ID F4HFT9_GALAU Unreviewed; 316 AA.
AC F4HFT9;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 68.
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 OrderedLocusNames=UMN179_02279 {ECO:0000313|EMBL:AEC18292.1};
OS Gallibacterium anatis (strain UMN179) (Pasteurella anatis).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Gallibacterium.
OX NCBI_TaxID=1005058 {ECO:0000313|EMBL:AEC18292.1, ECO:0000313|Proteomes:UP000006908};
RN [1] {ECO:0000313|EMBL:AEC18292.1, ECO:0000313|Proteomes:UP000006908}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UMN179 {ECO:0000313|EMBL:AEC18292.1,
RC ECO:0000313|Proteomes:UP000006908};
RX PubMed=21602325; DOI=10.1128/JB.05177-11;
RA Johnson T.J., Fernandez-Alarcon C., Bojesen A.M., Nolan L.K., Trampel D.W.,
RA Seemann T.;
RT "Complete genome sequence of Gallibacterium anatis strain UMN179, isolated
RT from a laying hen with peritonitis.";
RL J. Bacteriol. 193:3676-3677(2011).
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}.
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DR EMBL; CP002667; AEC18292.1; -; Genomic_DNA.
DR RefSeq; WP_013747048.1; NC_015460.1.
DR AlphaFoldDB; F4HFT9; -.
DR STRING; 1005058.UMN179_02279; -.
DR GeneID; 77263163; -.
DR KEGG; gan:UMN179_02279; -.
DR eggNOG; COG0462; Bacteria.
DR HOGENOM; CLU_033546_2_0_6; -.
DR UniPathway; UPA00087; UER00172.
DR Proteomes; UP000006908; 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; 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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00583}.
FT DOMAIN 4..121
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 37..39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00583"
FT BINDING 96..97
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00583"
FT BINDING 131
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00583"
FT BINDING 171
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; 34342 MW; C6765D27395586DB CRC64;
MPDIKLFAGN ATPELAKKIS ERLYTSLSDA IVGRFSDGEI QIQINENVRG SDVFIVQSTC
APTNDSLMEL VVMIDALRRA SAGRITAVVP YFGYARQDRR VRSSRVPITA KVVADILSNV
GVDRVLTCDL HAEQIQGFFD VPVDNVFGSP VLLDDILKKT DLENPIVVSP DIGGVVRARA
VAKLLNDTDM AIIDKRRPRA NVSQVMHIIG DVADRDCILV DDMIDTGGTL CKAAEALKER
GAKRVFAYAT HAVFSGSAPK NIASPALDEI VVTDTIPLRP EIIALNKVRV LTLSGMLAEA
IRRISNEESI SAMFNN
//
