CC       {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; AY653733; AAV50879.1; -; Genomic_DNA.
DR   RefSeq; YP_003987134.1; NC_014649.1.
DR   SMR; Q5UR67; -.
DR   GeneID; 9925257; -.
DR   KEGG; vg:9925257; -.
DR   Proteomes; UP000001134; Genome.
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..170
FT                   /note="N-glycosidase R617"
FT                   /id="PRO_0000244050"
SQ   SEQUENCE   170 AA;  19894 MW;  B08C5F5A0AAF9784 CRC64;
     METDKYVFFH GANKNQAGVH IFSQWFPVNF KEYLNGEEFA EYVSAEQYMM AHKALLFGDM
     FHFKKIMECS KQCKIKYLGR RVRNFNPTIW DKHKFDIVTE GNRLKFSQNP DLMKRLLETG
     NKTIVEASPS DKIWGIGLTA QQAVNIPENK WPGKNLLGKV LMKIREENQQ