ID A1K3G7_AZOSB Unreviewed; 316 AA.
AC A1K3G7;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 103.
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=prsA {ECO:0000313|EMBL:CAL93372.1};
GN Synonyms=prs {ECO:0000256|HAMAP-Rule:MF_00583};
GN OrderedLocusNames=azo0755 {ECO:0000313|EMBL:CAL93372.1};
OS Azoarcus sp. (strain BH72).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC Azoarcus.
OX NCBI_TaxID=418699 {ECO:0000313|EMBL:CAL93372.1, ECO:0000313|Proteomes:UP000002588};
RN [1] {ECO:0000313|EMBL:CAL93372.1, ECO:0000313|Proteomes:UP000002588}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BH72 {ECO:0000313|EMBL:CAL93372.1,
RC ECO:0000313|Proteomes:UP000002588};
RX PubMed=17057704; DOI=10.1038/nbt1243;
RA Krause A., Ramakumar A., Bartels D., Battistoni F., Bekel T., Boch J.,
RA Boehm M., Friedrich F., Hurek T., Krause L., Linke B., McHardy A.C.,
RA Sarkar A., Schneiker S., Syed A.A., Thauer R., Vorhoelter F.-J.,
RA Weidner S., Puehler A., Reinhold-Hurek B., Kaiser O., Goesmann A.;
RT "Complete genome of the mutualistic, N2-fixing grass endophyte Azoarcus sp.
RT strain BH72.";
RL Nat. Biotechnol. 24:1385-1391(2006).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AM406670; CAL93372.1; -; Genomic_DNA.
DR RefSeq; WP_011764489.1; NZ_CP016210.1.
DR AlphaFoldDB; A1K3G7; -.
DR STRING; 62928.azo0755; -.
DR KEGG; aoa:dqs_0829; -.
DR KEGG; azo:azo0755; -.
DR eggNOG; COG0462; Bacteria.
DR HOGENOM; CLU_033546_2_0_4; -.
DR OrthoDB; 9777067at2; -.
DR UniPathway; UPA00087; UER00172.
DR Proteomes; UP000002588; Chromosome.
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; 2.
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:UP000002588};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00583}.
FT DOMAIN 6..123
FT /note="Ribose-phosphate pyrophosphokinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF13793"
FT ACT_SITE 195
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00583"
FT BINDING 39..41
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00583"
FT BINDING 98..99
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00583"
FT BINDING 133
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00583"
FT BINDING 172
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00583"
FT BINDING 197
FT /ligand="D-ribose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:78346"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00583"
FT BINDING 221
FT /ligand="D-ribose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:78346"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00583"
FT BINDING 225..229
FT /ligand="D-ribose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:78346"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00583"
SQ SEQUENCE 316 AA; 34200 MW; 1F77E812B2E096BF CRC64;
MPYGSLMVFT GNANPKLAAD VARRLGISLG SVTVGRFSDG EVNVELLENV RGKDVFILQP
TCAPTNENLM ELLVLVDALK RASAGRITAA IPYFGYARQD RRPRSARVPI TAKVVANMLQ
AVGVQRVLTM DLHADQIQGF FDIPVDNVYA APVLLADLDK QKYDDLMVVS PDVGGVVRAR
AFAKRMECDL AIIDKRRPKA NVSEVMNIIG EVDGRTCVIM DDIVDTAGTL CKAASALKEH
GAKRVLAYCT HAVLSGAAVS RINDSELDEL VVTDTIPLRD DAKASSRIRQ VSVASLLADT
VLRISNEESV SSLFME
//
