ID   ISN1_DEBHA              Reviewed;         485 AA.
AC   Q6BIV1;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=IMP-specific 5'-nucleotidase 1;
DE            EC=3.1.3.99 {ECO:0000250|UniProtKB:Q99312};
GN   Name=ISN1; OrderedLocusNames=DEHA2G07414g;
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS   / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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; CR382139; CAG90331.2; -; Genomic_DNA.
DR   RefSeq; XP_461870.2; XM_461870.1.
DR   AlphaFoldDB; Q6BIV1; -.
DR   SMR; Q6BIV1; -.
DR   STRING; 4959.XP_461870.2; -.
DR   EnsemblFungi; CAG90331; CAG90331; DEHA2G07414g.
DR   GeneID; 2904750; -.
DR   KEGG; dha:DEHA2G07414g; -.
DR   VEuPathDB; FungiDB:DEHA2G07414g; -.
DR   eggNOG; ENOG502QR24; Eukaryota.
DR   HOGENOM; CLU_031816_1_0_1; -.
DR   InParanoid; Q6BIV1; -.
DR   OMA; FKARLAC; -.
DR   OrthoDB; 1219919at2759; -.
DR   Proteomes; UP000000599; Chromosome G.
DR   GO; GO:0050483; F:IMP 5'-nucleotidase activity; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0006190; P:inosine salvage; IEA:InterPro.
DR   GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR009453; ISN1.
DR   PANTHER; PTHR28213; PTHR28213; 1.
DR   Pfam; PF06437; ISN1; 1.
DR   PIRSF; PIRSF028836; ISN1; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Magnesium; Nucleotide metabolism; Reference proteome.
FT   CHAIN           1..485
FT                   /note="IMP-specific 5'-nucleotidase 1"
FT                   /id="PRO_0000084250"
SQ   SEQUENCE   485 AA;  55584 MW;  DC3C74B9DFDF5686 CRC64;
     MTSRYRVEYA LKSHRRDEFI EWIKGLLAVP FVLHADVENY DTDFMKHYED PEAYEDYLLS
     REYEIALECQ NRYKEIFADV EKLVNHAIII DKLQDKNPTY VDTSRLRKLV PSVGRFFTPL
     PLTEAFLVED SRRSISKRRL VSPSFNDVRS ILNTAQVLAL AKMYQDSDES GSRLKLITFD
     GDVTLYADGS SLTPDAPVID KLIKLLSMNL FIGVVTAAGY PGQSGVPQYY ERLKGLIDRI
     RTTPELNDHQ RENLLVMGGE SNYLFRYDNE FGNLKFIEAD EWYLPIMSSW DKLKIDYIMS
     TTDKHLKHLQ KKFKLDDMDK TTIIRKERSI GIIPNPGYRI LREHLEEMVL SCSMKLQEIL
     ARTARTPVNM EIVNQLDTSQ AVSTQNAADD HIKVCAFNGG SDVWVDIGDK SLGVESLQKY
     LCKDVKYEHK VCPILKSESL HIGDQFASLG ANDFKARLSA CTVWIASPRE TVAILEDLIQ
     HLSNK