ID C7NFD1_KYTSD Unreviewed; 433 AA.
AC C7NFD1;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE SubName: Full=Thymidine phosphorylase {ECO:0000313|EMBL:ACV05866.1};
DE EC=2.4.2.2 {ECO:0000313|EMBL:ACV05866.1};
GN OrderedLocusNames=Ksed_08120 {ECO:0000313|EMBL:ACV05866.1};
OS Kytococcus sedentarius (strain ATCC 14392 / DSM 20547 / CCM 314 / 541)
OS (Micrococcus sedentarius).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Kytococcaceae;
OC Kytococcus.
OX NCBI_TaxID=478801 {ECO:0000313|EMBL:ACV05866.1, ECO:0000313|Proteomes:UP000006666};
RN [1] {ECO:0000313|EMBL:ACV05866.1, ECO:0000313|Proteomes:UP000006666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14392 / DSM 20547 / CCM 314 / 541
RC {ECO:0000313|Proteomes:UP000006666};
RX PubMed=21304632; DOI=10.4056/sigs.761;
RA Sims D., Brettin T., Detter J.C., Han C., Lapidus A., Copeland A.,
RA Glavina Del Rio T., Nolan M., Chen F., Lucas S., Tice H., Cheng J.F.,
RA Bruce D., Goodwin L., Pitluck S., Ovchinnikova G., Pati A., Ivanova N.,
RA Mavrommatis K., Chen A., Palaniappan K., D'haeseleer P., Chain P.,
RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Schneider S.,
RA Goker M., Pukall R., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Kytococcus sedentarius type strain (541).";
RL Stand. Genomic Sci. 1:12-20(2009).
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; CP001686; ACV05866.1; -; Genomic_DNA.
DR RefSeq; WP_012802281.1; NC_013169.1.
DR AlphaFoldDB; C7NFD1; -.
DR STRING; 478801.Ksed_08120; -.
DR KEGG; kse:Ksed_08120; -.
DR eggNOG; COG0213; Bacteria.
DR HOGENOM; CLU_025040_0_1_11; -.
DR Proteomes; UP000006666; Chromosome.
DR GO; GO:0004645; F:1,4-alpha-oligoglucan phosphorylase activity; IEA:InterPro.
DR GO; GO:0016154; F:pyrimidine-nucleoside phosphorylase activity; IEA:UniProtKB-EC.
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; IPR017872; Pyrmidine_PPase_CS.
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.
DR PROSITE; PS00647; THYMID_PHOSPHORYLASE; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000313|EMBL:ACV05866.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ACV05866.1}.
FT DOMAIN 342..416
FT /note="Pyrimidine nucleoside phosphorylase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00941"
SQ SEQUENCE 433 AA; 45007 MW; 9FFA940A25EBFC85 CRC64;
MTGTQHDAVD IIRTKRDGER LSDEQIDWVI DAYTRGDVAD EQMSALAMAI YLNGMEPDEI
SRWTSAMIAS GERMDFSTLS RPTADKHSTG GVGDKITLPL APLVAACGVA VPQLSGRGLG
HTGGTLDKLE AIPGWQADLT NEAMMQQLEE VGAVICAAGA GLAPADKKLY ALRDVTGTVE
ALPLIASSIM SKKIAEGTGA LVLDVKVGSG AFMKTEADAR ALAERMVALG DAAGVTTVAL
LTDMSAPLGR TAGNGLEVIE SVEVLSGGGP ADVRELTIAL AREMVLASGI EGADAVDVAE
VLDSGKALQV WKQMIAAQGG DPEAELALGE HTAEVTAEAG GVITEMDAYK VGVAAWRLGA
GRARKEDPVQ AGAGVRWHAG VGERVEAGQV LFTCYTETSE RLQRGVETLA GAVTIDTGAE
PFERTLVIDR ITA
//
