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Database: UniProt
Entry: A0A1I1MNP9_9GAMM
LinkDB: A0A1I1MNP9_9GAMM
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ID   A0A1I1MNP9_9GAMM        Unreviewed;       445 AA.
AC   A0A1I1MNP9;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=Thymidine phosphorylase {ECO:0000256|ARBA:ARBA00011892, ECO:0000256|HAMAP-Rule:MF_01628};
DE            EC=2.4.2.4 {ECO:0000256|ARBA:ARBA00011892, ECO:0000256|HAMAP-Rule:MF_01628};
DE   AltName: Full=TdRPase {ECO:0000256|HAMAP-Rule:MF_01628};
GN   Name=deoA {ECO:0000256|HAMAP-Rule:MF_01628};
GN   ORFNames=SAMN02745724_02664 {ECO:0000313|EMBL:SFC83170.1};
OS   Pseudoalteromonas denitrificans DSM 6059.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=1123010 {ECO:0000313|EMBL:SFC83170.1, ECO:0000313|Proteomes:UP000198862};
RN   [1] {ECO:0000313|EMBL:SFC83170.1, ECO:0000313|Proteomes:UP000198862}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6059 {ECO:0000313|EMBL:SFC83170.1,
RC   ECO:0000313|Proteomes:UP000198862};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: The enzymes which catalyze the reversible phosphorolysis of
CC       pyrimidine nucleosides are involved in the degradation of these
CC       compounds and in their utilization as carbon and energy sources, or in
CC       the rescue of pyrimidine bases for nucleotide synthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_01628}.
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_01628};
CC   -!- PATHWAY: Pyrimidine metabolism; dTMP biosynthesis via salvage pathway;
CC       dTMP from thymine: step 1/2. {ECO:0000256|HAMAP-Rule:MF_01628}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738, ECO:0000256|HAMAP-
CC       Rule:MF_01628}.
CC   -!- SIMILARITY: Belongs to the thymidine/pyrimidine-nucleoside
CC       phosphorylase family. {ECO:0000256|ARBA:ARBA00006915,
CC       ECO:0000256|HAMAP-Rule:MF_01628}.
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DR   EMBL; FOLO01000019; SFC83170.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I1MNP9; -.
DR   STRING; 1123010.SAMN02745724_02664; -.
DR   OrthoDB; 9763887at2; -.
DR   UniPathway; UPA00578; UER00638.
DR   Proteomes; UP000198862; Unassembled WGS sequence.
DR   GO; GO:0004645; F:1,4-alpha-oligoglucan phosphorylase activity; IEA:InterPro.
DR   GO; GO:0016154; F:pyrimidine-nucleoside 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:0046104; P:thymidine metabolic process; IEA:UniProtKB-UniRule.
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_01628; Thymid_phosp; 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; IPR018090; Pyrmidine_PPas_bac/euk.
DR   InterPro; IPR017872; Pyrmidine_PPase_CS.
DR   InterPro; IPR000053; Thymidine/pyrmidine_PPase.
DR   InterPro; IPR013465; Thymidine_Pase.
DR   NCBIfam; TIGR02643; T_phosphoryl; 1.
DR   NCBIfam; TIGR02644; Y_phosphoryl; 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   PIRSF; PIRSF000478; TP_PyNP; 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_01628}; Reference proteome {ECO:0000313|Proteomes:UP000198862};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01628}.
FT   DOMAIN          350..424
FT                   /note="Pyrimidine nucleoside phosphorylase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00941"
SQ   SEQUENCE   445 AA;  47404 MW;  6D3019741F9CEE69 CRC64;
     MFLIQEIIRQ KRDGQVLTDE QICFFVNGIS DNTISDGQVA AFAMATYFHG MNINERIALT
     GAMRDSGDVL DWKNLDLNGP IVDKHSTGGV GDLVSLVLGP IIAACGGYVP MISGRGLGHT
     GGTLDKLDAI KGYQTQVSNE KFRQVVKDVG VAIIGQSANL APADKRLYAT RDVTATVESL
     DLITASILSK KLACGLDALV MDVKAGNGAV MKDYQNSVAL AKSIVEVANG AGVKTSCLIT
     DMSQVLANSA GNALEVKEAI LFLTGEYRSP KLTKVIYALA DEMLIVSGLA ANQSQAEKMR
     TVSLNSGAAA EKFAKMITQL GGPTDLLEKP NKYLPQANII KPIYAKQSGF LTAMDTRAMG
     MAVVSLGGGR SHINDKLDYS VGLNQIASLG MKLDQATPIC YVHASNENAF QLIENQLQNA
     IVVGEDMAKE IPSIYQSISL QDVIH
//
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