ID A0A165RTX8_9MICO Unreviewed; 435 AA.
AC A0A165RTX8;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Thymidine phosphorylase {ECO:0000313|EMBL:KZE89073.1};
GN Name=deoA {ECO:0000313|EMBL:KZE89073.1};
GN ORFNames=AVP41_01864 {ECO:0000313|EMBL:KZE89073.1};
OS Microbacterium sp. TNHR37B.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1775956 {ECO:0000313|EMBL:KZE89073.1, ECO:0000313|Proteomes:UP000076535};
RN [1] {ECO:0000313|EMBL:KZE89073.1, ECO:0000313|Proteomes:UP000076535}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TNHR37B {ECO:0000313|EMBL:KZE89073.1,
RC ECO:0000313|Proteomes:UP000076535};
RA Adelskov J., Patel B.K.;
RT "Draft Genome Sequence of Microbacterium sp. TNHR37B isolated from the
RT Great Artesian Basin of Australia.";
RL Submitted (JAN-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}.
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:KZE89073.1}.
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DR EMBL; LQGV01000003; KZE89073.1; -; Genomic_DNA.
DR RefSeq; WP_067163591.1; NZ_LQGV01000003.1.
DR AlphaFoldDB; A0A165RTX8; -.
DR STRING; 1775956.AVP41_01864; -.
DR PATRIC; fig|1775956.3.peg.1857; -.
DR OrthoDB; 9763887at2; -.
DR Proteomes; UP000076535; 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:UP000076535};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 345..419
FT /note="Pyrimidine nucleoside phosphorylase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00941"
SQ SEQUENCE 435 AA; 45589 MW; 249907B0E6E4E473 CRC64;
MSSPTTPDVE PFDAVDVIRT KRDGGAVAED ALRWMVDAYT REYVADSQMA AFAMAVLLNG
MTRDEIRVMT DAMIASGERM SFAGLGKTTV DKHSTGGVGD KITLPLAPLV AAFGVAVPQL
SGRGLGHTGG TLDKLESIPG WRAALSNDEM FAQLRDVGAV ICAAGSGLAP ADKRLYALRD
VTGTVEAIPL IASSIMSKKI AEGTDSLVLD VKFGSGAFMR DVDRARELAR TMVALGTDSG
VATTALLTDM NTPLGLAIGN ANEVRESVEV LAGGGPADVV ELTVALAREM LALAGQPDAD
VEAALTDGRA MDAWRRMIRA QDGDPDAPLP APRETHTVVA DREGVVTALE ALPFGVAAWR
LGAGRARAQD PVIHAAGIDL HVKPGDRVAP GQPVFTLLAD DEHRFARALD ALDGAWTIGD
EAPARSPLVR ERITA
//