ID A0A0Q9LST5_9MICO Unreviewed; 429 AA.
AC A0A0Q9LST5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Pyrimidine-nucleoside phosphorylase {ECO:0000313|EMBL:KRE57069.1};
GN ORFNames=ASG70_01125 {ECO:0000313|EMBL:KRE57069.1};
OS Phycicoccus sp. Soil748.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Phycicoccus.
OX NCBI_TaxID=1736397 {ECO:0000313|EMBL:KRE57069.1, ECO:0000313|Proteomes:UP000051855};
RN [1] {ECO:0000313|Proteomes:UP000051855}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil748 {ECO:0000313|Proteomes:UP000051855};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRE57069.1, ECO:0000313|Proteomes:UP000051855}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil748 {ECO:0000313|EMBL:KRE57069.1,
RC ECO:0000313|Proteomes:UP000051855};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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:KRE57069.1}.
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DR EMBL; LMSC01000005; KRE57069.1; -; Genomic_DNA.
DR RefSeq; WP_056882486.1; NZ_LMSC01000005.1.
DR AlphaFoldDB; A0A0Q9LST5; -.
DR STRING; 1736397.ASG70_01125; -.
DR OrthoDB; 9763887at2; -.
DR Proteomes; UP000051855; 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 Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 338..412
FT /note="Pyrimidine nucleoside phosphorylase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00941"
SQ SEQUENCE 429 AA; 44953 MW; 8FF3739611DC0B2F CRC64;
MSERFDAVDV IITKRGRGEL SDAQIDWVID AYTRGAVADE QMSSLAMAIL LNGMNRREIS
RWTAAMIASG ERMDFSSLSR PTADKHSTGG VGDKITLPLA PLVAACGVAV PQLSGRGLGH
TGGTLDKLES VPGWRAALSN DEMMRQLEDV GAVICAAGDG LAPADKKLYA LRDVTGTVEA
IPLIASSIMS KKIAEGTGAL VLDVKVGSGA FMKTVEDARE LARTMVDLGT DAGVNTVALL
TNMQVPLGLT AGNALEVRES VEVLAGGGPE DVVELTLALA REMLAAAGRD DIDPADALKD
GRAMDAWKSM IRAQGGDPDA ELPVAKETHE VLVPADGVLT ELDALKVGVA AWRLGAGRAR
KEDPVQAGAG VEMHAKPGAT VRAGEKLLTL HTDTPERFER ALESLDGAFT IAPEGSRPDL
LPLVIEKIS
//
