ID A0A371IWH2_9FIRM Unreviewed; 441 AA.
AC A0A371IWH2;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=Pyrimidine-nucleoside phosphorylase {ECO:0000256|ARBA:ARBA00014680};
DE EC=2.4.2.2 {ECO:0000256|ARBA:ARBA00011889};
GN ORFNames=CHF27_001100 {ECO:0000313|EMBL:RDY24825.1};
OS Romboutsia maritimum.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC Romboutsia.
OX NCBI_TaxID=2020948 {ECO:0000313|EMBL:RDY24825.1, ECO:0000313|Proteomes:UP000243494};
RN [1] {ECO:0000313|EMBL:RDY24825.1, ECO:0000313|Proteomes:UP000243494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCRI-22766 {ECO:0000313|EMBL:RDY24825.1,
RC ECO:0000313|Proteomes:UP000243494};
RX PubMed=29025937;
RA Maheux A.F., Boudreau D.K., Berube E., Boissinot M., Raymond F.,
RA Brodeur S., Corbeil J., Brightwell G., Broda D., Omar R.F., Bergeron M.G.;
RT "Draft Genome Sequence of Romboutsia maritimum sp. nov. Strain CCRI-
RT 22766(T), Isolated from Coastal Estuarine Mud.";
RL Genome Announc. 5:e01044-17(2017).
CC -!- FUNCTION: Catalyzes phosphorolysis of the pyrimidine nucleosides
CC uridine, thymidine and 2'-deoxyuridine with the formation of the
CC corresponding pyrimidine base and ribose-1-phosphate.
CC {ECO:0000256|ARBA:ARBA00003877}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2'-deoxyuridine + phosphate = 2-deoxy-alpha-D-ribose 1-
CC phosphate + uracil; Xref=Rhea:RHEA:22824, ChEBI:CHEBI:16450,
CC ChEBI:CHEBI:17568, ChEBI:CHEBI:43474, ChEBI:CHEBI:57259; EC=2.4.2.2;
CC Evidence={ECO:0000256|ARBA:ARBA00001066};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=phosphate + thymidine = 2-deoxy-alpha-D-ribose 1-phosphate +
CC thymine; Xref=Rhea:RHEA:16037, ChEBI:CHEBI:17748, ChEBI:CHEBI:17821,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57259; EC=2.4.2.2;
CC Evidence={ECO:0000256|ARBA:ARBA00000722};
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=2.4.2.2;
CC Evidence={ECO:0000256|ARBA:ARBA00001004};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the thymidine/pyrimidine-nucleoside
CC phosphorylase family. {ECO:0000256|ARBA:ARBA00006915}.
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:RDY24825.1}.
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DR EMBL; NOJZ02000001; RDY24825.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A371IWH2; -.
DR OrthoDB; 9763887at2; -.
DR Proteomes; UP000243494; Unassembled WGS sequence.
DR GO; GO:0004645; F:1,4-alpha-oligoglucan phosphorylase activity; IEA:InterPro.
DR GO; GO:0047847; F:deoxyuridine phosphorylase activity; IEA:RHEA.
DR GO; GO:0016154; F:pyrimidine-nucleoside phosphorylase activity; IEA:UniProtKB-EC.
DR GO; GO:0009032; F:thymidine phosphorylase activity; IEA:RHEA.
DR GO; GO:0004850; F:uridine phosphorylase activity; IEA:RHEA.
DR GO; GO:0006206; P:pyrimidine nucleobase metabolic process; IEA:InterPro.
DR GO; GO:0006213; P:pyrimidine nucleoside metabolic process; IEA:InterPro.
DR Gene3D; 3.40.1030.10; Nucleoside phosphorylase/phosphoribosyltransferase catalytic domain; 1.
DR Gene3D; 3.90.1170.30; Pyrimidine nucleoside phosphorylase-like, C-terminal domain; 1.
DR InterPro; IPR000312; Glycosyl_Trfase_fam3.
DR InterPro; IPR017459; Glycosyl_Trfase_fam3_N_dom.
DR InterPro; IPR036320; Glycosyl_Trfase_fam3_N_dom_sf.
DR InterPro; IPR035902; Nuc_phospho_transferase.
DR InterPro; IPR036566; PYNP-like_C_sf.
DR InterPro; IPR013102; PYNP_C.
DR InterPro; IPR018090; Pyrmidine_PPas_bac/euk.
DR InterPro; IPR017872; Pyrmidine_PPase_CS.
DR InterPro; IPR000053; Thymidine/pyrmidine_PPase.
DR NCBIfam; TIGR02644; Y_phosphoryl; 1.
DR PANTHER; PTHR10515; THYMIDINE PHOSPHORYLASE; 1.
DR PANTHER; PTHR10515:SF0; THYMIDINE PHOSPHORYLASE; 1.
DR Pfam; PF02885; Glycos_trans_3N; 1.
DR Pfam; PF00591; Glycos_transf_3; 1.
DR Pfam; PF07831; PYNP_C; 1.
DR PIRSF; PIRSF000478; TP_PyNP; 1.
DR SMART; SM00941; PYNP_C; 1.
DR SUPFAM; SSF52418; Nucleoside phosphorylase/phosphoribosyltransferase catalytic domain; 1.
DR SUPFAM; SSF47648; Nucleoside phosphorylase/phosphoribosyltransferase N-terminal domain; 1.
DR SUPFAM; SSF54680; Pyrimidine nucleoside phosphorylase C-terminal domain; 1.
DR PROSITE; PS00647; THYMID_PHOSPHORYLASE; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000313|EMBL:RDY24825.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000243494};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:RDY24825.1}.
FT DOMAIN 345..419
FT /note="Pyrimidine nucleoside phosphorylase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00941"
SQ SEQUENCE 441 AA; 48089 MW; 20BD719337A9D87F CRC64;
MRIYDIIKKK RDNNELTKEE INFFVEQYSK GEIPDYQASA LLMAIYLNKM NKQETVYLTE
AMMNSGEVID LSEIKGIKVD KHSTGGVGDK TTIALAPLVA ACKAPVAKMS GRGLGHTGGT
LDKLEAIPGF SIEMESDKFV DSVNKHKIAV CGQTASIAVA DKKMYALRDV TATVDNISLI
AASIMCKKLA SGANAILLDV KTGDGAFMKT LDDSFELAKA MVDIGSGMNR ETIGMITDMD
EPLGFAVGNS LEVIEAIETL KGNGPKDFVH LCETLGAYML VLAKVAKDYE EGILKIRHAI
SSGEALDKLK VFIENQGGDK RVIDDYSLLP KASKIVPIKS SKAGYISKIE AEEVGISAMI
LGAGRETKED ILDLSAGIVL EKKVGDYVRE GDILAYMHFN KEEKFESAKE RFIRAYSIVE
AKVAPRKLIY GVVTKNEIKK F
//
