TYPH_MARMM
ID TYPH_MARMM Reviewed; 519 AA.
AC Q0ATA0;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Putative thymidine phosphorylase {ECO:0000255|HAMAP-Rule:MF_00703};
DE EC=2.4.2.4 {ECO:0000255|HAMAP-Rule:MF_00703};
DE AltName: Full=TdRPase {ECO:0000255|HAMAP-Rule:MF_00703};
GN OrderedLocusNames=Mmar10_0191;
OS Maricaulis maris (strain MCS10).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Maricaulales; Maricaulaceae;
OC Maricaulis.
OX NCBI_TaxID=394221;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCS10;
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 Saunders E., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Viollier P.,
RA Stephens C., Richardson P.;
RT "Complete sequence of Maricaulis maris MCS10.";
RL Submitted (AUG-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:0000255|HAMAP-Rule:MF_00703};
CC -!- SIMILARITY: Belongs to the thymidine/pyrimidine-nucleoside
CC phosphorylase family. Type 2 subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_00703}.
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DR EMBL; CP000449; ABI64487.1; -; Genomic_DNA.
DR RefSeq; WP_011642134.1; NC_008347.1.
DR AlphaFoldDB; Q0ATA0; -.
DR SMR; Q0ATA0; -.
DR STRING; 394221.Mmar10_0191; -.
DR EnsemblBacteria; ABI64487; ABI64487; Mmar10_0191.
DR KEGG; mmr:Mmar10_0191; -.
DR eggNOG; COG0213; Bacteria.
DR HOGENOM; CLU_025040_6_0_5; -.
DR OMA; DVWRRMI; -.
DR OrthoDB; 1724909at2; -.
DR Proteomes; UP000001964; Chromosome.
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; PTHR10515; 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; SSF47648; SSF47648; 1.
DR SUPFAM; SSF52418; SSF52418; 1.
DR SUPFAM; SSF54680; SSF54680; 1.
DR TIGRFAMs; TIGR02645; ARCH_P_rylase; 1.
DR PROSITE; PS00647; THYMID_PHOSPHORYLASE; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase; Reference proteome; Transferase.
FT CHAIN 1..519
FT /note="Putative thymidine phosphorylase"
FT /id="PRO_0000314701"
SQ SEQUENCE 519 AA; 55091 MW; EFA638F8D029E71B CRC64;
MTKMIDISAM PAELSEKNTL TARRLGIDTH EHAVIYMRAD CHICRAEGFN NHARIKVSGP
SNKAIIATLN LVVTDLLSPG QIGLSETAWL RLQLNEGDPV RLIHPAPLLS LSAVRAKIFG
EPLDQNNLDA IVGDIAAGRF SDIHLSAFLT ASAAHEQSFE EIRDLTLSMV NVGQRLDWGR
APIVDKHCVG GLPGNRTTPI VVAICVAAGL TMPKTSSRAI TSPAGTADTM ETLAPVELDV
SAMRRVVETV GGCIVWGGAV ALSPVDDTLI RIERALDIDS DGQLVASVLS KKIAAGATHL
VIDMPVGPTA KVRTEEAAAR LEGLFARVGS NLGLNLKIMR TDGSQPVGRG IGPALEAWDV
LAVLNNEGHN VPDLTVQATL LAGELLEMGQ AAPAGRGAEL ATELLVNGRA WRAFEAICEA
QGGFREPPTA PHYQVIQSPR DGVVGRIDNR RLAKAAKLAG APASKAAGIV LHAKLGSQMV
KGQPLYSLHS QSLGELSYAH DYLASQPEII EIEEEQCPR