ID A0A062VE73_9MICO Unreviewed; 236 AA.
AC A0A062VE73;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Uridine phosphorylase {ECO:0000256|ARBA:ARBA00021980};
DE EC=2.4.2.3 {ECO:0000256|ARBA:ARBA00011888};
GN ORFNames=DC31_05250 {ECO:0000313|EMBL:KDA04707.1};
OS Microbacterium sp. CH12i.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1479651 {ECO:0000313|EMBL:KDA04707.1, ECO:0000313|Proteomes:UP000027096};
RN [1] {ECO:0000313|EMBL:KDA04707.1, ECO:0000313|Proteomes:UP000027096}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CH12i {ECO:0000313|EMBL:KDA04707.1,
RC ECO:0000313|Proteomes:UP000027096};
RA Ferreras E.R., DeMaayer P., Guerrero L.D., Aislabie J.M., Cowan D.A.;
RT "Draft genome sequence of Microbacterium sp. strain CH12i, isolated from
RT shallow groundwater in Cape Hallet, Antarctica.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the PNP/UDP phosphorylase family.
CC {ECO:0000256|ARBA:ARBA00010456}.
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:KDA04707.1}.
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DR EMBL; JHET01000013; KDA04707.1; -; Genomic_DNA.
DR RefSeq; WP_036281692.1; NZ_JHET01000013.1.
DR AlphaFoldDB; A0A062VE73; -.
DR STRING; 1479651.DC31_05250; -.
DR OrthoDB; 9782889at2; -.
DR Proteomes; UP000027096; Unassembled WGS sequence.
DR GO; GO:0004731; F:purine-nucleoside phosphorylase activity; IEA:InterPro.
DR GO; GO:0004850; F:uridine phosphorylase activity; IEA:RHEA.
DR GO; GO:0009164; P:nucleoside catabolic process; IEA:UniProt.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000027096};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 14..224
FT /note="Nucleoside phosphorylase"
FT /evidence="ECO:0000259|Pfam:PF01048"
SQ SEQUENCE 236 AA; 25508 MW; 8156FE1ED36D0590 CRC64;
MSTDIAAEPG QIAPIVLFPG DPLRAKWIAE NFLDDASLYS ETRGMLGFTG TWEGHRVSVQ
GSGMGQPSMA IYATELFTQY DVQTIVRVGS CGALSERLAV RDIIIANGAC TDSGINRVRF
HGLDYAPVAD FSLLRAAVEA SEQMPLESAV HVGLLFSSDQ FYSTRPELTE PFVQHGALAV
EMETSGLYTL AAFHGRRALS ICTVSDHIVT GKETTAQERE QTFGDMIEIA LRAATA
//
