ISN1_YARLI
ID ISN1_YARLI Reviewed; 420 AA.
AC Q6C673;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 25-MAY-2022, entry version 87.
DE RecName: Full=IMP-specific 5'-nucleotidase 1;
DE EC=3.1.3.99 {ECO:0000250|UniProtKB:Q99312};
GN Name=ISN1; OrderedLocusNames=YALI0E11913g;
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150;
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; CR382131; CAG79432.1; -; Genomic_DNA.
DR RefSeq; XP_503839.1; XM_503839.1.
DR AlphaFoldDB; Q6C673; -.
DR SMR; Q6C673; -.
DR STRING; 4952.CAG79432; -.
DR EnsemblFungi; CAG79432; CAG79432; YALI0_E11913g.
DR GeneID; 2912803; -.
DR KEGG; yli:YALI0E11913g; -.
DR VEuPathDB; FungiDB:YALI0_E11913g; -.
DR HOGENOM; CLU_031816_1_0_1; -.
DR InParanoid; Q6C673; -.
DR OMA; FKARLAC; -.
DR Proteomes; UP000001300; Chromosome E.
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..420
FT /note="IMP-specific 5'-nucleotidase 1"
FT /id="PRO_0000084256"
SQ SEQUENCE 420 AA; 47198 MW; 7DD869A58FCAED59 CRC64;
MTSRYRVEYS LKQHRRDEFI EWVKTLLATP FVLHAGSTGD GRPGDENRSV VETRRRYAEI
FYDVEKLIEN QLYHDNNDSG ERARLRQLVP TIGQFFTKLP LERAFYTQDE IRSISHRRFV
SPSFNDVRMI LNTAQVMALA TGRQPLKLVT FDGDVTLYAD GGNIDPDSPI IPVLLGLLRN
DVYVGIVTAA GYSEKDGSKY GVRLYGLLEA IVKTDTLTEQ QKNHLLVMGG ESNFLFKFIA
AENRFEWIDP EEWTLPEVRT WSQEDITSVL NIGERVFTNA LTKCSLPATI IRKVRGVGIV
PLPGKKIMRE QLEEMVLAAQ KTLETSKATG NVQFCAFNGG SDVWVDIGDK DLGVRSLQAY
LGNITGTQTL HVGDQFAALG ANDFKARLAA TTVWIANPSE TVEIIAELID YIEHERQCSA