ID F7RNU6_9GAMM Unreviewed; 195 AA.
AC F7RNU6;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Nucleotidase YfbR, HD superfamily {ECO:0000313|EMBL:EGM69957.1};
GN ORFNames=SOHN41_02034 {ECO:0000313|EMBL:EGM69957.1};
OS Shewanella sp. HN-41.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=327275 {ECO:0000313|EMBL:EGM69957.1, ECO:0000313|Proteomes:UP000002956};
RN [1] {ECO:0000313|EMBL:EGM69957.1, ECO:0000313|Proteomes:UP000002956}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HN-41 {ECO:0000313|EMBL:EGM69957.1,
RC ECO:0000313|Proteomes:UP000002956};
RX PubMed=21868804; DOI=10.1128/JB.05578-11;
RA Kim D.H., Jiang S., Lee J.H., Cho Y.J., Chun J., Choi S.H., Park H.S.,
RA Hur H.G.;
RT "Draft Genome Sequence of Shewanella sp. Strain HN-41, Which Produces
RT Arsenic-Sulfide Nanotubes.";
RL J. Bacteriol. 193:5039-5040(2011).
CC -!- FUNCTION: Catalyzes the strictly specific dephosphorylation of 2'-
CC deoxyribonucleoside 5'-monophosphates. {ECO:0000256|HAMAP-
CC Rule:MF_01100}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-phosphate + H2O = a 2'-
CC deoxyribonucleoside + phosphate; Xref=Rhea:RHEA:36167,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:18274, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:65317; EC=3.1.3.89; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_01100};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01100};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01100}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01100}.
CC -!- SIMILARITY: Belongs to the 5DNU family. {ECO:0000256|HAMAP-
CC Rule:MF_01100}.
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:EGM69957.1}.
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DR EMBL; AFOZ01000024; EGM69957.1; -; Genomic_DNA.
DR RefSeq; WP_007648273.1; NZ_AFOZ01000024.1.
DR AlphaFoldDB; F7RNU6; -.
DR STRING; 327275.SOHN41_02034; -.
DR OrthoDB; 9812744at2; -.
DR Proteomes; UP000002956; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0002953; F:5'-deoxynucleotidase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR Gene3D; 1.10.3210.10; Hypothetical protein af1432; 1.
DR HAMAP; MF_01100; 5DNU; 1.
DR InterPro; IPR006674; HD_domain.
DR InterPro; IPR022971; YfbR.
DR InterPro; IPR039356; YfbR/HDDC2.
DR PANTHER; PTHR11845:SF13; 5'-DEOXYNUCLEOTIDASE HDDC2; 1.
DR PANTHER; PTHR11845; UNCHARACTERIZED; 1.
DR Pfam; PF12917; YfbR-like; 1.
DR SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR PROSITE; PS51831; HD; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01100};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01100};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01100};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01100}.
FT DOMAIN 28..140
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT BINDING 16..17
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01100"
FT BINDING 31
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01100"
FT BINDING 31
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01100"
FT BINDING 66
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01100"
FT BINDING 67
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01100"
FT BINDING 67
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01100"
FT BINDING 75..78
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01100"
FT BINDING 135
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01100"
FT BINDING 135
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01100"
FT SITE 16
FT /note="Appears to be important in orienting the phosphate
FT for catalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01100"
SQ SEQUENCE 195 AA; 22395 MW; 89C7333AB7D55AF5 CRC64;
MSHLFAHLAR MKLIQRWPLM YNVRPENVQE HSLQVAMVAH ALVIISNKKF GTALDPHQAT
SLAIFHDASE ILTGDLPTPV KYFNKEIEAE YKKIEAIAEQ RMLDMVPEEF KEDYRSLFIS
DYADPIYKTI VKSADTLCAY LKCLEENRAG NTEFNTARKR LEAMLAANVD PAVKYFMDCF
VPSFTLNLDE INKML
//
