ID A0A0U2XRS1_9BURK Unreviewed; 592 AA.
AC A0A0U2XRS1;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=Ribose 1,5-bisphosphate phosphokinase PhnN {ECO:0000256|HAMAP-Rule:MF_00836};
DE EC=2.7.4.23 {ECO:0000256|HAMAP-Rule:MF_00836};
DE AltName: Full=Ribose 1,5-bisphosphokinase {ECO:0000256|HAMAP-Rule:MF_00836};
GN Name=phnN {ECO:0000256|HAMAP-Rule:MF_00836};
GN ORFNames=AT302_20350 {ECO:0000313|EMBL:ALS61774.1};
OS Pandoraea norimbergensis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Pandoraea.
OX NCBI_TaxID=93219 {ECO:0000313|EMBL:ALS61774.1, ECO:0000313|Proteomes:UP000060277};
RN [1] {ECO:0000313|Proteomes:UP000060277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11628 {ECO:0000313|Proteomes:UP000060277};
RA Ee R., Lim Y.-L., Yong D., Yin W.-F., Chan K.-G.;
RT "Complete genome sequence of Pandoraea norimbergensis DSM 11628.";
RL Submitted (DEC-2015) 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).
CC {ECO:0000256|ARBA:ARBA00002554, ECO:0000256|HAMAP-Rule:MF_00836}.
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; Evidence={ECO:0000256|ARBA:ARBA00000373,
CC ECO:0000256|HAMAP-Rule:MF_00836};
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 Evidence={ECO:0000256|ARBA:ARBA00000749};
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 {ECO:0000256|ARBA:ARBA00005069, ECO:0000256|HAMAP-Rule:MF_00836}.
CC -!- SIMILARITY: Belongs to the ribose 1,5-bisphosphokinase family.
CC {ECO:0000256|HAMAP-Rule:MF_00836}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the
CC thymidine/pyrimidine-nucleoside phosphorylase family. Type 2 subfamily.
CC {ECO:0000256|ARBA:ARBA00008689}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the ribose 1,5-
CC bisphosphokinase family. {ECO:0000256|ARBA:ARBA00005935}.
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DR EMBL; CP013480; ALS61774.1; -; Genomic_DNA.
DR RefSeq; WP_058378684.1; NZ_CP013480.3.
DR AlphaFoldDB; A0A0U2XRS1; -.
DR STRING; 93219.AT302_20350; -.
DR KEGG; pnr:AT302_20350; -.
DR OrthoDB; 341217at2; -.
DR UniPathway; UPA00087; UER00175.
DR Proteomes; UP000060277; 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-EC.
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: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 InterPro; IPR008145; GK/Ca_channel_bsu.
DR InterPro; IPR000312; Glycosyl_Trfase_fam3.
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; IPR000053; Thymidine/pyrmidine_PPase.
DR NCBIfam; TIGR02322; phosphon_PhnN; 1.
DR PANTHER; PTHR10515; THYMIDINE PHOSPHORYLASE; 1.
DR PANTHER; PTHR10515:SF0; THYMIDINE PHOSPHORYLASE; 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; 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 ATP-binding {ECO:0000256|HAMAP-Rule:MF_00836};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00836};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00836}.
FT DOMAIN 4..184
FT /note="Guanylate kinase/L-type calcium channel beta
FT subunit"
FT /evidence="ECO:0000259|SMART:SM00072"
FT DOMAIN 523..590
FT /note="Pyrimidine nucleoside phosphorylase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00941"
FT BINDING 12..19
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00836"
SQ SEQUENCE 592 AA; 62520 MW; D8A2775C333E4107 CRC64;
MTLPGIFFFV VGPSGAGKDT LIDGARTCLT DGGRFVFATR TITRADDAPG EAHIGVTEAE
FAARDAAGAF LVTWQAHGLH YGLDASLRDV LAQGRHVVAN GSRAILPKLI GRVQRLVIVE
VSAPVEVLAA RIAGRGRETP EQIAARLART VTAYPAGVPL VRVSNDSTSD VGIARFTAAL
QACAQPPKSR ELADAKRTGV SLNEASWGQL LDDLMYDRYA PDEGEALLRL LIEHIDDDEI
VALTRARTRL MPRIDWGRPM VVDKHSMGGV PGSRITLIVV PLVVAYGLCM PKTSSRAITS
AAGTADAMEA AARVDLDAAE VRAAVEQAGG CIVWNGRLNH SRVDDVTNAM VRPLRLDTRR
WSVASILSKK FCAGSTHVVV DLPWGPQAKM TDEAQARKLG ALFERVGAAL GMTVQAFATD
GRAPIGRGIG PALELRDVLQ VLDNDATAPK DLRAKALTFA ARILSWHPAL GGDLVKAHAT
AEQLLASGEA RRAFERIVDA QGRKDFAMPA ASFVDIVAQA DGVVASIDGW EVSGIARDAG
GPTDMGAGVD LLCATGQSVR AGDALLRVHG NDPQRLAAAA ARAQDVSGIV LQ
//
