ID U4K211_9VIBR Unreviewed; 442 AA.
AC U4K211;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 24-JAN-2024, entry version 53.
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 ECO:0000313|EMBL:CCO56684.1};
GN ORFNames=VIBNI_A0494 {ECO:0000313|EMBL:CCO56684.1};
OS Vibrio nigripulchritudo.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=28173 {ECO:0000313|EMBL:CCO56684.1, ECO:0000313|Proteomes:UP000016895};
RN [1] {ECO:0000313|EMBL:CCO56684.1, ECO:0000313|Proteomes:UP000016895}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SnF1 {ECO:0000313|Proteomes:UP000016895};
RX PubMed=23739050; DOI=10.1038/ismej.2013.90;
RA Goudenege D., Labreuche Y., Krin E., Ansquer D., Mangenot S., Calteau A.,
RA Medigue C., Mazel D., Polz M.F., Le Roux F.;
RT "Comparative genomics of pathogenic lineages of Vibrio nigripulchritudo
RT identifies virulence-associated traits.";
RL ISME J. 7:1985-1996(2013).
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; FO203526; CCO56684.1; -; Genomic_DNA.
DR RefSeq; WP_022549801.1; NC_022528.1.
DR AlphaFoldDB; U4K211; -.
DR STRING; 28173.VIBNI_A0494; -.
DR KEGG; vni:VIBNI_A0494; -.
DR PATRIC; fig|1260221.3.peg.468; -.
DR eggNOG; COG0213; Bacteria.
DR OrthoDB; 9763887at2; -.
DR UniPathway; UPA00578; UER00638.
DR Proteomes; UP000016895; Chromosome 1.
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:UP000016895};
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 442 AA; 47017 MW; 0E7F88DDA5DD4737 CRC64;
MYLPQEIIRK KRDGEVLSAE EIQFFIQGVA KGEVSEGQIA AFAMAIFFNE MSMPERIALT
CAMRDSGMVI NWDHMNFGGP IVDKHSTGGV GDVTSLMLGP MVAACGGFVP MISGRGLGHT
GGTLDKLESI PGYNITPNNE VFGDVTKEAG VAIIGQTGDL APADKRVYAT RDITATVDNI
SLITASILSK KLAAGLDSLV MDVKVGSGAF MPTYEASEEL AKSIVAVANG AGTKTTAILT
DMNQVLASSA GNAVEVREAV QFLTGEYRNP RLLEITLALC SEMLVLGKLA DNTEDARKKL
MAVLDNGKAA ECFGKMVAGL GGPVDFVENY DNYLEKAEII KPVYAKESGV VSSMDTRAIG
MAVVAMGGGR RVATDSIDYA VGFDQFIRLG EVANSETPLA MIHARSEEQW SEAAEALQSA
IVVGGEYQKT PDVYRQIRAE DV
//
