ID A4XET0_NOVAD Unreviewed; 495 AA.
AC A4XET0;
DT 29-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 88.
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 OrderedLocusNames=Saro_3581 {ECO:0000313|EMBL:ABP64441.1};
OS Novosphingobium aromaticivorans (strain ATCC 700278 / DSM 12444 / CCUG
OS 56034 / CIP 105152 / NBRC 16084 / F199).
OG Plasmid pNL2 {ECO:0000313|EMBL:ABP64441.1,
OG ECO:0000313|Proteomes:UP000009134}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=279238 {ECO:0000313|EMBL:ABP64441.1, ECO:0000313|Proteomes:UP000009134};
RN [1] {ECO:0000313|EMBL:ABP64441.1, ECO:0000313|Proteomes:UP000009134}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700278 / DSM 12444 / CCUG 56034 / CIP 105152 / NBRC 16084
RC / F199 {ECO:0000313|Proteomes:UP000009134};
RC PLASMID=pNL2 {ECO:0000313|EMBL:ABP64441.1,
RC ECO:0000313|Proteomes:UP000009134};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chertkov O., Han C., Thomson S., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Ivanova N., Fredrickson J., Romine M.F., Richardson P.;
RT "Complete sequence of plasmid pNL2 of Novosphingobium aromaticivorans DSM
RT 12444.";
RL Submitted (APR-2007) 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}.
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DR EMBL; CP000677; ABP64441.1; -; Genomic_DNA.
DR RefSeq; WP_011906828.1; NC_009427.1.
DR AlphaFoldDB; A4XET0; -.
DR KEGG; nar:Saro_3581; -.
DR eggNOG; COG0213; Bacteria.
DR HOGENOM; CLU_025040_6_0_5; -.
DR Proteomes; UP000009134; Plasmid pNL2.
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}; Plasmid {ECO:0000313|EMBL:ABP64441.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000009134};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00703}.
FT DOMAIN 426..493
FT /note="Pyrimidine nucleoside phosphorylase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00941"
SQ SEQUENCE 495 AA; 53373 MW; 2D27C851D58F9A08 CRC64;
MALKIKRIAI DTHPENTAFL LRRRNGYSPE QFVALRKIEI TGGDASILAT LALIDDESLL
EPHMIGLGEQ AFRRLGLPEG AEVTFRQAPV PHSLEHVRRK IDGDELEETE IAEIIRDIAG
YRYSPMEIGA FLVACAGFMS THETLALTRA MAGVGRQMHW PSEIVVDKHC IGGIPGNRTS
MIIVPIIAAH GLTMPKTSSR AITSPSGTAD TMEVLASVDL PEDRLVSIVA KEHAVLAWGG
RVNLSPADDV LITVERPLRI DTFDQMVASI LSKKLAAGST HLLIDIPVGP TAKVRTTREA
IRLRKLFEYV GHRLGLVLDI VVTDGSQPVG RGVGPVLEAR DVMAVLRNED DAPRDLRERA
VMLAGRVLEF DPALAGGKGY ARAMELLGSG AALAAMERLI DAQGRCREVI LPGSHVHDIC
APAGGTVMSI DCHLIARIAR LAGAPMDKGA GIDLLHKVGD RVRADEVLYR IHAHSPTGLE
YARELAVASS GYVVG
//
