ID   RBKTP_ROSDO             Reviewed;         677 AA.
AC   Q16A32;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   27-MAR-2024, entry version 111.
DE   RecName: Full=Bifunctional ribose 1,5-bisphosphokinase-thymidine phosphorylase;
DE   Includes:
DE     RecName: Full=Ribose 1,5-bisphosphate phosphokinase PhnN;
DE              EC=2.7.4.23;
DE     AltName: Full=Ribose 1,5-bisphosphokinase;
DE   Includes:
DE     RecName: Full=Putative thymidine phosphorylase;
DE              EC=2.4.2.4;
DE     AltName: Full=TdRPase;
GN   Name=phnN; OrderedLocusNames=RD1_1528;
OS   Roseobacter denitrificans (strain ATCC 33942 / OCh 114) (Erythrobacter sp.
OS   (strain OCh 114)) (Roseobacter denitrificans).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Roseobacter.
OX   NCBI_TaxID=375451;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33942 / OCh 114;
RX   PubMed=17098896; DOI=10.1128/jb.01390-06;
RA   Swingley W.D., Sadekar S., Mastrian S.D., Matthies H.J., Hao J., Ramos H.,
RA   Acharya C.R., Conrad A.L., Taylor H.L., Dejesa L.C., Shah M.K.,
RA   O'Huallachain M.E., Lince M.T., Blankenship R.E., Beatty J.T.,
RA   Touchman J.W.;
RT   "The complete genome sequence of Roseobacter denitrificans reveals a
RT   mixotrophic rather than photosynthetic metabolism.";
RL   J. Bacteriol. 189:683-690(2007).
CC   -!- FUNCTION: Catalyzes the phosphorylation of ribose 1,5-bisphosphate to
CC       5-phospho-D-ribosyl alpha-1-diphosphate (PRPP). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=alpha-D-ribose 1,5-bisphosphate + ATP = 5-phospho-alpha-D-
CC         ribose 1-diphosphate + ADP; Xref=Rhea:RHEA:20109, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:58017, ChEBI:CHEBI:68688, ChEBI:CHEBI:456216;
CC         EC=2.7.4.23;
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=2.4.2.4;
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; 5-phospho-alpha-D-ribose
CC       1-diphosphate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate from
CC       D-ribose 5-phosphate (route II): step 3/3.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the ribose 1,5-
CC       bisphosphokinase family. {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the
CC       thymidine/pyrimidine-nucleoside phosphorylase family. Type 2 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; CP000362; ABG31161.1; -; Genomic_DNA.
DR   RefSeq; WP_011567781.1; NZ_FOOO01000013.1.
DR   AlphaFoldDB; Q16A32; -.
DR   SMR; Q16A32; -.
DR   STRING; 375451.RD1_1528; -.
DR   KEGG; rde:RD1_1528; -.
DR   eggNOG; COG0213; Bacteria.
DR   eggNOG; COG3709; Bacteria.
DR   HOGENOM; CLU_025040_6_0_5; -.
DR   OrthoDB; 341217at2; -.
DR   UniPathway; UPA00087; UER00175.
DR   Proteomes; UP000007029; Chromosome.
DR   GO; GO:0004645; F:1,4-alpha-oligoglucan phosphorylase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0033863; F:ribose 1,5-bisphosphate phosphokinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009032; F:thymidine phosphorylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006015; P:5-phosphoribose 1-diphosphate biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0019634; P:organic phosphonate metabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0015716; P:organic phosphonate transport; IEA:UniProtKB-KW.
DR   GO; GO:0006206; P:pyrimidine nucleobase metabolic process; IEA:InterPro.
DR   GO; GO:0006213; P:pyrimidine nucleoside metabolic process; IEA:InterPro.
DR   Gene3D; 1.20.970.50; -; 1.
DR   Gene3D; 3.40.1030.10; Nucleoside phosphorylase/phosphoribosyltransferase catalytic domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 3.90.1170.30; Pyrimidine nucleoside phosphorylase-like, C-terminal domain; 1.
DR   HAMAP; MF_00836; PhnN; 1.
DR   HAMAP; MF_00703; Thymid_phosp_2; 1.
DR   InterPro; IPR008145; GK/Ca_channel_bsu.
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; IPR008144; Guanylate_kin-like_dom.
DR   InterPro; IPR035902; Nuc_phospho_transferase.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR012699; PhnN.
DR   InterPro; IPR036566; PYNP-like_C_sf.
DR   InterPro; IPR013102; PYNP_C.
DR   InterPro; IPR017872; Pyrmidine_PPase_CS.
DR   InterPro; IPR028579; Thym_Pase_Put.
DR   InterPro; IPR013466; Thymidine/AMP_Pase.
DR   InterPro; IPR000053; Thymidine/pyrmidine_PPase.
DR   NCBIfam; TIGR02645; ARCH_P_rylase; 1.
DR   NCBIfam; TIGR02322; phosphon_PhnN; 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; PF00625; Guanylate_kin; 1.
DR   Pfam; PF07831; PYNP_C; 1.
DR   SMART; SM00072; GuKc; 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; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF54680; Pyrimidine nucleoside phosphorylase C-terminal domain; 1.
DR   PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
DR   PROSITE; PS00647; THYMID_PHOSPHORYLASE; 1.
PE   3: Inferred from homology;
KW   Alkylphosphonate uptake; ATP-binding; Glycosyltransferase;
KW   Multifunctional enzyme; Nucleotide-binding; Reference proteome;
KW   Transferase.
FT   CHAIN           1..677
FT                   /note="Bifunctional ribose 1,5-bisphosphokinase-thymidine
FT                   phosphorylase"
FT                   /id="PRO_0000314717"
FT   REGION          1..187
FT                   /note="Ribose 1,5-bisphosphokinase"
FT   REGION          188..677
FT                   /note="Thymidinephosphorylase"
SQ   SEQUENCE   677 AA;  72031 MW;  21D61E53D52766DE CRC64;
     MPGTLFLIVG PSGVGKDTLL EGARDRLATS RWFSFPQRVV TRAADAGGED YIPVTPSEFE
     QQLAAGAFWH QWHAHGLSYG IPMQVARDLD NGINVVLNAS RNEIGAFRDK ATHVVTIGIS
     APPGIVEERL HERGRESEEE IKRRLARLVE QAPLTGYALE IVNDRTIEEG ITALVDLIAG
     ACDLNAEITR FPVTIGSKQV CLVHKGNQIA SRVLAGSSRV TLSLRGKSVS AELGETWSDE
     IVSQDLCALS EGAMAALDAV EGDVVSIERS PTPKSRSILQ KKVRGGELSH AEMEAFIHDL
     VNGRFSTSEI AGFLVAASNN LTMDEVISLT QVRAAFAHRH DWGKAIVVDK HSMGGVPGNR
     ITPIIIPILA AFGLTVPKTS SRAITSAAGT ADMMEVLSRV DLSPDEMKSV VEQTNGCIAW
     NGNLTHSPVD DVMNAINRPL GLQSTLLDVS SIMSKKLAAG STHVLIDMPV GPKAKTRTQG
     EAGALKNLFE SVGQGIGLNT KVQISDGTKP IGRGVGPVLE ALDVLSVLRG EAGAPTDLLD
     KSIGYAATIL EWSGAVSQGQ GAQVTRDLVS SGKAFEKLFE IRDAQGRQHD PLQPGQFTED
     ICADRSGRVE AIDIQGISEV ARLSGAPKDK AAGVVLNVQV GDQIAEKQPL LRVHSSSLRG
     IEEAVCAAQA QSAFKIL
//