ID   RBKTP_AZOC5             Reviewed;         693 AA.
AC   A8IA58;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 1.
DT   27-MAR-2024, entry version 93.
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=AZC_2467;
OS   Azorhizobium caulinodans (strain ATCC 43989 / DSM 5975 / JCM 20966 / LMG
OS   6465 / NBRC 14845 / NCIMB 13405 / ORS 571).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Xanthobacteraceae; Azorhizobium.
OX   NCBI_TaxID=438753;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43989 / DSM 5975 / JCM 20966 / LMG 6465 / NBRC 14845 /
RC   NCIMB 13405 / ORS 571;
RA   Lee K.B., Backer P.D., Aono T., Liu C.T., Suzuki S., Suzuki T., Kaneko T.,
RA   Yamada M., Tabata S., Kupfer D.M., Najar F.Z., Wiley G.B., Roe B.,
RA   Binnewies T., Ussery D., Vereecke D., Gevers D., Holsters M., Oyaizu H.;
RT   "Complete genome sequence of the nitrogen-fixing bacterium Azorhizobium
RT   caulinodans ORS571.";
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
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; AP009384; BAF88465.1; -; Genomic_DNA.
DR   AlphaFoldDB; A8IA58; -.
DR   SMR; A8IA58; -.
DR   STRING; 438753.AZC_2467; -.
DR   KEGG; azc:AZC_2467; -.
DR   eggNOG; COG0213; Bacteria.
DR   eggNOG; COG3709; Bacteria.
DR   HOGENOM; CLU_025040_6_0_5; -.
DR   UniPathway; UPA00087; UER00175.
DR   Proteomes; UP000000270; 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; 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; 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; 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..693
FT                   /note="Bifunctional ribose 1,5-bisphosphokinase-thymidine
FT                   phosphorylase"
FT                   /id="PRO_0000314696"
FT   REGION          1..193
FT                   /note="Ribose 1,5-bisphosphokinase"
FT   REGION          194..693
FT                   /note="Thymidinephosphorylase"
FT   BINDING         14..21
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   693 AA;  72760 MW;  8847CD4C7646E9EB CRC64;
     MSVMGSGLFF FVVGPSGSGK DTLIEGAKAA LGPTGRYVFA RRAITRPADA GGEAHEALSV
     DQFDAVLAQG GFLIHWEAHG LKYGLRATLL DDMAAGRHVI ANGSRAMVAA LAERVPHLVV
     VEITAPEAVL AERLKGRGRE GAENIAARLE RKVPPFPESV TVIQVPNDST PRAGIEKFVA
     ALVAQTARLR LVRMAIETGR RNVAFLARGN TVVAAPDYLG PGRVDLIGEG RSIRAEVALV
     GDALLPSDAV GLSSEAFGAL GLPEGAELVL TRTPVPESRA ALRRKIQGAT LDEGAYAQVV
     GDIVEGRYPD SEVAGFLVAA DRSLSDDEVL ALAKVRAKFA SRITWDEPMV VDKHSMGGIP
     GSRITMIVVP IVAAHGLAIP KTSSRAITSA AGTADAMETL ARVDLDSAEV RRTVERARGC
     IAWNGRLSHS ALDDVMNAIT RPLGLDSTRW SVASILSKKL AAGSTHVVID LPFGARARVK
     GAGEAHEMAR LFEQVGAGLG LTVEAIPTDG SAPIGRGIGP ALEVRDVLWV LEDHSEAPPD
     LKEKALFFAS RILAWDPAVG PDRARARAEE LLASGAARAA LERIVEAQGR WSEPVRPARL
     THTVTAQNDG QVSDIDGFAV AGIARLAGAP LDKGAGIDLK ARVGDVVRAG DPLFVIHAST
     AADLEAAAGA ALAFDGYGIM MDGKAFRRIN PER
//