ID A0A6G1EH35_9ORYZ Unreviewed; 338 AA.
AC A0A6G1EH35;
DT 12-AUG-2020, integrated into UniProtKB/TrEMBL.
DT 12-AUG-2020, sequence version 1.
DT 27-MAR-2024, entry version 9.
DE RecName: Full=5'-nucleotidase {ECO:0000256|ARBA:ARBA00012643};
DE EC=3.1.3.5 {ECO:0000256|ARBA:ARBA00012643};
GN ORFNames=E2562_006684 {ECO:0000313|EMBL:KAF0923712.1};
OS Oryza meyeriana var. granulata.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza meyeriana.
OX NCBI_TaxID=110450 {ECO:0000313|EMBL:KAF0923712.1, ECO:0000313|Proteomes:UP000479710};
RN [1] {ECO:0000313|EMBL:KAF0923712.1, ECO:0000313|Proteomes:UP000479710}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Menghai {ECO:0000313|Proteomes:UP000479710};
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF0923712.1};
RA Li W.;
RT "Whole genome sequence of Oryza granulata.";
RL Submitted (NOV-2019) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAF0923712.1}.
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DR EMBL; SPHZ02000003; KAF0923712.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A6G1EH35; -.
DR Proteomes; UP000479710; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
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:UP000479710}.
SQ SEQUENCE 338 AA; 37556 MW; 302D10568FC2484E CRC64;
MTSPPLLSPS PSSTSRLLLR LLLSRRRSPT PCSPPPPLRR CLPLLAASMS SSSSAAATRN
FGSVVADADG LARKVIADFD GTLTRYWYDG ARGQSSHGLL RQGNKEYDAK REELFEHYHP
IEINPDIPLP EKAKLMEEWW EKTHGLLIEG GLTYEAIKKS VADAKIAFRD GVVDLFEFLE
ERDIPVLVFS AGLADIIEEV FRQKLHRSFK NIKIVSNRMV FNEEGHLVSF KGKTIHVLNK
NEHALDMAAP VHDNLGDPNG STDDYSLVKK RTNVLLLGDH IGDLGMSDGL NYENRIAVGF
LNNNIEKSLI DYSEAFDIVY LNDAPMLGVV ELASELCP
//
