ID K9EXM4_9LACT Unreviewed; 433 AA.
AC K9EXM4;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Pyrimidine-nucleoside phosphorylase {ECO:0000256|ARBA:ARBA00014680};
DE EC=2.4.2.2 {ECO:0000256|ARBA:ARBA00011889};
GN ORFNames=HMPREF9698_00455 {ECO:0000313|EMBL:EKU93975.1};
OS Alloiococcus otitis ATCC 51267.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC Alloiococcus.
OX NCBI_TaxID=883081 {ECO:0000313|EMBL:EKU93975.1, ECO:0000313|Proteomes:UP000009875};
RN [1] {ECO:0000313|EMBL:EKU93975.1, ECO:0000313|Proteomes:UP000009875}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51267 {ECO:0000313|EMBL:EKU93975.1,
RC ECO:0000313|Proteomes:UP000009875};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Huys G., Walker B., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Goldberg J., Griggs A., Gujja S.,
RA Hansen M., Howarth C., Imamovic A., Larimer J., McCowen C., Montmayeur A.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Alloiococcus otitis ATCC 51267.";
RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes phosphorolysis of the pyrimidine nucleosides
CC uridine, thymidine and 2'-deoxyuridine with the formation of the
CC corresponding pyrimidine base and ribose-1-phosphate.
CC {ECO:0000256|ARBA:ARBA00003877}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2'-deoxyuridine + phosphate = 2-deoxy-alpha-D-ribose 1-
CC phosphate + uracil; Xref=Rhea:RHEA:22824, ChEBI:CHEBI:16450,
CC ChEBI:CHEBI:17568, ChEBI:CHEBI:43474, ChEBI:CHEBI:57259; EC=2.4.2.2;
CC Evidence={ECO:0000256|ARBA:ARBA00001066};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=phosphate + thymidine = 2-deoxy-alpha-D-ribose 1-phosphate +
CC thymine; Xref=Rhea:RHEA:16037, ChEBI:CHEBI:17748, ChEBI:CHEBI:17821,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57259; EC=2.4.2.2;
CC Evidence={ECO:0000256|ARBA:ARBA00000722};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=phosphate + uridine = alpha-D-ribose 1-phosphate + uracil;
CC Xref=Rhea:RHEA:24388, ChEBI:CHEBI:16704, ChEBI:CHEBI:17568,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57720; EC=2.4.2.2;
CC Evidence={ECO:0000256|ARBA:ARBA00001004};
CC -!- COFACTOR:
CC Name=K(+); Xref=ChEBI:CHEBI:29103;
CC Evidence={ECO:0000256|ARBA:ARBA00001958};
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:EKU93975.1}.
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DR EMBL; AGXA01000007; EKU93975.1; -; Genomic_DNA.
DR RefSeq; WP_003776941.1; NZ_JH992957.1.
DR AlphaFoldDB; K9EXM4; -.
DR STRING; 883081.HMPREF9698_00455; -.
DR PATRIC; fig|883081.3.peg.455; -.
DR eggNOG; COG0213; Bacteria.
DR HOGENOM; CLU_025040_0_1_9; -.
DR OrthoDB; 9763887at2; -.
DR Proteomes; UP000009875; 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 Reference proteome {ECO:0000313|Proteomes:UP000009875};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 345..418
FT /note="Pyrimidine nucleoside phosphorylase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00941"
SQ SEQUENCE 433 AA; 46603 MW; 36165AA14AE0E141 CRC64;
MRMVDLIEKK RDGQALSQDE ITWMVDQYSK DQIKDYQMSA MLMAIYFQGM SHEEAGYLTM
SMVESGDQID LSQIDGIKVD KHSTGGVGDT TTLILAPLVA SLGVPVAKMS GRGLGHTGGT
IDKLESIPGF HIELTSEEFV NQVNQHKIAL VGQSGNLTPA DKKLYALRDV TATVNAIPLI
ASSIMSKKIA AGNDAIVLDV KVGSGAFMKD DQAGEDLART MVKIGRSVGR QTMALVSDMS
QPLGRAIGNA LEVKEAIDVL KGKGPEDLRE LVLALGSQML VLAKQAKDLN QGKQKLLQAI
QSGQALAKFK ELLEIQGGNS QVVEDSDLLP QAKYQIDLPA LESGYISSMV ADKIGQASMV
LGAGRKKLDD QINPAVGLIL HKKIGDPVEK GEPLLTIHSD QVRVEEVKAL LYDSIRISSQ
AQKPQLIHQI IGS
//
