RBKTP_AZOC5
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 03-AUG-2022, entry version 87.
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; Proteobacteria; 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 / NCIMB
RC 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 EnsemblBacteria; BAF88465; BAF88465; AZC_2467.
DR KEGG; azc:AZC_2467; -.
DR eggNOG; COG0213; Bacteria.
DR eggNOG; COG3709; Bacteria.
DR HOGENOM; CLU_025040_6_0_5; -.
DR OMA; QMVASIM; -.
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; 3.40.1030.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR Gene3D; 3.90.1170.30; -; 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 PANTHER; PTHR10515; PTHR10515; 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; SSF47648; SSF47648; 1.
DR SUPFAM; SSF52418; SSF52418; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF54680; SSF54680; 1.
DR TIGRFAMs; TIGR02645; ARCH_P_rylase; 1.
DR TIGRFAMs; TIGR02322; phosphon_PhnN; 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
