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Database: UniProt
Entry: S6G839_9MOLU
LinkDB: S6G839_9MOLU
Original site: S6G839_9MOLU 
ID   S6G839_9MOLU            Unreviewed;       437 AA.
AC   S6G839;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   SubName: Full=Thymidine phosphorylase {ECO:0000313|EMBL:EOA07154.1};
GN   Name=deoA-2 {ECO:0000313|EMBL:EOA07154.1};
GN   ORFNames=MYEA_5190 {ECO:0000313|EMBL:EOA07154.1};
OS   Mycoplasma yeatsii 13926.
OC   Bacteria; Mycoplasmatota; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=1188240 {ECO:0000313|EMBL:EOA07154.1, ECO:0000313|Proteomes:UP000015348};
RN   [1] {ECO:0000313|EMBL:EOA07154.1, ECO:0000313|Proteomes:UP000015348}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=13926 {ECO:0000313|EMBL:EOA07154.1,
RC   ECO:0000313|Proteomes:UP000015348};
RX   PubMed=23766401;
RA   Dordet-Frisoni E., Baranowski E., Barre A., Blanchard A., Breton M.,
RA   Couture C., Dupuy V., Gaurivaud P., Jacob D., Lemaitre C., Manso-Silvan L.,
RA   Nikolski M., Nouvel L.X., Poumarat F., Sirand-Pugnet P., Thebault P.,
RA   Theil S., Thiaucourt F., Citti C., Tardy F.;
RT   "Draft Genome Sequences of Mycoplasma auris and Mycoplasma yeatsii, Two
RT   Species of the Ear Canal of Caprinae.";
RL   Genome Announc. 1:e00280-13(2013).
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:EOA07154.1}.
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DR   EMBL; AORK01000021; EOA07154.1; -; Genomic_DNA.
DR   RefSeq; WP_004429111.1; NZ_AORK01000021.1.
DR   AlphaFoldDB; S6G839; -.
DR   PATRIC; fig|1188240.3.peg.524; -.
DR   eggNOG; COG0213; Bacteria.
DR   OrthoDB; 9763887at2; -.
DR   Proteomes; UP000015348; 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:0006206; P:pyrimidine nucleobase metabolic process; IEA:InterPro.
DR   GO; GO:0006213; P:pyrimidine nucleoside metabolic process; IEA:InterPro.
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   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; IPR000053; Thymidine/pyrmidine_PPase.
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.
PE   3: Inferred from homology;
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
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   437 AA;  48275 MW;  B413AC5C64EA6F6F CRC64;
     MNTFTNIIEK KKHNIKLTQD EINWLIKGYV DGSITDYQMA AFCMATYFTD MNDLETSYLT
     KSYIESGSQY DLSSVKGFKA DKHSTGGVGD KTSLVYAPLV ASYGINICKL TGRGLGKTGG
     TADKLESFPG WKCELENDEF TGVINKTGLS IICQSDDVVP ADKKIYALRD VTGTIDSMPL
     ITASIMSKKL VVENDGLVLD VKVGNGAFMT NLDDAIDLSN RMIDVAKNYN RKIGVILSNM
     ECPLGKAIGN AIEVKEAWDT LNGKGPKDFV ELITTIVGVT LLQAKMFNTL DEAKADVYKK
     LQTGEAAHYF KDFVIAQGGD WSVLENYDKV FKCKNKLEIK ATKSGYVKYT RAEELGLISV
     QLGAGRAKKT DTIDHAAGIY LDKEYGDQVN VGDVIMTLYT NKEINPLWEK EVLKTFEIVE
     SQPTKEVIFK IISDDVK
//
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