ID A0A1D9E013_9MICO Unreviewed; 427 AA.
AC A0A1D9E013;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Thymidine phosphorylase {ECO:0000313|EMBL:AOY56405.1};
GN ORFNames=A4Z71_05495 {ECO:0000313|EMBL:AOY56405.1};
OS Candidatus Rhodoluna planktonica.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Luna cluster; Luna-1 subcluster; Rhodoluna.
OX NCBI_TaxID=535712 {ECO:0000313|EMBL:AOY56405.1, ECO:0000313|Proteomes:UP000243784};
RN [1] {ECO:0000313|EMBL:AOY56405.1, ECO:0000313|Proteomes:UP000243784}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MWH-Dar1 {ECO:0000313|EMBL:AOY56405.1,
RC ECO:0000313|Proteomes:UP000243784};
RX PubMed=27659506; DOI=10.1016/j.bbabio.2016.09.006;
RA Nakamura S., Kikukawa T., Tamogami J., Kamiya M., Aizawa T., Hahn M.W.,
RA Ihara K., Kamo N., Demura M.;
RT "Photochemical characterization of actinorhodopsin and its functional
RT existence in the natural host.";
RL Biochim. Biophys. Acta 1857:1900-1908(2016).
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the thymidine/pyrimidine-nucleoside
CC phosphorylase family. {ECO:0000256|ARBA:ARBA00006915}.
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DR EMBL; CP015208; AOY56405.1; -; Genomic_DNA.
DR RefSeq; WP_070954910.1; NZ_CP015208.1.
DR AlphaFoldDB; A0A1D9E013; -.
DR STRING; 535712.A4Z71_05495; -.
DR KEGG; rpla:A4Z71_05495; -.
DR OrthoDB; 9763887at2; -.
DR Proteomes; UP000243784; Chromosome.
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 Reference proteome {ECO:0000313|Proteomes:UP000243784};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 337..411
FT /note="Pyrimidine nucleoside phosphorylase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00941"
SQ SEQUENCE 427 AA; 45305 MW; 6869EC7CD85FA2D4 CRC64;
MAEFSAVDLI IKKRSKFELS TEEINWLIGN YTSGVVADEQ MSSMAMAILL NGMNRREIKD
LTMAMIASGE RLDWTGLSKP TVDKHSTGGV GDKITLPLVP LVAVFGAAVP QLGGRGLGHT
GGTLDKFEAI AGWNPSLTNQ QFFDQLQSVG GAVCGASENI APADKKLYAL RDVTGTVEAI
PLITSSIMSK KIAEGTSALV LDVKVGSGAF MKDFDKAREL AQGMVRLGID AGVKTSAMLT
DMSTPLGKKI GNALEVEESL EVLAGGGPAD VVELTVALAT EMLRLVGIEN VDVAAALKDG
RAMDKWRAMV SAQGGDPDAA LPKAKESHTI LADADGWLTE LDALGLGIAS WRLGAGRERK
EDDVLLGAGI ELHAQKGDRV SKGQPLLTLL TDEPNRFDRA LEAIEGKISI SAEQPQARKI
VLERIYE
//
