ID A0A060B7X4_9GAMM Unreviewed; 241 AA.
AC A0A060B7X4;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE RecName: Full=Purine nucleoside phosphorylase DeoD-type {ECO:0000256|HAMAP-Rule:MF_01627};
DE Short=PNP {ECO:0000256|HAMAP-Rule:MF_01627};
DE EC=2.4.2.1 {ECO:0000256|HAMAP-Rule:MF_01627};
GN Name=deoD {ECO:0000256|HAMAP-Rule:MF_01627,
GN ECO:0000313|EMBL:HCA01886.1};
GN ORFNames=DEO68_06830 {ECO:0000313|EMBL:HCA01886.1};
OS Halomonas campaniensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=213554 {ECO:0000313|EMBL:HCA01886.1, ECO:0000313|Proteomes:UP000262828};
RN [1] {ECO:0000313|EMBL:HCA01886.1, ECO:0000313|Proteomes:UP000262828}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UBA11284 {ECO:0000313|EMBL:HCA01886.1};
RX PubMed=30148503; DOI=.1038/nbt.4229;
RA Parks D.H., Chuvochina M., Waite D.W., Rinke C., Skarshewski A.,
RA Chaumeil P.A., Hugenholtz P.;
RT "A standardized bacterial taxonomy based on genome phylogeny substantially
RT revises the tree of life.";
RL Nat. Biotechnol. 36:996-1004(2018).
CC -!- FUNCTION: Catalyzes the reversible phosphorolytic breakdown of the N-
CC glycosidic bond in the beta-(deoxy)ribonucleoside molecules, with the
CC formation of the corresponding free purine bases and pentose-1-
CC phosphate. {ECO:0000256|HAMAP-Rule:MF_01627}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a purine 2'-deoxy-D-ribonucleoside + phosphate = 2-deoxy-
CC alpha-D-ribose 1-phosphate + a purine nucleobase;
CC Xref=Rhea:RHEA:36431, ChEBI:CHEBI:26386, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57259, ChEBI:CHEBI:142361; EC=2.4.2.1;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01627};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a purine D-ribonucleoside + phosphate = a purine nucleobase +
CC alpha-D-ribose 1-phosphate; Xref=Rhea:RHEA:19805, ChEBI:CHEBI:26386,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57720, ChEBI:CHEBI:142355; EC=2.4.2.1;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01627};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=phosphate + uridine = alpha-D-ribose 1-phosphate + uracil;
CC Xref=Rhea:RHEA:24388, ChEBI:CHEBI:16704, ChEBI:CHEBI:17568,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57720; EC=2.4.2.3;
CC Evidence={ECO:0000256|ARBA:ARBA00001020};
CC -!- SUBUNIT: Homohexamer; trimer of homodimers. {ECO:0000256|HAMAP-
CC Rule:MF_01627}.
CC -!- SIMILARITY: Belongs to the PNP/UDP phosphorylase family.
CC {ECO:0000256|ARBA:ARBA00010456, ECO:0000256|HAMAP-Rule:MF_01627}.
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:HCA01886.1}.
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DR EMBL; DOTR01000034; HCA01886.1; -; Genomic_DNA.
DR KEGG; hcs:FF32_10575; -.
DR HOGENOM; CLU_068457_2_0_6; -.
DR OrthoDB; 9782889at2; -.
DR Proteomes; UP000262828; Unassembled WGS sequence.
DR GO; GO:0004731; F:purine-nucleoside phosphorylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009164; P:nucleoside catabolic process; IEA:UniProt.
DR GO; GO:0042278; P:purine nucleoside metabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd09006; PNP_EcPNPI-like; 1.
DR Gene3D; 3.40.50.1580; Nucleoside phosphorylase domain; 1.
DR HAMAP; MF_01627; Pur_nucleosid_phosp; 1.
DR InterPro; IPR004402; DeoD-type.
DR InterPro; IPR018016; Nucleoside_phosphorylase_CS.
DR InterPro; IPR000845; Nucleoside_phosphorylase_d.
DR InterPro; IPR035994; Nucleoside_phosphorylase_sf.
DR NCBIfam; TIGR00107; deoD; 1.
DR PANTHER; PTHR43691:SF11; FI09636P-RELATED; 1.
DR PANTHER; PTHR43691; URIDINE PHOSPHORYLASE; 1.
DR Pfam; PF01048; PNP_UDP_1; 1.
DR SUPFAM; SSF53167; Purine and uridine phosphorylases; 1.
DR PROSITE; PS01232; PNP_UDP_1; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676, ECO:0000256|HAMAP-
KW Rule:MF_01627};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01627}.
FT DOMAIN 17..221
FT /note="Nucleoside phosphorylase"
FT /evidence="ECO:0000259|Pfam:PF01048"
FT ACT_SITE 205
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01627"
FT BINDING 5
FT /ligand="a purine D-ribonucleoside"
FT /ligand_id="ChEBI:CHEBI:142355"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01627"
FT BINDING 21
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01627"
FT BINDING 25
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01627"
FT BINDING 44
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01627"
FT BINDING 88..91
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01627"
FT BINDING 180..182
FT /ligand="a purine D-ribonucleoside"
FT /ligand_id="ChEBI:CHEBI:142355"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01627"
FT BINDING 204..205
FT /ligand="a purine D-ribonucleoside"
FT /ligand_id="ChEBI:CHEBI:142355"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01627"
FT SITE 218
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01627"
SQ SEQUENCE 241 AA; 26066 MW; DB49BB657E45D11D CRC64;
MATPHINAEM GDFADTVLMP GDPLRAKYIA DTYLENVRQV NDVRSMFGYT GTYKGREISV
MGHGMGIPSV SIYAKELITD YGVKSIIRVG SCGAVRDDVN VRDVVIGMGA CTDSKVNRMR
FNDHDFSAIA DFELTSHAVA AAKAQNVPVK VGNIFSADLF YNPQTDMAEL LKRYGIVGVE
MEAAGLYGVA AEFGARALTI CTVSDHILKG ESLSSADRQT TFNDMMTIAL DTVLRDDAAK
A
//
