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KPRS_BIFLO
ID   KPRS_BIFLO              Reviewed;         340 AA.
AC   Q8G5P2;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   13-APR-2004, sequence version 2.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Ribose-phosphate pyrophosphokinase {ECO:0000255|HAMAP-Rule:MF_00583};
DE            Short=RPPK {ECO:0000255|HAMAP-Rule:MF_00583};
DE            EC=2.7.6.1 {ECO:0000255|HAMAP-Rule:MF_00583};
DE   AltName: Full=5-phospho-D-ribosyl alpha-1-diphosphate {ECO:0000255|HAMAP-Rule:MF_00583};
DE   AltName: Full=Phosphoribosyl diphosphate synthase {ECO:0000255|HAMAP-Rule:MF_00583};
DE   AltName: Full=Phosphoribosyl pyrophosphate synthase {ECO:0000255|HAMAP-Rule:MF_00583};
DE            Short=P-Rib-PP synthase {ECO:0000255|HAMAP-Rule:MF_00583};
DE            Short=PRPP synthase {ECO:0000255|HAMAP-Rule:MF_00583};
DE            Short=PRPPase {ECO:0000255|HAMAP-Rule:MF_00583};
GN   Name=prs {ECO:0000255|HAMAP-Rule:MF_00583}; Synonyms=prsA;
GN   OrderedLocusNames=BL0963;
OS   Bifidobacterium longum (strain NCC 2705).
OC   Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC   Bifidobacterium.
OX   NCBI_TaxID=206672;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCC 2705;
RX   PubMed=12381787; DOI=10.1073/pnas.212527599;
RA   Schell M.A., Karmirantzou M., Snel B., Vilanova D., Berger B., Pessi G.,
RA   Zwahlen M.-C., Desiere F., Bork P., Delley M., Pridmore R.D., Arigoni F.;
RT   "The genome sequence of Bifidobacterium longum reflects its adaptation to
RT   the human gastrointestinal tract.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14422-14427(2002).
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:0000255|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:0000255|HAMAP-
CC         Rule:MF_00583};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00583};
CC       Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000255|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:0000255|HAMAP-
CC       Rule:MF_00583}.
CC   -!- SUBUNIT: Homohexamer. {ECO:0000255|HAMAP-Rule:MF_00583}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00583}.
CC   -!- SIMILARITY: Belongs to the ribose-phosphate pyrophosphokinase family.
CC       Class I subfamily. {ECO:0000255|HAMAP-Rule:MF_00583}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAN24774.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AE014295; AAN24774.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_696138.1; NC_004307.2.
DR   RefSeq; WP_007052033.1; NC_004307.2.
DR   AlphaFoldDB; Q8G5P2; -.
DR   SMR; Q8G5P2; -.
DR   STRING; 206672.BL0963; -.
DR   EnsemblBacteria; AAN24774; AAN24774; BL0963.
DR   KEGG; blo:BL0963; -.
DR   PATRIC; fig|206672.9.peg.667; -.
DR   HOGENOM; CLU_033546_2_0_11; -.
DR   OMA; FGWARQD; -.
DR   UniPathway; UPA00087; UER00172.
DR   Proteomes; UP000000439; 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   PANTHER; PTHR10210; PTHR10210; 1.
DR   Pfam; PF14572; Pribosyl_synth; 1.
DR   Pfam; PF13793; Pribosyltran_N; 1.
DR   SUPFAM; SSF53271; SSF53271; 1.
DR   TIGRFAMs; TIGR01251; ribP_PPkin; 1.
DR   PROSITE; PS00114; PRPP_SYNTHASE; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Kinase; Magnesium; Metal-binding;
KW   Nucleotide biosynthesis; Nucleotide-binding; Reference proteome;
KW   Transferase.
FT   CHAIN           1..340
FT                   /note="Ribose-phosphate pyrophosphokinase"
FT                   /id="PRO_0000141111"
FT   ACT_SITE        206
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00583"
FT   BINDING         47..49
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00583"
FT   BINDING         106..107
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00583"
FT   BINDING         140
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00583"
FT   BINDING         182
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00583"
FT   BINDING         208
FT                   /ligand="D-ribose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:78346"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00583"
FT   BINDING         234
FT                   /ligand="D-ribose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:78346"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00583"
FT   BINDING         238..242
FT                   /ligand="D-ribose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:78346"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00583"
SQ   SEQUENCE   340 AA;  36863 MW;  93A682F022A8A300 CRC64;
     MVSAILEGKP DKNLILVTGR IHPKLAEDVA EQLGIDVLET TAYDFANGEM YVRYTESVRG
     ADVFVLQSHY KPINKAIMEQ LIMIDALKRA SARSITAVCP LLGYSRQDKK HRGREPISCR
     LVFDLLKTAG ADRIMSVDLH AAQSQGFFDG PVDHLVAMPV LVDYIRDRFQ GHLDNVAVVS
     PDAGRIRVAE QWAQRLGGGP LAFVHKTRDI TRPNQAVANR VVGDVAGKDC VLVDDLIDTA
     GTIAGACHVL QDAGAKSVTV VATHGVLSGP AVERLKNCGA REVVLTDTVP IPEEKRWDGL
     TVLSIAPLLA SAIRAVFEDG SVAELFDTYP EHHGQGFLFA
 
 
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