Y1459_SYNY3
ID Y1459_SYNY3 Reviewed; 225 AA.
AC P73440;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Putative 5'-nucleotidase alr3139;
DE EC=3.1.3.5;
DE AltName: Full=Nucleoside 5'-monophosphate phosphohydrolase;
GN OrderedLocusNames=sll1459;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
CC -!- FUNCTION: Nucleotidase that shows phosphatase activity on nucleoside
CC 5'-monophosphates. {ECO:0000250}.
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 -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000250};
CC Note=Binds 1 divalent metal cation per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the SurE nucleotidase family. {ECO:0000305}.
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DR EMBL; BA000022; BAA17480.1; -; Genomic_DNA.
DR PIR; S77377; S77377.
DR AlphaFoldDB; P73440; -.
DR SMR; P73440; -.
DR STRING; 1148.1652559; -.
DR PaxDb; P73440; -.
DR EnsemblBacteria; BAA17480; BAA17480; BAA17480.
DR KEGG; syn:sll1459; -.
DR eggNOG; COG0496; Bacteria.
DR InParanoid; P73440; -.
DR OMA; YVGEYGK; -.
DR PhylomeDB; P73440; -.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0106411; F:XMP 5'-nucleosidase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.40.1210.10; -; 1.
DR InterPro; IPR030048; SurE.
DR InterPro; IPR002828; SurE-like_Pase/nucleotidase.
DR InterPro; IPR036523; SurE-like_sf.
DR PANTHER; PTHR30457; PTHR30457; 1.
DR Pfam; PF01975; SurE; 1.
DR SUPFAM; SSF64167; SSF64167; 1.
DR TIGRFAMs; TIGR00087; surE; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Hydrolase; Metal-binding; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..225
FT /note="Putative 5'-nucleotidase alr3139"
FT /id="PRO_0000111873"
FT BINDING 8
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 9
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 37
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 88
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
SQ SEQUENCE 225 AA; 24907 MW; 42CF7E02A02AECC2 CRC64;
MNFLLTNDDG IDAPGIEALY EALGKRGVWV APKNQHSGCG HKVTTDQAIA VEQRGKNRYA
VDGTPADCTR LGVVHFYPEV DWVIAGINAG GNMGIDSYLS GTVAAVREAA ILGHKAIAIS
HWINKPRTIN WAWASHWANA VFNTLWQQDL PPQHFWNVNL PHWQSGDPEP EVIFCEPSRD
PLPVAFTIEG SNFFYRGEYS QRPRQPGSDI DVCFSGNIAI TQLRV