ID Q0F1X0_9PROT Unreviewed; 515 AA.
AC Q0F1X0;
DT 17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 17-OCT-2006, sequence version 1.
DT 24-JAN-2024, entry version 70.
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=SPV1_02492 {ECO:0000313|EMBL:EAU55780.1};
OS Mariprofundus ferrooxydans PV-1.
OC Bacteria; Pseudomonadota; Zetaproteobacteria; Mariprofundales;
OC Mariprofundaceae; Mariprofundus.
OX NCBI_TaxID=314345 {ECO:0000313|EMBL:EAU55780.1, ECO:0000313|Proteomes:UP000005297};
RN [1] {ECO:0000313|EMBL:EAU55780.1, ECO:0000313|Proteomes:UP000005297}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PV-1 {ECO:0000313|EMBL:EAU55780.1,
RC ECO:0000313|Proteomes:UP000005297};
RA Emerson D., Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K.,
RA Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL Submitted (SEP-2006) 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:EAU55780.1}.
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DR EMBL; AATS01000002; EAU55780.1; -; Genomic_DNA.
DR RefSeq; WP_009850799.1; NZ_DS022295.1.
DR AlphaFoldDB; Q0F1X0; -.
DR STRING; 314344.AL013_05485; -.
DR eggNOG; COG0213; Bacteria.
DR HOGENOM; CLU_025040_6_0_0; -.
DR InParanoid; Q0F1X0; -.
DR OrthoDB; 341217at2; -.
DR Proteomes; UP000005297; 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; 1.20.970.50; -; 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 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}; Reference proteome {ECO:0000313|Proteomes:UP000005297};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00703}.
FT DOMAIN 434..501
FT /note="Pyrimidine nucleoside phosphorylase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00941"
SQ SEQUENCE 515 AA; 55664 MW; 53DA0F72CCB2A9A7 CRC64;
MNIPDFHLRL RRVGIDTYKE NVAYLHRDCP IYRAEGFQAL AKVQINSTAM DQQVLAVLNV
ASDERIMATD ELGLSEQAFE QLGLAEGETV CISHAIPPES LNAVHRKIAG EHLDGADFTG
IMQDVVDNRY SRMEMSAFLV ACSENGMERD EILALTQAMV DTGERLDWGE PLVADKHCIG
GIPGNRTTML VVPIVAAHGM LIPKTSSRAI TSPSGTADTM ETLAHVQLNL ARLRKIVRHE
RGCLAWGGTA RLAPADDMLI SVERPLALDS PGQMVASILS KKIAAGCTHL LIDIPVGPSA
KVHGMNDALR LRKMFEYVGD RSGLNLEVVI TNGEQPIGRG IGPVLEARDV ILVLENDPEA
PSDLREKALR LAGRILEFDP DVRGGQGYAI ARDILETGRA MKKMQAIIAA QGMNKTAMKP
GVLVKEILAS ESGYVTGIDN LQMARIARLA GAPMDKGAGV DLLKKLGDPV SEGEALYRIH
AEFPSDFEFA QDLAAKGDGY TIGAVPPAPR YFPAL
//
