ID I1E0A7_9GAMM Unreviewed; 437 AA.
AC I1E0A7;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 24-JAN-2024, entry version 52.
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:GAB59735.1};
GN ORFNames=RNAN_2741 {ECO:0000313|EMBL:GAB59735.1};
OS Rheinheimera nanhaiensis E407-8.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Rheinheimera.
OX NCBI_TaxID=562729 {ECO:0000313|EMBL:GAB59735.1, ECO:0000313|Proteomes:UP000004374};
RN [1] {ECO:0000313|EMBL:GAB59735.1, ECO:0000313|Proteomes:UP000004374}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E407-8 {ECO:0000313|EMBL:GAB59735.1,
RC ECO:0000313|Proteomes:UP000004374};
RX PubMed=23209246; DOI=10.1128/JB.01922-12;
RA Zhang X.-Y., Zhang Y.-J., Qin Q.-L., Xie B.-B., Chen X.-L., Zhou B.-C.,
RA Zhang Y.-Z.;
RT "Genome Sequence of the Protease-Producing Bacterium Rheinheimera
RT nanhaiensis E407-8T, Isolated from Deep-Sea Sediment of the South China
RT Sea.";
RL J. Bacteriol. 194:7001-7002(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:GAB59735.1}.
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DR EMBL; BAFK01000016; GAB59735.1; -; Genomic_DNA.
DR RefSeq; WP_008222593.1; NZ_BAFK01000016.1.
DR AlphaFoldDB; I1E0A7; -.
DR STRING; 562729.RNAN_2741; -.
DR OrthoDB; 9763887at2; -.
DR UniPathway; UPA00578; UER00638.
DR Proteomes; UP000004374; 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:UP000004374};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01628}.
FT DOMAIN 348..422
FT /note="Pyrimidine nucleoside phosphorylase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00941"
SQ SEQUENCE 437 AA; 45852 MW; 4644A69ED4306327 CRC64;
MIPQEIIKTK RNGNTLSQAE IQQFVRGLTD DSFSEGQVAA LAMAIYLNGM SVDEIVALTL
AMRDSGTVLN WQGKLNGPVV DKHSTGGVGD KVTLMLAPMV AACGAFMPSI AGRGLGHTGG
TVDKLETIPG YSCTQSLDTI RKLLPQLGCV IVGQSSELAP ADRRLYAIRD VTATVESIPL
ITASILSKKL SEGLDALVMD VKIGNGAIMR SVDDASALAN SIVNVARGAG VNTRALLTDM
NQILGTSAGN VLEVLETLDY LTGKYREPRL HQVTLELGAN MLMLGGLYQD KARAIAALEH
SLSSGKAAEI FAKMVSALGG PANLLEQPQQ YLATAPVVQD IVAPHSGYLH YTDTVGLGMA
VVRLGGGRSH PSQQIDPAVG FSHITSTGQK VQQGDVLAKV HAASTEAAKV AVAEYLQALT
ITTQATAPYP LVHHIVG
//
