ID A0A0N0TJI1_9ACTN Unreviewed; 427 AA.
AC A0A0N0TJI1;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Pyrimidine-nucleoside phosphorylase {ECO:0000313|EMBL:KOX06973.1};
GN ORFNames=ADL04_05120 {ECO:0000313|EMBL:KOX06973.1};
OS Streptomyces sp. NRRL B-3648.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1519493 {ECO:0000313|EMBL:KOX06973.1, ECO:0000313|Proteomes:UP000037702};
RN [1] {ECO:0000313|EMBL:KOX06973.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL B-3648 {ECO:0000313|EMBL:KOX06973.1};
RA Noorani M.;
RL Submitted (JUL-2015) 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}.
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:KOX06973.1}.
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DR EMBL; LGDZ01000052; KOX06973.1; -; Genomic_DNA.
DR RefSeq; WP_053707784.1; NZ_LGDZ01000052.1.
DR AlphaFoldDB; A0A0N0TJI1; -.
DR PATRIC; fig|1519493.3.peg.1132; -.
DR OrthoDB; 9763887at2; -.
DR Proteomes; UP000037702; 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:UP000037702};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 336..410
FT /note="Pyrimidine nucleoside phosphorylase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00941"
SQ SEQUENCE 427 AA; 44359 MW; 1CBFFFC52081B98A CRC64;
MAMDAISVIR TKRDRGELTD EQIDWVIDAY TRGEVADEQM SALAMAILLN GMNRREIARW
TAAMIASGER MDFSSLSRPT ADKHSTGGVG DKITLPLAPL VAACGAAVPQ LSGRGLGHTG
GTLDKLESVP GWRALLSNEE MLHVLDTTGA VICAAGDGLA PADKKLYALR DVTGTVEAIP
LIASSIMSKK IAEGTGSLVL DVKVGTGAFM KTIEDARELA STMVGLGTDH GVRTVALLTD
MSTPLGLTAG NALEVRESVE VLAGGGPADV VELTIALARE MLDAAGVKDA DPAKALADGS
AMDVWRRMIA AQGGDPDAPL PTAKEQHVVK APASGVLTRL DAYGIGVGAW RLGAGRARKE
DPVQAGAGIE LHAKPGDTVT EGQPLLTLHT DTPERFDYAL QAVAGSYDIA APGTDFTASP
VVLERIA
//