Y3139_NOSS1
ID Y3139_NOSS1 Reviewed; 226 AA.
AC Q8YSE9;
DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 05-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Putative 5'-nucleotidase alr3139;
DE EC=3.1.3.5;
DE AltName: Full=Nucleoside 5'-monophosphate phosphohydrolase;
GN OrderedLocusNames=alr3139;
OS Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=103690;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT "Complete genomic sequence of the filamentous nitrogen-fixing
RT cyanobacterium Anabaena sp. strain PCC 7120.";
RL DNA Res. 8:205-213(2001).
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; BA000019; BAB74838.1; -; Genomic_DNA.
DR PIR; AD2198; AD2198.
DR RefSeq; WP_010997290.1; NZ_RSCN01000001.1.
DR AlphaFoldDB; Q8YSE9; -.
DR SMR; Q8YSE9; -.
DR STRING; 103690.17132234; -.
DR EnsemblBacteria; BAB74838; BAB74838; BAB74838.
DR KEGG; ana:alr3139; -.
DR eggNOG; COG0496; Bacteria.
DR OMA; YVGEYGK; -.
DR OrthoDB; 1909278at2; -.
DR Proteomes; UP000002483; 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..226
FT /note="Putative 5'-nucleotidase alr3139"
FT /id="PRO_0000111872"
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 38
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 89
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
SQ SEQUENCE 226 AA; 24624 MW; 0ADD98D002C8B8E8 CRC64;
MTIILTNDDG IDAPGIKALA QAVSGKNFIV AAPRDHQSGC GHQVTTTRPI NLQRRSDSEY
AIAGTPADCI RIAITQISQD VKFVLSGINA GGNLGVDAYI SGTVAAVREA AMHGIAGVAI
SHYRKAKQNF DWELAAKWTA EVLEELLHRP LEPGYFWNVN LPHLQPGETQ PELVFCQPCT
KPLPANYRID GDDFYYVGEY GKRERTPGSD VDVCFTGNIA ITQLRV