RBKTP_ROSDO
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 03-AUG-2022, entry version 104.
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; Proteobacteria; 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 EnsemblBacteria; ABG31161; ABG31161; RD1_1528.
DR KEGG; rde:RD1_1528; -.
DR eggNOG; COG0213; Bacteria.
DR eggNOG; COG3709; Bacteria.
DR HOGENOM; CLU_025040_6_0_5; -.
DR OMA; QMVASIM; -.
DR OrthoDB; 1724909at2; -.
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; 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; 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 PANTHER; PTHR10515; PTHR10515; 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; 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; 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
