ID A0A3B8WBH7_MARNT Unreviewed; 504 AA. AC A0A3B8WBH7; DT 16-JAN-2019, integrated into UniProtKB/TrEMBL. DT 16-JAN-2019, sequence version 1. DT 14-DEC-2022, entry version 12. 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=DCF82_05310 {ECO:0000313|EMBL:HAC27217.1}; OS Marinobacter nauticus (Marinobacter hydrocarbonoclasticus) (Marinobacter OS aquaeolei). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Marinobacteraceae; Marinobacter. OX NCBI_TaxID=2743 {ECO:0000313|EMBL:HAC27217.1, ECO:0000313|Proteomes:UP000261325}; RN [1] {ECO:0000313|EMBL:HAC27217.1, ECO:0000313|Proteomes:UP000261325} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UBA9049 {ECO:0000313|EMBL:HAC27217.1}; RX PubMed=30148503; DOI=.1038/nbt.4229; RA Parks D.H., Chuvochina M., Waite D.W., Rinke C., Skarshewski A., RA Chaumeil P.A., Hugenholtz P.; RT "A standardized bacterial taxonomy based on genome phylogeny substantially RT revises the tree of life."; RL Nat. Biotechnol. 36:996-1004(2018). 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:HAC27217.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; DLYI01000063; HAC27217.1; -; Genomic_DNA. DR AlphaFoldDB; A0A3B8WBH7; -. DR Proteomes; UP000261325; 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; -; 1. DR Gene3D; 3.90.1170.30; -; 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 PANTHER; PTHR10515; 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 TIGRFAMs; TIGR02645; ARCH_P_rylase; 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 431..498 FT /note="PYNP_C" FT /evidence="ECO:0000259|SMART:SM00941" SQ SEQUENCE 504 AA; 53104 MW; EC7FBA258E000684 CRC64; MVASSSQLRV FKMGINTHQE PVVYMRDDCD VCLSEGFAAS SRVGISSQGR SIIATLNISS DETVPKGYAG LSDIAIERLG VAQSDLVSVH HAPYIESLSL VRRKVFGHSL LPAEMARIVS DISAHKYSDV EIACFLSACA GGRLGFDEIV ALTQAMVNCG QQLDWPGVDR VFDKHCVGGL PGNRTTPLVV SIVSAAGLVM PKTSSRAITS PAGTADTMEA LTNVRLGLNE IRRVVRETGA CLAWGGAMNL SPADDLLIRI ERALDLDGEG QLVASVLSKK IAAGSTHAVI DIPVGETAKV RTPGDADRLA SLFTSVGAAC GLKVRCIATD GSKPVGAGIG PTEEARDVLA VLQGKQGAPR DLRGRAILLA GHLFDLADGL GVKEGMIKAE RLLQNGSAWE QFKRITKAQG GLKSLGEARF RRPVLSSESG TIVSIDNRRL ARVAKLAGAP ASSTAGLRLL VNVGDIVIKG EPLYELLSDS PGQQDYALAF NDMGPAIFTV SQEE //