ID A0A143Q9H7_9NOCA Unreviewed; 425 AA.
AC A0A143Q9H7;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=Thymidine phosphorylase {ECO:0000313|EMBL:AMY19484.1};
DE EC=2.4.2.4 {ECO:0000313|EMBL:AMY19484.1};
GN Name=deoA {ECO:0000313|EMBL:AMY19484.1};
GN ORFNames=A3Q40_02108 {ECO:0000313|EMBL:AMY19484.1};
OS Rhodococcus sp. PBTS 1.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=1653478 {ECO:0000313|EMBL:AMY19484.1, ECO:0000313|Proteomes:UP000076180};
RN [1] {ECO:0000313|EMBL:AMY19484.1, ECO:0000313|Proteomes:UP000076180}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PBTS 1 {ECO:0000313|EMBL:AMY19484.1,
RC ECO:0000313|Proteomes:UP000076180};
RX PubMed=27284129;
RA Stamler R.A., Vereecke D., Zhang Y., Schilkey F., Devitt N., Randall J.J.;
RT "Complete Genome and Plasmid Sequences for Rhodococcus fascians D188 and
RT Draft Sequences for Rhodococcus Isolates PBTS 1 and PBTS 2.";
RL Genome Announc. 4:0-0(2016).
RN [2] {ECO:0000313|Proteomes:UP000076180}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PBTS 1 {ECO:0000313|Proteomes:UP000076180};
RA Stamer R., Vereecke D., Zhang Y., Schilkey F., Devitt N., Randall J.;
RT "Complete Genome and Plasmid Sequences for Rhodococcus fascians D188 and
RT Draft Sequences for Rhodococcus spp. Isolates PBTS 1 and PBTS 2.";
RL Submitted (APR-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; CP015219; AMY19484.1; -; Genomic_DNA.
DR RefSeq; WP_068102046.1; NZ_CP015219.1.
DR AlphaFoldDB; A0A143Q9H7; -.
DR STRING; 1653478.A3Q40_02108; -.
DR KEGG; rhu:A3Q40_02108; -.
DR PATRIC; fig|1653478.3.peg.2121; -.
DR Proteomes; UP000076180; Chromosome.
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:0009032; F:thymidine 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:AMY19484.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000076180};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AMY19484.1}.
FT DOMAIN 336..410
FT /note="Pyrimidine nucleoside phosphorylase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00941"
SQ SEQUENCE 425 AA; 44189 MW; 1844CF8DA466EA7A CRC64;
MADAVSVIAA KRDGNTLDSD QIAWMVDAYT RGEVADEQMS ALTMAILLRG MNRREIADWT
AAMIASGRRM DFSTLARPTV DKHSTGGIGD KITLPLAPLV AACGAAVPQL SGRGLGYTGG
TLDKLESIPG WRADLTADEM TRILDDPAVG AVVCAAGADL APADKKLYAL RDVTATVESI
PMIAASIMSK KIAEGTGALV LDVKCGSGAF MSTLGDAQEL ARTMVDLGTD AGVRTVALVT
DMNTPLGRTA GNALEVEESV EVLAGGGPAD VVELTLALAR EMVAAAGLDV DPADKLADGT
AMDRWRAMIA AQGGDPDAAL PVARHTHEVT AERSGVLTRL DARAVGIAAW RLGAGRERQG
QPVQAGAGVR WHAALGDTVT AGQPLLTLCT DTPERFDRAL DALTGGWTVE DGSAQERRLI
LDRIG
//
