ID   ISN1_ASHGO              Reviewed;         425 AA.
AC   Q75EG6;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=IMP-specific 5'-nucleotidase 1;
DE            EC=3.1.3.99 {ECO:0000250|UniProtKB:Q99312};
GN   Name=ISN1; OrderedLocusNames=AAR112C;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
CC   -!- FUNCTION: IMP-specific 5'-nucleotidase involved in IMP (inositol
CC       monophosphate) degradation. {ECO:0000250|UniProtKB:Q99312}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + IMP = inosine + phosphate; Xref=Rhea:RHEA:27718,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:17596, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:58053; EC=3.1.3.99;
CC         Evidence={ECO:0000250|UniProtKB:Q99312};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:Q99312};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:Q99312}.
CC   -!- SIMILARITY: Belongs to the ISN1 family. {ECO:0000305}.
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DR   EMBL; AE016814; AAS50478.1; -; Genomic_DNA.
DR   RefSeq; NP_982654.1; NM_208007.1.
DR   AlphaFoldDB; Q75EG6; -.
DR   SMR; Q75EG6; -.
DR   STRING; 33169.AAS50478; -.
DR   PRIDE; Q75EG6; -.
DR   EnsemblFungi; AAS50478; AAS50478; AGOS_AAR112C.
DR   GeneID; 4618586; -.
DR   KEGG; ago:AGOS_AAR112C; -.
DR   eggNOG; ENOG502QR24; Eukaryota.
DR   HOGENOM; CLU_031816_1_0_1; -.
DR   OMA; FKARLAC; -.
DR   Proteomes; UP000000591; Chromosome I.
DR   GO; GO:0050483; F:IMP 5'-nucleotidase activity; IBA:GO_Central.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0006190; P:inosine salvage; IBA:GO_Central.
DR   GO; GO:0071590; P:nicotinamide riboside biosynthetic process; IBA:GO_Central.
DR   GO; GO:0071592; P:nicotinic acid riboside biosynthetic process; IBA:GO_Central.
DR   GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR009453; ISN1.
DR   PANTHER; PTHR28213; PTHR28213; 1.
DR   Pfam; PF06437; ISN1; 1.
DR   PIRSF; PIRSF028836; ISN1; 1.
DR   SUPFAM; SSF56784; SSF56784; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Magnesium; Nucleotide metabolism; Reference proteome.
FT   CHAIN           1..425
FT                   /note="IMP-specific 5'-nucleotidase 1"
FT                   /id="PRO_0000084246"
SQ   SEQUENCE   425 AA;  48003 MW;  0CE652360E3617B3 CRC64;
     MSSRYRVEYQ LKAHRKDAFI EWIKGLLAVP FVLHSVTERD NAQEKYRRVF EDVETLINEK
     ITVDSDESLT RAAGVSRLDK LVPTIGTFFT PLPLTEAFLR QNARRAISER AYVSPSFNDI
     RHILNTAQIV QLARAGELSL VTFDGDVTLY EDGASLAAED KVIGRLLRLL GAGMHVGIVT
     AAGYDDAENY ERRLFGLLRR LERADLPNEA KRRLCVMGGE SNFLFRCYER DGRAGFERVP
     ESVWMSAELH QWNQQDINAT LDLAEVMLRA LREKLRLPAE TQIIRKVRAV GIVPGQRFDP
     ELGREIRVPL LRETLEEIVL TVQGRLENFP PAQRVQFSCF DGGSDVWCDI GGKDLGVAFL
     QRFYSPERPI RPEQSLHVGD QFAPVGSAND FKARLAGCTA WISSPQETVA LLDDLLAELE
     AQKNM