ID A0A243PJT9_9SPHN Unreviewed; 495 AA.
AC A0A243PJT9;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=Putative thymidine phosphorylase {ECO:0000256|HAMAP-Rule:MF_00703};
DE EC=2.4.2.4 {ECO:0000256|HAMAP-Rule:MF_00703};
DE AltName: Full=TdRPase {ECO:0000256|HAMAP-Rule:MF_00703};
GN ORFNames=CA262_16150 {ECO:0000313|EMBL:OUC56921.1};
OS Sphingobium sp. GW456-12-10-14-TSB1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=1987165 {ECO:0000313|EMBL:OUC56921.1, ECO:0000313|Proteomes:UP000194660};
RN [1] {ECO:0000313|EMBL:OUC56921.1, ECO:0000313|Proteomes:UP000194660}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GW456-12-10-14-TSB1 {ECO:0000313|EMBL:OUC56921.1};
RA Song R., Chenine A.L., Ruprecht R.M.;
RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
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=2.4.2.4;
CC Evidence={ECO:0000256|ARBA:ARBA00000749, ECO:0000256|HAMAP-
CC Rule:MF_00703};
CC -!- SIMILARITY: Belongs to the thymidine/pyrimidine-nucleoside
CC phosphorylase family. Type 2 subfamily. {ECO:0000256|HAMAP-
CC Rule:MF_00703}.
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:OUC56921.1}.
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DR EMBL; NGUN01000003; OUC56921.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A243PJT9; -.
DR OrthoDB; 341217at2; -.
DR Proteomes; UP000194660; Unassembled WGS sequence.
DR GO; GO:0004645; F:1,4-alpha-oligoglucan phosphorylase activity; IEA:InterPro.
DR GO; GO:0009032; F:thymidine phosphorylase activity; IEA:UniProtKB-UniRule.
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 HAMAP; MF_00703; Thymid_phosp_2; 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; IPR017872; Pyrmidine_PPase_CS.
DR InterPro; IPR028579; Thym_Pase_Put.
DR InterPro; IPR013466; Thymidine/AMP_Pase.
DR InterPro; IPR000053; Thymidine/pyrmidine_PPase.
DR NCBIfam; TIGR02645; ARCH_P_rylase; 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 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, ECO:0000256|HAMAP-
KW Rule:MF_00703};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00703}.
FT DOMAIN 425..492
FT /note="Pyrimidine nucleoside phosphorylase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00941"
SQ SEQUENCE 495 AA; 53556 MW; 22D2C1E0172FC003 CRC64;
MMKIRRIAID THPENTAFLS RSGNGYSPEQ FQALRKIEIG NGNVSILATL AIVDDACLLQ
PGEIGLGEQA FRRLGLAEGS EVSFRQAPVP HSLEHVRRKI DGDTLDDTEI REIINDIAAY
RYSPMEIGAF LVGCASFMTT QETLALTSAM AGVGRRMRWG SDVVVDKHCI GGIPGNRTSM
IVVPIIAAHG LTMPKTSSRA ITSPSGTADT MEVLAAVDLA EEKLISVVEQ HHAVLAWGGR
VNLSPADDIL ITVERPLRID TFDQMVASIL SKKVAAGSTH LLIDIPVGPS AKVRSQREAI
RLRKLFEHVA HKLGLVLEVI FTDGTQPVGR GVGPVLEARD VMAVLRNDED APEDLRERSL
MLAGRVLEFD PGLKGGRGYA RAMELLGSGK ALAAMERLID AQGRRKEVLE PAKFIHEVRA
TTRGTVTSID CHLIARIARL AGAPMDKGAG IDLLRKVGEP VRRDEALYRI HAESETGLGY
ARDLALTSSG YAVTP
//
