ID A0A0Q5ATM3_9MICO Unreviewed; 325 AA.
AC A0A0Q5ATM3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Ribose-phosphate pyrophosphokinase {ECO:0000256|HAMAP-Rule:MF_00583};
DE Short=RPPK {ECO:0000256|HAMAP-Rule:MF_00583};
DE EC=2.7.6.1 {ECO:0000256|HAMAP-Rule:MF_00583};
DE AltName: Full=5-phospho-D-ribosyl alpha-1-diphosphate synthase {ECO:0000256|HAMAP-Rule:MF_00583};
DE AltName: Full=Phosphoribosyl diphosphate synthase {ECO:0000256|HAMAP-Rule:MF_00583};
DE AltName: Full=Phosphoribosyl pyrophosphate synthase {ECO:0000256|HAMAP-Rule:MF_00583};
DE Short=P-Rib-PP synthase {ECO:0000256|HAMAP-Rule:MF_00583};
DE Short=PRPP synthase {ECO:0000256|HAMAP-Rule:MF_00583};
DE Short=PRPPase {ECO:0000256|HAMAP-Rule:MF_00583};
GN Name=prs {ECO:0000256|HAMAP-Rule:MF_00583};
GN ORFNames=ASF46_11600 {ECO:0000313|EMBL:KQQ08008.1};
OS Rathayibacter sp. Leaf296.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Rathayibacter.
OX NCBI_TaxID=1736327 {ECO:0000313|EMBL:KQQ08008.1, ECO:0000313|Proteomes:UP000050868};
RN [1] {ECO:0000313|EMBL:KQQ08008.1, ECO:0000313|Proteomes:UP000050868}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf296 {ECO:0000313|EMBL:KQQ08008.1,
RC ECO:0000313|Proteomes:UP000050868};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQQ08008.1, ECO:0000313|Proteomes:UP000050868}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf296 {ECO:0000313|EMBL:KQQ08008.1,
RC ECO:0000313|Proteomes:UP000050868};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in the biosynthesis of the central metabolite
CC phospho-alpha-D-ribosyl-1-pyrophosphate (PRPP) via the transfer of
CC pyrophosphoryl group from ATP to 1-hydroxyl of ribose-5-phosphate (Rib-
CC 5-P). {ECO:0000256|HAMAP-Rule:MF_00583}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-ribose 5-phosphate = 5-phospho-alpha-D-ribose 1-
CC diphosphate + AMP + H(+); Xref=Rhea:RHEA:15609, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58017, ChEBI:CHEBI:78346,
CC ChEBI:CHEBI:456215; EC=2.7.6.1; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_00583};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00583};
CC Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000256|HAMAP-
CC Rule:MF_00583};
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 I): step 1/1. {ECO:0000256|HAMAP-
CC Rule:MF_00583}.
CC -!- SUBUNIT: Homohexamer. {ECO:0000256|HAMAP-Rule:MF_00583}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00583}.
CC -!- SIMILARITY: Belongs to the ribose-phosphate pyrophosphokinase family.
CC Class I subfamily. {ECO:0000256|HAMAP-Rule:MF_00583}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KQQ08008.1}.
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DR EMBL; LMNR01000002; KQQ08008.1; -; Genomic_DNA.
DR RefSeq; WP_055793762.1; NZ_LMNR01000002.1.
DR AlphaFoldDB; A0A0Q5ATM3; -.
DR STRING; 1736327.ASF46_11600; -.
DR UniPathway; UPA00087; UER00172.
DR Proteomes; UP000050868; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004749; F:ribose phosphate diphosphokinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006015; P:5-phosphoribose 1-diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009165; P:nucleotide biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0009156; P:ribonucleoside monophosphate biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd06223; PRTases_typeI; 1.
DR Gene3D; 3.40.50.2020; -; 2.
DR HAMAP; MF_00583_B; RibP_PPkinase_B; 1.
DR InterPro; IPR000842; PRib_PP_synth_CS.
DR InterPro; IPR029099; Pribosyltran_N.
DR InterPro; IPR000836; PRibTrfase_dom.
DR InterPro; IPR029057; PRTase-like.
DR InterPro; IPR005946; Rib-P_diPkinase.
DR InterPro; IPR037515; Rib-P_diPkinase_bac.
DR NCBIfam; TIGR01251; ribP_PPkin; 1.
DR PANTHER; PTHR10210; RIBOSE-PHOSPHATE DIPHOSPHOKINASE FAMILY MEMBER; 1.
DR PANTHER; PTHR10210:SF119; RIBOSE-PHOSPHATE PYROPHOSPHOKINASE; 1.
DR Pfam; PF14572; Pribosyl_synth; 1.
DR Pfam; PF13793; Pribosyltran_N; 1.
DR SMART; SM01400; Pribosyltran_N; 1.
DR SUPFAM; SSF53271; PRTase-like; 1.
DR PROSITE; PS00114; PRPP_SYNTHASE; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00583}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00583};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_00583};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00583};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00583};
KW Nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022727, ECO:0000256|HAMAP-
KW Rule:MF_00583}; Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00583};
KW Reference proteome {ECO:0000313|Proteomes:UP000050868};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00583}.
FT DOMAIN 13..128
FT /note="Ribose-phosphate pyrophosphokinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF13793"
FT ACT_SITE 201
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00583"
FT BINDING 45..47
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00583"
FT BINDING 104..105
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00583"
FT BINDING 138
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00583"
FT BINDING 178
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00583"
FT BINDING 203
FT /ligand="D-ribose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:78346"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00583"
FT BINDING 229
FT /ligand="D-ribose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:78346"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00583"
FT BINDING 233..237
FT /ligand="D-ribose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:78346"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00583"
SQ SEQUENCE 325 AA; 35263 MW; 195694060E616F34 CRC64;
MTGITASNKK SLVLVSGRAH PALAEAVASE LGTELVTTEG RTFANGELYV RYGESVRGGD
VFVLQSHTSP INEWLMEQLI MVDALKRASA KRITVVAPFY PYARQDKKGR GREPISARLV
ADLFKAAGAD RIMSVDLHAA QIQGFFDGPV DHLFAMPVLL EHFREKLDPS TLTVVSPDMG
RVRVADIWSD KLGVPLAIIH KRRDPKVANQ VSVHEIVGEV KGRVCLLVDD LIDTGRTIAK
AAEALKNAGA IGVVVAATHA VFSDPARELL SSEFIDSVVV TDTLPLPEEK KWDRLTILPI
APLLARAIHE VFDDGSVTSM FDGDA
//
