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Entry: I1NHU7_SOYBN
LinkDB: I1NHU7_SOYBN
Original site: I1NHU7_SOYBN 
ID   I1NHU7_SOYBN            Unreviewed;       346 AA.
AC   I1NHU7;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   RecName: Full=5'-nucleotidase {ECO:0000256|ARBA:ARBA00012643};
DE            EC=3.1.3.5 {ECO:0000256|ARBA:ARBA00012643};
GN   Name=100815584 {ECO:0000313|EnsemblPlants:KRG92162};
GN   ORFNames=GLYMA_20G195000 {ECO:0000313|EMBL:KRG92162.1};
OS   Glycine max (Soybean) (Glycine hispida).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC   Glycine subgen. Soja.
OX   NCBI_TaxID=3847 {ECO:0000313|EnsemblPlants:KRG92162};
RN   [1] {ECO:0000313|EMBL:KRG92162.1, ECO:0000313|EnsemblPlants:KRG92162}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRG92162};
RC   TISSUE=Callus {ECO:0000313|EMBL:KRG92162.1};
RX   PubMed=20075913; DOI=10.1038/nature08670;
RA   Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA   Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D.,
RA   Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D.,
RA   Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D.,
RA   Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N.,
RA   Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K.,
RA   Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D.,
RA   Stacey G., Shoemaker R.C., Jackson S.A.;
RT   "Genome sequence of the palaeopolyploid soybean.";
RL   Nature 463:178-183(2010).
RN   [2] {ECO:0000313|EnsemblPlants:KRG92162}
RP   IDENTIFICATION.
RC   STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRG92162};
RG   EnsemblPlants;
RL   Submitted (FEB-2018) to UniProtKB.
RN   [3] {ECO:0000313|EMBL:KRG92162.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Callus {ECO:0000313|EMBL:KRG92162.1};
RA   Schmutz J., Cannon S., Schlueter J., Ma J., Mitros T., Nelson W., Hyten D.,
RA   Song Q., Thelen J., Cheng J., Xu D., Hellsten U., May G., Yu Y.,
RA   Sakurai T., Umezawa T., Bhattacharyya M., Sandhu D., Valliyodan B.,
RA   Lindquist E., Peto M., Grant D., Shu S., Goodstein D., Barry K.,
RA   Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N., Joshi T.,
RA   Libault M., Sethuraman A., Zhang X., Shinozaki K., Nguyen H., Wing R.,
RA   Cregan P., Specht J., Grimwood J., Rokhsar D., Stacey G., Shoemaker R.,
RA   Jackson S.;
RT   "WGS assembly of Glycine max.";
RL   Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ribonucleoside 5'-phosphate + H2O = a ribonucleoside +
CC         phosphate; Xref=Rhea:RHEA:12484, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:18254, ChEBI:CHEBI:43474, ChEBI:CHEBI:58043; EC=3.1.3.5;
CC         Evidence={ECO:0000256|ARBA:ARBA00000815};
CC   -!- SIMILARITY: Belongs to the pyrimidine 5'-nucleotidase family.
CC       {ECO:0000256|ARBA:ARBA00008389}.
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DR   EMBL; CM000853; KRG92162.1; -; Genomic_DNA.
DR   RefSeq; XP_003556315.1; XM_003556267.3.
DR   AlphaFoldDB; I1NHU7; -.
DR   SMR; I1NHU7; -.
DR   STRING; 3847.I1NHU7; -.
DR   PaxDb; 3847-GLYMA20G33690-1; -.
DR   EnsemblPlants; KRG92162; KRG92162; GLYMA_20G195000.
DR   GeneID; 100815584; -.
DR   Gramene; KRG92162; KRG92162; GLYMA_20G195000.
DR   KEGG; gmx:100815584; -.
DR   eggNOG; KOG3128; Eukaryota.
DR   HOGENOM; CLU_048584_1_0_1; -.
DR   InParanoid; I1NHU7; -.
DR   OMA; GPERMQI; -.
DR   OrthoDB; 531581at2759; -.
DR   Proteomes; UP000008827; Chromosome 20.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0008253; F:5'-nucleotidase activity; IBA:GO_Central.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0106411; F:XMP 5'-nucleosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR   Gene3D; 1.10.150.340; Pyrimidine 5'-nucleotidase (UMPH-1), N-terminal domain; 1.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR006434; Pyrimidine_nucleotidase_eu.
DR   PANTHER; PTHR13045; 5'-NUCLEOTIDASE; 1.
DR   PANTHER; PTHR13045:SF0; CYTOSOLIC 5'-NUCLEOTIDASE 3A; 1.
DR   Pfam; PF05822; UMPH-1; 1.
DR   SFLD; SFLDG01128; C1.4:_5'-Nucleotidase_Like; 1.
DR   SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide metabolism {ECO:0000256|ARBA:ARBA00023080};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008827}.
SQ   SEQUENCE   346 AA;  38997 MW;  C03CC76726D40612 CRC64;
     MSHRLQLQGI FVTSFRQRHF SFFSPYTSTT TRVSFSSSSC GKNLQMEEVK VASDLLVGDP
     ASLEKKIDAI RLGGPQKLQV IADFDATLTK FWVNGTRGQT SHGLLQQGNP EYDAKRQQLY
     EYYHPLEFSP TIGLEEKTKL MEEWWGKTHG LLVEGGLTYD SIRQSVANAN IAFREGVSEL
     FEFLEERDIP VLIFSAGLAD IIEEVLRQKL HRSFKNVRIV SNRMVFDDDG RLVSFKGKLI
     HSLNKNEHAL DMAAPVHERL GDMDGPTDDN SSLKKRTNVL LLGDHTGDLG MSDGLNYETR
     ISMGFLNHNV ENSLSCYQEA FDVVFVNDAP MWGVIKLVSH MCLSGR
//
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