ID B0RBN2_CLAMS Unreviewed; 432 AA.
AC B0RBN2;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE SubName: Full=Thymidine phosphorylase {ECO:0000313|EMBL:CAQ02928.1};
DE EC=2.4.2.4 {ECO:0000313|EMBL:CAQ02928.1};
GN Name=deoA {ECO:0000313|EMBL:CAQ02928.1};
GN OrderedLocusNames=CMS2857 {ECO:0000313|EMBL:CAQ02928.1};
OS Clavibacter michiganensis subsp. sepedonicus (strain ATCC 33113 / DSM 20744
OS / JCM 9667 / LMG 2889 / C-1) (Corynebacterium sepedonicum).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Clavibacter.
OX NCBI_TaxID=31964 {ECO:0000313|EMBL:CAQ02928.1, ECO:0000313|Proteomes:UP000001318};
RN [1] {ECO:0000313|EMBL:CAQ02928.1, ECO:0000313|Proteomes:UP000001318}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33113 / DSM 20744 / JCM 9667 / LMG 2889 / C-1
RC {ECO:0000313|Proteomes:UP000001318};
RX PubMed=18192393; DOI=10.1128/JB.01598-07;
RA Bentley S.D., Corton C., Brown S.E., Barron A., Clark L., Doggett J.,
RA Harris B., Ormond D., Quail M.A., May G., Francis D., Knudson D.,
RA Parkhill J., Ishimaru C.A.;
RT "Genome of the actinomycete plant pathogen Clavibacter michiganensis subsp.
RT sepedonicus suggests recent niche adaptation.";
RL J. Bacteriol. 190:2150-2160(2008).
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; AM849034; CAQ02928.1; -; Genomic_DNA.
DR RefSeq; WP_012300084.1; NZ_MZMN01000003.1.
DR AlphaFoldDB; B0RBN2; -.
DR STRING; 31964.CMS2857; -.
DR KEGG; cms:CMS2857; -.
DR eggNOG; COG0213; Bacteria.
DR HOGENOM; CLU_025040_0_1_11; -.
DR OrthoDB; 9763887at2; -.
DR Proteomes; UP000001318; 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:CAQ02928.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CAQ02928.1}.
FT DOMAIN 338..412
FT /note="Pyrimidine nucleoside phosphorylase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00941"
SQ SEQUENCE 432 AA; 45667 MW; 0F599F61D7BAA561 CRC64;
MSAAFDVVDL IRTKRDGGRL STAEIDWLVA AYTDRYVADE QMAALAMAIL LRGMDRTEIR
DLTLAMIASG ETLDFSRLGK PTVDKHSTGG VGDKITLPLM PLVASYGVAV PQLSGRGLGH
TGGTLDKLES IPGWRADLST EEMVRQMRDH GGVICAAGSG LAPADKRLYA LRDTTGTVEA
IPLIASSIMS KKIAEGTGAL VLDVKFGSGA FMTDIDRSRE LARTMVELGT DAGVRTTALL
TDMDVPLGLA IGNANEVRES LEVLAGGGPA DVVELTLALA REMLAAVGIP DADVDVALRD
GRAMDSWRAT VRAQGGDPDA AMPVARETHV VTAERDGVLV QQDALPFGIA AWRLGTGRAR
QGDAVQHAAG VDLHAKPGDA VRRGDPLFTL STDEPERFAR ALESLEGAYR VGDAEEHVAR
GPLVRERITA EG
//