ID A0A4R6IH48_9MOLU Unreviewed; 433 AA.
AC A0A4R6IH48;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 18-JUN-2025, entry version 19.
DE SubName: Full=Pyrimidine-nucleoside phosphorylase/thymidine phosphorylase {ECO:0000313|EMBL:TDO21171.1};
GN ORFNames=EI74_0202 {ECO:0000313|EMBL:TDO21171.1};
OS Mycoplasma testudineum.
OC Bacteria; Bacillati; Mycoplasmatota; Mollicutes; Mycoplasmataceae;
OC Mycoplasma.
OX NCBI_TaxID=244584 {ECO:0000313|EMBL:TDO21171.1, ECO:0000313|Proteomes:UP000295518};
RN [1] {ECO:0000313|EMBL:TDO21171.1, ECO:0000313|Proteomes:UP000295518}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700618 {ECO:0000313|EMBL:TDO21171.1,
RC ECO:0000313|Proteomes:UP000295518};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (MAR-2019) 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|ARBA:ARBA00056338}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=thymidine + phosphate = 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:ARBA00048550};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the thymidine/pyrimidine-nucleoside
CC phosphorylase family. {ECO:0000256|ARBA:ARBA00006915}.
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:TDO21171.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; SNWN01000009; TDO21171.1; -; Genomic_DNA.
DR RefSeq; WP_094254316.1; NZ_NNCE01000001.1.
DR AlphaFoldDB; A0A4R6IH48; -.
DR OrthoDB; 9763887at2; -.
DR Proteomes; UP000295518; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR GO; GO:0004645; F:1,4-alpha-oligoglucan phosphorylase activity; IEA:InterPro.
DR GO; GO:0009032; F:thymidine phosphorylase activity; IEA:TreeGrafter.
DR GO; GO:0006206; P:pyrimidine nucleobase metabolic process; IEA:InterPro.
DR GO; GO:0006213; P:pyrimidine nucleoside metabolic process; IEA:InterPro.
DR FunFam; 3.40.1030.10:FF:000003; Pyrimidine-nucleoside phosphorylase; 1.
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 Gene3D; 1.20.970.10; Transferase, Pyrimidine Nucleoside Phosphorylase, Chain C; 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 NCBIfam; NF004490; PRK05820.1; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000295518};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 346..419
FT /note="Pyrimidine nucleoside phosphorylase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00941"
SQ SEQUENCE 433 AA; 47795 MW; 54FF682DD9619CCF CRC64;
MDFNIVSLIE KKFQNQELSK DEINFIVNGF VDKRIKDYQM SSLLMAIRFN GMNDEELTHL
TMAMMYSGSI LDLSDISGIK VDKHSTGGVG DKISLILGPI LAACGVKFAK MSGRGLGHTG
GTIDKLESIN NFSISLSDND FKNQVNKINM AIIGQDEKLV PADKLIYALR DVTGTVNSIP
LIASSIMSKK LATGSDKILL DVKVGKGAFM KTIKSARELG KRMIAIGKLL NREVRVEITN
MDRPLGRAIG NKNEVLEAIQ TLQGHYANDI KTIIYSSAAT LLIMAQKAKT QGEAITLIEK
VIRQGSALDS FKNFIEAQGG NFEEITQDKW WNPKYSLDIK ADKQGYLVIK DALAFGITAL
ELGAGRHTKE DILDNEAGIW FNKQTNDVVQ KDDVLFTLYS SKPIPNSITN LFKGAYSLED
KQVANTIIFE QLK
//