RBKTP_CUPPJ
ID RBKTP_CUPPJ Reviewed; 602 AA.
AC Q46UT0;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 03-AUG-2022, entry version 99.
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=Reut_B3746;
OS Cupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Cupriavidus necator
OS (strain JMP 134)).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=264198;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JMP134 / LMG 1197;
RX PubMed=20339589; DOI=10.1371/journal.pone.0009729;
RA Lykidis A., Perez-Pantoja D., Ledger T., Mavromatis K., Anderson I.J.,
RA Ivanova N.N., Hooper S.D., Lapidus A., Lucas S., Gonzalez B.,
RA Kyrpides N.C.;
RT "The complete multipartite genome sequence of Cupriavidus necator JMP134, a
RT versatile pollutant degrader.";
RL PLoS ONE 5:E9729-E9729(2010).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAZ63104.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CP000091; AAZ63104.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_041680127.1; NC_007348.1.
DR AlphaFoldDB; Q46UT0; -.
DR SMR; Q46UT0; -.
DR STRING; 264198.Reut_B3746; -.
DR EnsemblBacteria; AAZ63104; AAZ63104; Reut_B3746.
DR KEGG; reu:Reut_B3746; -.
DR eggNOG; COG0213; Bacteria.
DR HOGENOM; CLU_025040_6_0_4; -.
DR OMA; HDDVRRC; -.
DR OrthoDB; 1724909at2; -.
DR UniPathway; UPA00087; UER00175.
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; IPR000312; Glycosyl_Trfase_fam3.
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; IPR000053; Thymidine/pyrmidine_PPase.
DR PANTHER; PTHR10515; PTHR10515; 1.
DR Pfam; PF00591; Glycos_transf_3; 1.
DR Pfam; PF07831; PYNP_C; 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; 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; Transferase.
FT CHAIN 1..602
FT /note="Bifunctional ribose 1,5-bisphosphokinase-thymidine
FT phosphorylase"
FT /id="PRO_0000314710"
FT REGION 1..187
FT /note="Ribose 1,5-bisphosphokinase"
FT REGION 188..602
FT /note="Thymidinephosphorylase"
SQ SEQUENCE 602 AA; 63580 MW; D622AFD8F873E7CA CRC64;
MKESGTFFLV VGPSGAGKDS LIDGARATLG NDEYVFARRI ITRPSGSPGE DHESVAEAEF
AERERNGEFL VTWHAHGLRY GLPQWLVGLL ETGKHVVANG SRGVIAMLAR QLPRFVVVNV
TAPQDVLAQR IAARGRESGD DVMRRVARQA PPMPDGVHCV TVTNDSTLDL GVARFTDALR
NGANAGSVPQ PASRRHLAAK LDGQPLDEGA YEAILRDAIA GRYTAQELTA FLTAATRSLD
DREVVALARA RTRFTARIEW DEPIVVDKHS MGGIPGSRIT LIVVPIVAAY GLAMPKTSSR
AITSAAGTAD AMETVARVDL THDDVRRCVA QARACIAWNG RLNHSVIDDV MNAITRPLGL
DSRRWAVASI LSKKATAGAT HVIVDIPYGP QTKLSARADA DALAGLFEEV GKGLGLHVRA
LVTDGSRPIG RGVGPALEVR DVRQVLENHP DAPMDLREKA LRFAGEIIAF DPRVASAAQG
MRIATALLDE GSARAAFDRI VATQGIRPDP VAPGAHTHVI VAPAEGRVAA INGWQISGIA
RAAGAPRSAG AGIDLLCTIG ERVAAGEPLY RIHAESAADL ATAVAMTGPA GEASTAVRVD
PD
