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KPRS_LISWE
ID   KPRS_LISWE              Reviewed;         318 AA.
AC   Q83TK1;
DT   31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 91.
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};
OS   Listeria welshimeri.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=1643;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=FSLc2006, and FSLn1064;
RA   Cai S., Nielsen R., Roberts A.J., Wiedmann M.;
RT   "Molecular evolution of Listeria spp. and Listeria monocytogenes.";
RL   Submitted (JUL-2002) 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: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}.
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DR   EMBL; AY135441; AAN10329.1; -; Genomic_DNA.
DR   EMBL; AY135442; AAN10330.1; -; Genomic_DNA.
DR   RefSeq; WP_011701034.1; NZ_NYPG01000004.1.
DR   AlphaFoldDB; Q83TK1; -.
DR   SMR; Q83TK1; -.
DR   GeneID; 61188048; -.
DR   OMA; FGWARQD; -.
DR   UniPathway; UPA00087; UER00172.
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; Transferase.
FT   CHAIN           1..318
FT                   /note="Ribose-phosphate pyrophosphokinase"
FT                   /id="PRO_0000141159"
FT   ACT_SITE        199
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00583"
FT   BINDING         43..45
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00583"
FT   BINDING         102..103
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00583"
FT   BINDING         136
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00583"
FT   BINDING         176
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00583"
FT   BINDING         201
FT                   /ligand="D-ribose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:78346"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00583"
FT   BINDING         225
FT                   /ligand="D-ribose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:78346"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00583"
FT   BINDING         229..233
FT                   /ligand="D-ribose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:78346"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00583"
SQ   SEQUENCE   318 AA;  35095 MW;  CF64024B2CCE6329 CRC64;
     MSNEYFDPKL KIFSLNSNRE LAEEIAKEVG IELGKSSVTH FSDGEIQINI EESIRGCHVY
     VIQSTSNPVN QNLMELLIMI DALKRASAAT INIVMPYYGY ARQDRKARSR EPITAKLVAN
     LIETAGATRM ITLDMHAPQI QGFFDIPIDH LNAVRLLSNY FSERHLGDDL VVVSPDHGGV
     TRARKMADRL KAPIAIIDKR RPRPNVAEVM NIVGNVEGKV CIIIDDIIDT AGTITLAAKA
     LREAGATKVY ACCSHPVLSG PAMKRIEDSP IEKLIVTNSI ALPEEKWIDK MEQLSVAPLL
     GEAIVRVHEN ASVSSLFE
 
 
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