ID A0A1S2LTU8_9BACI Unreviewed; 433 AA.
AC A0A1S2LTU8;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Pyrimidine-nucleoside phosphorylase {ECO:0000256|ARBA:ARBA00014680};
DE EC=2.4.2.2 {ECO:0000256|ARBA:ARBA00011889};
GN Name=deoA {ECO:0000313|EMBL:OIJ15938.1};
GN ORFNames=BKP35_02840 {ECO:0000313|EMBL:OIJ15938.1};
OS Anaerobacillus arseniciselenatis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Anaerobacillus.
OX NCBI_TaxID=85682 {ECO:0000313|EMBL:OIJ15938.1, ECO:0000313|Proteomes:UP000180098};
RN [1] {ECO:0000313|EMBL:OIJ15938.1, ECO:0000313|Proteomes:UP000180098}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15340 {ECO:0000313|EMBL:OIJ15938.1,
RC ECO:0000313|Proteomes:UP000180098};
RA Bassil N.M., Lloyd J.R.;
RT "Draft genome sequences of four alkaliphilic bacteria belonging to the
RT Anaerobacillus genus.";
RL Submitted (OCT-2016) 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=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 -!- 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:OIJ15938.1}.
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DR EMBL; MLQQ01000001; OIJ15938.1; -; Genomic_DNA.
DR RefSeq; WP_071311863.1; NZ_MLQQ01000001.1.
DR AlphaFoldDB; A0A1S2LTU8; -.
DR OrthoDB; 9763887at2; -.
DR Proteomes; UP000180098; Unassembled WGS sequence.
DR GO; GO:0004645; F:1,4-alpha-oligoglucan phosphorylase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016154; F:pyrimidine-nucleoside phosphorylase activity; IEA:UniProtKB-EC.
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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Potassium {ECO:0000256|ARBA:ARBA00022958};
KW Reference proteome {ECO:0000313|Proteomes:UP000180098};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 345..418
FT /note="Pyrimidine nucleoside phosphorylase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00941"
SQ SEQUENCE 433 AA; 46160 MW; C499B1ACCA4E34ED CRC64;
MRMVDLIEKK RDGVELSKDE INFIIEGYTK EEIPEYQMSA FAMAVFFQNM SDDERAALTM
AMVESGDKID LTAIEGVKVD KHSTGGVGDT TTLVLAPLVA SVGIPVAKMS GRGLGHTGGT
IDKLEAVTGF SVEITSEQFV DLVNKNKVAV VGQSGNLTPA DKKLYGLRDV TATVNSIPLI
ASSIMSKKIA SGADAIVLDV KTGAGAFMKE LRQAEELAKA MVDIGNNLGR NTIAVISDMS
QPLGFAIGNA LEVKEAINTL KGEGPSDLME LCLNLGSQMV VLGGGAKTLT EAREQLEEAI
SSGKALETFK TFLSAQGGDV SVVDDVSKLP TAKYKIDVQA KQSGYVSEII ADKVGVAAMI
LGAGRATKES VIDLAVGIEL RKKIGDYVNQ GEPLLTLHSN QENVDECLKR VYESYKISDE
EVSAPTLIYK EIR
//
