ID H0IYB0_9GAMM Unreviewed; 450 AA.
AC H0IYB0;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 62.
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=MOY_01744 {ECO:0000313|EMBL:EHK62401.1};
OS Halomonas sp. GFAJ-1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=1118153 {ECO:0000313|EMBL:EHK62401.1, ECO:0000313|Proteomes:UP000004512};
RN [1] {ECO:0000313|EMBL:EHK62401.1, ECO:0000313|Proteomes:UP000004512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GFAJ-1 {ECO:0000313|EMBL:EHK62401.1,
RC ECO:0000313|Proteomes:UP000004512};
RX PubMed=22408239; DOI=10.1128/JB.06664-11;
RA Phung le T., Silver S., Trimble W.L., Gilbert J.A.;
RT "Draft Genome of Halomonas Species Strain GFAJ-1 (ATCC BAA-2256).";
RL J. Bacteriol. 194:1835-1836(2012).
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}.
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:EHK62401.1}.
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DR EMBL; AHBC01000004; EHK62401.1; -; Genomic_DNA.
DR RefSeq; WP_009095848.1; NZ_CP016490.1.
DR AlphaFoldDB; H0IYB0; -.
DR STRING; 1118153.MOY_01744; -.
DR KEGG; hag:BB497_07685; -.
DR PATRIC; fig|1118153.6.peg.345; -.
DR eggNOG; COG0213; Bacteria.
DR OrthoDB; 9763887at2; -.
DR UniPathway; UPA00578; UER00638.
DR Proteomes; UP000004512; 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:UP000004512};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01628}.
FT DOMAIN 358..432
FT /note="Pyrimidine nucleoside phosphorylase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00941"
SQ SEQUENCE 450 AA; 47305 MW; 720B9FC81A7FCBF4 CRC64;
MPSNASHHAL LPQELIRLKR DGQPLPAEEI KAFVQGIADD RISDAQIGAF TMSVFLNGMS
REEVVALTTA TRDSGHVMQW DSLNLPGPIV DKHSTGGVGD LVSLVLGPWV AACGAFVPMI
SGRGLGHTGG TLDKLESIPG YNPYPAPERF SEVVKSTGVA IIGQTGNLAP ADKRIYGVRD
VTATVESIPL ITASILGKKL ASGLDALVMD VKVGSGAFMP TPEKSRELAK SIANVATQAG
TPTTALLTDM SQPLAPCAGN AVEIVETLAL LRGDRANSRV MQVTRELAVE MLIAGKLVAN
REDALAKLEK ALTSGAAAEV FARMVRELGG PADFMERPDS YLATAPVIQA VYPEQSGIVQ
RFDTRAVGMS VVELGGGRLR NDASVDHSVG FSDIVEIGDR VDSQRPLAIV HARTEDAATR
AAAQLRAAVT LGDADASADT LLQETFRGEA
//
