ID A0A4Q1T951_9BACL Unreviewed; 434 AA.
AC A0A4Q1T951;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 18-JUN-2025, entry version 27.
DE RecName: Full=Pyrimidine-nucleoside phosphorylase {ECO:0000256|ARBA:ARBA00014680};
DE EC=2.4.2.2 {ECO:0000256|ARBA:ARBA00011889};
GN ORFNames=EIZ39_05205 {ECO:0000313|EMBL:RXT14018.1};
OS Ammoniphilus sp. CFH 90114.
OC Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Paenibacillaceae;
OC Aneurinibacillus group; Ammoniphilus.
OX NCBI_TaxID=2493665 {ECO:0000313|EMBL:RXT14018.1, ECO:0000313|Proteomes:UP000289396};
RN [1] {ECO:0000313|EMBL:RXT14018.1, ECO:0000313|Proteomes:UP000289396}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFH 90114 {ECO:0000313|EMBL:RXT14018.1,
RC ECO:0000313|Proteomes:UP000289396};
RA Ming H.;
RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
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=thymidine + phosphate = 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:ARBA00048525};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=uridine + phosphate = 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:ARBA00048453};
CC -!- COFACTOR:
CC Name=K(+); Xref=ChEBI:CHEBI:29103;
CC Evidence={ECO:0000256|ARBA:ARBA00001958};
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:RXT14018.1}.
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DR EMBL; SDLI01000002; RXT14018.1; -; Genomic_DNA.
DR RefSeq; WP_129199116.1; NZ_SDLI01000002.1.
DR AlphaFoldDB; A0A4Q1T951; -.
DR OrthoDB; 9763887at2; -.
DR Proteomes; UP000289396; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
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:0009032; F:thymidine phosphorylase activity; IEA:TreeGrafter.
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 FunFam; 1.20.970.10:FF:000002; Pyrimidine-nucleoside phosphorylase; 1.
DR FunFam; 3.40.1030.10:FF:000003; Pyrimidine-nucleoside phosphorylase; 1.
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 Gene3D; 1.20.970.10; Transferase, Pyrimidine Nucleoside Phosphorylase, Chain C; 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; NF004490; PRK05820.1; 1.
DR NCBIfam; NF004747; PRK06078.1; 1.
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:RXT14018.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Potassium {ECO:0000256|ARBA:ARBA00022958};
KW Reference proteome {ECO:0000313|Proteomes:UP000289396};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:RXT14018.1}.
FT DOMAIN 345..419
FT /note="Pyrimidine nucleoside phosphorylase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00941"
SQ SEQUENCE 434 AA; 46686 MW; 5A2289E46E9255FD CRC64;
MRMVDLIQKK RDGLELTKSE IDFIIEGYTQ GAIPDYQVSA WAMSVFFQGM NPREIADLTM
AMVKSGDEVD LSAIEGIKVD KHSTGGVGDT TTLVLGPLVA AAGVPVAKMS GRGLGHTGGT
IDKLEAIDGF HTEITKEEFI KIVNEIKVAV VGQSGNLTPA DKKLYGLRDV TATVNSIPLI
ASSIMSKKIA SGADAIVLDV KTGDGAFMKT LEGSKELART MVEIGKRVGR NTVAVISDMN
QPLGFAVGNA LEVKEAIDTL RGHGPEDLTE LCLVLGAHMV VLAKKEDDFD MAYNRLKKIL
ASGEAISKLK EFIQAQGGNP EVVDHPERLP QSKYQVEVKT ASTGYVKSIK AEEIGHIAMM
LGAGRKTKED SIDLAVGVEL KKKVGDPVQE GDVLAVLHAN TEDEMEEWVT KTTHAYAIQQ
EQVSALPLIY DVIE
//
