ID T0GQ75_9SPHN Unreviewed; 543 AA.
AC T0GQ75;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 38.
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=L485_09015 {ECO:0000313|EMBL:EQB02143.1};
OS Sphingobium baderi LL03.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=1114964 {ECO:0000313|EMBL:EQB02143.1, ECO:0000313|Proteomes:UP000015524};
RN [1] {ECO:0000313|EMBL:EQB02143.1, ECO:0000313|Proteomes:UP000015524}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LL03 {ECO:0000313|EMBL:EQB02143.1,
RC ECO:0000313|Proteomes:UP000015524};
RX PubMed=24051322;
RA Kaur J., Verma H., Tripathi C., Khurana J.P., Lal R.;
RT "Draft Genome Sequence of a Hexachlorocyclohexane-Degrading Bacterium,
RT Sphingobium baderi Strain LL03T.";
RL Genome Announc. 1:e00751-13(2013).
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:EQB02143.1}.
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DR EMBL; ATIB01000050; EQB02143.1; -; Genomic_DNA.
DR AlphaFoldDB; T0GQ75; -.
DR PATRIC; fig|1114964.3.peg.1760; -.
DR eggNOG; COG0213; Bacteria.
DR Proteomes; UP000015524; 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:UP000015524};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00703}.
FT DOMAIN 473..540
FT /note="Pyrimidine nucleoside phosphorylase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00941"
SQ SEQUENCE 543 AA; 59021 MW; 94C5712DC3E022F1 CRC64;
MERRCPRNWA TGVDGKTAAP AFGQLRIAPP LIAYSLARQR KRKAESHPML TIRRLAIDTY
PENTAFLLRE SNGYSAEQFQ ALRKIRISGE NAEILATLAL VDEPAMLKPG EIGLGEQAFR
RLGLPEGATV AIEQAMPPTS LEFVRRKIDG DTLQDDEISA IIRDIATHRY SPMEIGAFLV
ACASFMSTQE TLAVTRAMAD VGHRFDWKAR LVVDKHCIGG IPGNRTSMIV VPIVAAHGLI
MPKTSSRAIT SPSGTADTME VLANVDLCEE NMRAIVAREK AVLAWGGRVN LSPADDVLIS
VERPLRIDTF DQMVASILSK KLAAGSTHLV LDIPVGPTAK VRTQDDAVRL RKLFEHIADK
IGLVIDIVIT DGSQPVGRGI GPVLEARDVM AVLRNDADAP QDLREHALFL AGRVLDFDPA
LRGGRGYARA MELLASGEAL AAMDRLVDAQ GRQTTKFALG EHVHEVHALH GGRVSTIDCH
RIARIARLAG APMDKGAGID LLHKVGAEVR KGQTLYRIHA QSRTGLGFAR DLAREDSGYE
VTQ
//
