ID A0A1I0ZJ65_9CELL Unreviewed; 438 AA.
AC A0A1I0ZJ65;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Thymidine phosphorylase {ECO:0000313|EMBL:SFB25695.1};
GN ORFNames=SAMN05421867_111125 {ECO:0000313|EMBL:SFB25695.1};
OS Cellulomonas marina.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC Cellulomonas.
OX NCBI_TaxID=988821 {ECO:0000313|EMBL:SFB25695.1, ECO:0000313|Proteomes:UP000199012};
RN [1] {ECO:0000313|EMBL:SFB25695.1, ECO:0000313|Proteomes:UP000199012}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.6945 {ECO:0000313|EMBL:SFB25695.1,
RC ECO:0000313|Proteomes:UP000199012};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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; FOKA01000011; SFB25695.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I0ZJ65; -.
DR STRING; 988821.SAMN05421867_111125; -.
DR OrthoDB; 9763887at2; -.
DR Proteomes; UP000199012; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000199012};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 346..420
FT /note="Pyrimidine nucleoside phosphorylase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00941"
SQ SEQUENCE 438 AA; 45132 MW; 2651770BDDAA0F04 CRC64;
MSAATGGSRP EPFDAVDVIR TKRDRGVLTD AQVDWVVDAY TRGVVAEEQM SALAMAILLN
GMERAEVARW TAAMIATGER MDFSGLSRPT ADKHSTGGVG DKITLPLAPL VAVFGVAVPQ
LSGRGLGHTG GTLDKLESIP GWRAALSNDE MMAQLEEVGA VICQAGSGLA PADRKLYALR
DVTGTVEAVP LIASSIMSKK IAEGTGSLVL DVKVGSGAFM KDEARARELA EVMVALGTDA
GVTTVALLTD MSTPLGLTAG NALEVQESVE VLAGGGPADV VELTVALARE MLAAAGCGDV
DPALALADGR AMDVWRAMIR AQGGDPDAPL PTARETETVV APADGVLARL DALAVGVAAW
RLGAGRARKE DAVQAGAGVR WHARPGDVVR AGQPLLTLHT DTPERFARAH EALADAVEVA
PPGTDGPLTP LVLDRISA
//
