ISN1_KLULA
ID ISN1_KLULA Reviewed; 422 AA.
AC Q6CY84;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 25-MAY-2022, entry version 88.
DE RecName: Full=IMP-specific 5'-nucleotidase 1;
DE EC=3.1.3.99 {ECO:0000250|UniProtKB:Q99312};
GN Name=ISN1; OrderedLocusNames=KLLA0A02365g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
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; CR382121; CAH02693.1; -; Genomic_DNA.
DR RefSeq; XP_451105.1; XM_451105.1.
DR AlphaFoldDB; Q6CY84; -.
DR SMR; Q6CY84; -.
DR STRING; 28985.XP_451105.1; -.
DR EnsemblFungi; CAH02693; CAH02693; KLLA0_A02365g.
DR GeneID; 2896792; -.
DR KEGG; kla:KLLA0_A02365g; -.
DR eggNOG; ENOG502QR24; Eukaryota.
DR HOGENOM; CLU_031816_1_0_1; -.
DR InParanoid; Q6CY84; -.
DR OMA; FKARLAC; -.
DR Proteomes; UP000000598; Chromosome A.
DR GO; GO:0050483; F:IMP 5'-nucleotidase activity; IEA:EnsemblFungi.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0006190; P:inosine salvage; IEA:EnsemblFungi.
DR GO; GO:0071590; P:nicotinamide riboside biosynthetic process; IEA:EnsemblFungi.
DR GO; GO:0071592; P:nicotinic acid riboside biosynthetic process; IEA:EnsemblFungi.
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..422
FT /note="IMP-specific 5'-nucleotidase 1"
FT /id="PRO_0000084253"
SQ SEQUENCE 422 AA; 47466 MW; 3FBA59843960B810 CRC64;
MSSRYRVEYN LKVHKKDAFI EWIKGLLAVP FVLQAGTDSG AERTYKQYCS IFSDIENLVS
QKIEIQNRRR QLGSLEEARL DQLVPQVGTF FTHLPLVEAF EVQNRRRAIC SRKMVSPSFN
DIRHILNSAQ ILALLKSKEL KLVTFDGDVT LYEDGGSIER GGKIVTRIIT LLKRGINVGV
VTAAGYDDPD KYKERLYGLC FALFSDKSMS LEQKSKLTVM GGESNYLFQY FETSEQFGFK
SIDDDEWVPS SVKAWSDDDI DATLDVAQTC FGELSHLLAL PSKCQIIRKK RAVGFVPGFI
FDDELEVNVK IKIPREALEE MVLVVQKKLE SYPPAQNIQF SCFDGGSDVW CDIGGKDLGV
SILQNFYQTD SPITAAQTLH IGDQFAPKGS ANDFKARSAG CTLWISSPRE TIEVLDDLLP
YL