ID J3MXL7_ORYBR Unreviewed; 535 AA.
AC J3MXL7;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=5'-nucleotidase {ECO:0008006|Google:ProtNLM};
GN Name=102718483 {ECO:0000313|EnsemblPlants:OB09G17460.1};
OS Oryza brachyantha (malo sina).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4533 {ECO:0000313|EnsemblPlants:OB09G17460.1};
RN [1] {ECO:0000313|EnsemblPlants:OB09G17460.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IRGC 101232 {ECO:0000313|EnsemblPlants:OB09G17460.1};
RX PubMed=23481403;
RA Chen J., Huang Q., Gao D., Wang J., Lang Y., Liu T., Li B., Bai Z.,
RA Luis Goicoechea J., Liang C., Chen C., Zhang W., Sun S., Liao Y., Zhang X.,
RA Yang L., Song C., Wang M., Shi J., Liu G., Liu J., Zhou H., Zhou W., Yu Q.,
RA An N., Chen Y., Cai Q., Wang B., Liu B., Min J., Huang Y., Wu H., Li Z.,
RA Zhang Y., Yin Y., Song W., Jiang J., Jackson S.A., Wing R.A., Wang J.,
RA Chen M.;
RT "Whole-genome sequencing of Oryza brachyantha reveals mechanisms underlying
RT Oryza genome evolution.";
RL Nat. Commun. 4:1595-1595(2013).
RN [2] {ECO:0000313|EnsemblPlants:OB09G17460.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2013) to UniProtKB.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|PIRSR:PIRSR017434-2};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|PIRSR:PIRSR017434-2};
CC -!- SIMILARITY: Belongs to the 5'(3')-deoxyribonucleotidase family.
CC {ECO:0000256|ARBA:ARBA00009589}.
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DR RefSeq; XP_006660641.2; XM_006660578.2.
DR AlphaFoldDB; J3MXL7; -.
DR STRING; 4533.J3MXL7; -.
DR EnsemblPlants; OB09G17460.1; OB09G17460.1; OB09G17460.
DR GeneID; 102718483; -.
DR Gramene; OB09G17460.1; OB09G17460.1; OB09G17460.
DR KEGG; obr:102718483; -.
DR eggNOG; KOG2470; Eukaryota.
DR HOGENOM; CLU_017845_5_2_1; -.
DR OMA; WSRYKEA; -.
DR OrthoDB; 3626840at2759; -.
DR Proteomes; UP000006038; Chromosome 9.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd07522; HAD_cN-II; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR008380; HAD-SF_hydro_IG_5-nucl.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR016695; Pur_nucleotidase.
DR NCBIfam; TIGR02244; HAD-IG-Ncltidse; 1.
DR PANTHER; PTHR12103; 5'-NUCLEOTIDASE DOMAIN-CONTAINING; 1.
DR PANTHER; PTHR12103:SF12; 5'-NUCLEOTIDASE DOMAIN-CONTAINING PROTEIN 1; 1.
DR Pfam; PF05761; 5_nucleotid; 1.
DR PIRSF; PIRSF017434; Purine_5'-nucleotidase; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR017434-2};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR017434-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000006038};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..535
FT /note="5'-nucleotidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003775323"
FT ACT_SITE 97
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR017434-1"
FT ACT_SITE 99
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR017434-1"
FT BINDING 97
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR017434-2"
FT BINDING 99
FT /ligand="GMP"
FT /ligand_id="ChEBI:CHEBI:58115"
FT /evidence="ECO:0000256|PIRSR:PIRSR017434-2"
FT BINDING 380
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR017434-2"
SQ SEQUENCE 535 AA; 61859 MW; A01965F7D573B0A5 CRC64;
MAAARLRLLS LGFLSPAVSW PRHSSRQGLR AMSTLSTTLG SGAGEDEIER IRREFEDAKR
NYLSIPVAIK DMPKMNPQGI YVNKNVKLDD LQVYGFDYDY TLSHYSEHLQ CLIYDLAKKH
LVNELKYPES CLKYEYDRSF PIRGLYYDRL KGCLLKLDFF GSIEPDGCFF GRRKLNLSEI
KELYGTRHIG RDQARQLVGL MDVFCFSEAC LIADTVQQFV DAKLEFDASY VYEDVNQSIQ
HVHRSGLIHR KILSEPQKYL IKNSQVFRFL KMLREKDKKL FLLTNSPFYF VDGGMSYLLE
DEHFDGNSWR ELFDVVIAQA NKPTFYNSDH PFRVYDTQKD TLAFTAVDKF LPNEVYYHGC
LKSFLQITKW RGPEVIYFGD HLLSDLRGPS KAGWRTAAVI RELEDEIEIQ NGENYRFQQA
KLSIIHDLLG KVHATVVSTE KGQVYRALLD ELNAERRQCR SAMRDLFNSS FGATFLTDTG
RESSFAYHIH QYADIYTSKL ENFLSYAPES WLHPPHDIKI MPHNAKVPAS LFSGS
//
