ID A0A0F0KVD4_9MICO Unreviewed; 430 AA.
AC A0A0F0KVD4;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE SubName: Full=Pyrimidine-nucleoside phosphorylase {ECO:0000313|EMBL:KJL23186.1};
DE EC=2.4.2.2 {ECO:0000313|EMBL:KJL23186.1};
GN Name=pdp {ECO:0000313|EMBL:KJL23186.1};
GN ORFNames=RN50_01124 {ECO:0000313|EMBL:KJL23186.1};
OS Microbacterium foliorum.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=104336 {ECO:0000313|EMBL:KJL23186.1, ECO:0000313|Proteomes:UP000033572};
RN [1] {ECO:0000313|EMBL:KJL23186.1, ECO:0000313|Proteomes:UP000033572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12966 {ECO:0000313|EMBL:KJL23186.1,
RC ECO:0000313|Proteomes:UP000033572};
RA Corretto E.;
RT "Draft genome sequences of ten Microbacterium spp. with emphasis on heavy
RT metal contaminated environments.";
RL Submitted (FEB-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:KJL23186.1}.
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DR EMBL; JYIU01000036; KJL23186.1; -; Genomic_DNA.
DR RefSeq; WP_045253521.1; NZ_JYIU01000036.1.
DR AlphaFoldDB; A0A0F0KVD4; -.
DR KEGG; mfol:DXT68_11455; -.
DR PATRIC; fig|104336.4.peg.1153; -.
DR Proteomes; UP000033572; 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: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:KJL23186.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000033572};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KJL23186.1}.
FT DOMAIN 340..414
FT /note="Pyrimidine nucleoside phosphorylase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00941"
SQ SEQUENCE 430 AA; 44904 MW; 76C9015B1F3BD322 CRC64;
MSVEPFDAVD VIRAKRDGGA VPEKALRWMV DAYTRGYVSD AQMASFAMAI FQRGMERDEI
RVLTDAMIAS GERMSFATLG KKTVDKHSTG GVGDKITLPL APLVAVFGVA VPQLSGRGLG
HTGGTLDKLE SIPGWRAALS NEEMFAQMQG DVGAVICAAG SGLAPADKKL YALRDVTGTV
EAIPLIASSI MSKKIAEGTD ALVLDVKFGS GAFMQDIDRA RELARTMVAL GTDSGVATTA
LLTDMNVPLG FAIGNANEVR ESVEILAGGG PADVRELTIA LAREMLALAG QPDADVEAAL
DDGRAMDGWK AMIRAQDGDP DAALPTARET HVVTAPADGV VSQMDALPFG VAAWRLGAGR
ARAEDPVVFE AGIDLHAKPG DRVVAGQPLF TLSAADEARF PRALEALEGA WAVGDEAPTA
GPIVRERITA
//
