ID Q1D0H5_MYXXD Unreviewed; 434 AA.
AC Q1D0H5;
DT 11-JUL-2006, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2006, sequence version 1.
DT 27-MAR-2024, entry version 113.
DE SubName: Full=Pyrimidine-nucleoside phosphorylase {ECO:0000313|EMBL:ABF91657.1};
DE EC=2.4.2.2 {ECO:0000313|EMBL:ABF91657.1};
GN Name=pdp {ECO:0000313|EMBL:ABF91657.1};
GN OrderedLocusNames=MXAN_5710 {ECO:0000313|EMBL:ABF91657.1};
OS Myxococcus xanthus (strain DK1622).
OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC Myxococcaceae; Myxococcus.
OX NCBI_TaxID=246197 {ECO:0000313|EMBL:ABF91657.1, ECO:0000313|Proteomes:UP000002402};
RN [1] {ECO:0000313|EMBL:ABF91657.1, ECO:0000313|Proteomes:UP000002402}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DK1622 {ECO:0000313|Proteomes:UP000002402};
RX PubMed=17015832; DOI=10.1073/pnas.0607335103;
RA Goldman B.S., Nierman W.C., Kaiser D., Slater S.C., Durkin A.S.,
RA Eisen J.A., Ronning C.M., Barbazuk W.B., Blanchard M., Field C.,
RA Halling C., Hinkle G., Iartchuk O., Kim H.S., Mackenzie C., Madupu R.,
RA Miller N., Shvartsbeyn A., Sullivan S.A., Vaudin M., Wiegand R.,
RA Kaplan H.B.;
RT "Evolution of sensory complexity recorded in a myxobacterial genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15200-15205(2006).
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; CP000113; ABF91657.1; -; Genomic_DNA.
DR RefSeq; WP_011555662.1; NC_008095.1.
DR AlphaFoldDB; Q1D0H5; -.
DR STRING; 246197.MXAN_5710; -.
DR EnsemblBacteria; ABF91657; ABF91657; MXAN_5710.
DR GeneID; 41362955; -.
DR KEGG; mxa:MXAN_5710; -.
DR eggNOG; COG0213; Bacteria.
DR HOGENOM; CLU_025040_0_1_7; -.
DR OrthoDB; 9763887at2; -.
DR Proteomes; UP000002402; 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:ABF91657.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002402};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ABF91657.1}.
FT DOMAIN 345..419
FT /note="Pyrimidine nucleoside phosphorylase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00941"
SQ SEQUENCE 434 AA; 46343 MW; B60F98ADA332279D CRC64;
MQPYELIKAK RDGGRLEPAD IRAFIEAYTA GTVADYQMAA MCMAIFFRGM DSRELGAWAR
AMLESGEVLD LSDTPGVKVD KHSTGGVGDK VSLSLAPLAA ACGVPVPMIS GRGLGHTGGT
LDKLESIPGF NVNLPTSEYR RLVREVNCCL IGQTAQVAPA DKKLYALRDV TATVDCIPLI
ASSIMSKKLA EGIDALVLDV KVGSGAFMKR DEDARTLAKT MIGLGAEMGK KVVALLTDMD
QPLGRKVGNA LEVIEAVDML RGNAPEDYTE VTYALTAEML VLGKKAATVE EAREKLRKVV
EDGSAVRKLK EIVQVQGGDP RSIDDYSLLP QAKATVDVVA PRDGFVTGID TEGVGMAAVA
LGAGRQRTDS KIDPAVGFTL LKKSGESVKQ GEPVVRVHYN DAAQLENVKA RLLAAYRFGD
VAPVARPLIR ERVE
//
