(data stored in SCRATCH zone)

SWISSPROT: Q2IM69_ANADE

ID   Q2IM69_ANADE            Unreviewed;       321 AA.
AC   Q2IM69;
DT   07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   07-MAR-2006, sequence version 1.
DT   08-MAY-2019, entry version 101.
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 {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=Adeh_0121 {ECO:0000313|EMBL:ABC79898.1};
OS   Anaeromyxobacter dehalogenans (strain 2CP-C).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
OX   NCBI_TaxID=290397 {ECO:0000313|EMBL:ABC79898.1, ECO:0000313|Proteomes:UP000001935};
RN   [1] {ECO:0000313|EMBL:ABC79898.1, ECO:0000313|Proteomes:UP000001935}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2CP-C {ECO:0000313|EMBL:ABC79898.1,
RC   ECO:0000313|Proteomes:UP000001935};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C.,
RA   Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S.,
RA   Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P.;
RT   "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C.";
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000001935}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2CP-C {ECO:0000313|Proteomes:UP000001935};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C.,
RA   Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S.,
RA   Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P.;
RT   "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C.";
RL   Submitted (JAN-2006) 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
CC       (Rib-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,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:58017,
CC         ChEBI:CHEBI:78346, ChEBI:CHEBI:456215; EC=2.7.6.1;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00583,
CC         ECO:0000256|SAAS:SAAS01115190};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         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-
CC       ribose 1-diphosphate biosynthesis; 5-phospho-alpha-D-ribose 1-
CC       diphosphate from D-ribose 5-phosphate (route I): step 1/1.
CC       {ECO:0000256|HAMAP-Rule:MF_00583, ECO:0000256|SAAS:SAAS00956751}.
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
CC       family. Class I subfamily. {ECO:0000256|HAMAP-Rule:MF_00583}.
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DR   EMBL; CP000251; ABC79898.1; -; Genomic_DNA.
DR   RefSeq; WP_011419181.1; NC_007760.1.
DR   STRING; 290397.Adeh_0121; -.
DR   EnsemblBacteria; ABC79898; ABC79898; Adeh_0121.
DR   KEGG; ade:Adeh_0121; -.
DR   eggNOG; ENOG4105C5T; Bacteria.
DR   eggNOG; COG0462; LUCA.
DR   HOGENOM; HOG000210449; -.
DR   KO; K00948; -.
DR   OMA; FGWARQD; -.
DR   BioCyc; ADEH290397:G1G5W-125-MONOMER; -.
DR   UniPathway; UPA00087; UER00172.
DR   Proteomes; UP000001935; 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:0009116; P:nucleoside metabolic process; IEA:InterPro.
DR   GO; GO:0009165; P:nucleotide biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009156; P:ribonucleoside monophosphate biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd06223; PRTases_typeI; 1.
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;
DR   PRODOM; Q2IM69.
DR   SWISS-2DPAGE; Q2IM69.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00583,
KW   ECO:0000256|SAAS:SAAS00956731};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001935};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00583};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00583,
KW   ECO:0000256|SAAS:SAAS00956744, ECO:0000313|EMBL:ABC79898.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00583,
KW   ECO:0000256|SAAS:SAAS00956743};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00583,
KW   ECO:0000256|SAAS:SAAS00956748};
KW   Nucleotide biosynthesis {ECO:0000256|HAMAP-Rule:MF_00583,
KW   ECO:0000256|SAAS:SAAS00956760};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00583,
KW   ECO:0000256|SAAS:SAAS00956754};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001935};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00583,
KW   ECO:0000256|SAAS:SAAS00956753, ECO:0000313|EMBL:ABC79898.1}.
FT   DOMAIN       11    126       Pribosyltran_N. {ECO:0000259|Pfam:
FT                                PF13793}.
FT   NP_BIND      43     45       ATP. {ECO:0000256|HAMAP-Rule:MF_00583}.
FT   NP_BIND     102    103       ATP. {ECO:0000256|HAMAP-Rule:MF_00583}.
FT   REGION      231    235       Ribose-5-phosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00583}.
FT   ACT_SITE    201    201       {ECO:0000256|HAMAP-Rule:MF_00583}.
FT   METAL       136    136       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00583}.
FT   METAL       178    178       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00583}.
FT   BINDING     203    203       Ribose-5-phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00583}.
FT   BINDING     227    227       Ribose-5-phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00583}.
SQ   SEQUENCE   321 AA;  34372 MW;  374965F4F39DE539 CRC64;
     MASNGHYPDY RVFCGNANRP LAEAIAKELG RPLARATVGR FSDGEIQVEI GENVRGLDTF
     IIQSTSPDAN TNLMELLIMI DALKRASAGS INAVLPYYGY ARQDRKVAPR VPITAKLIAD
     LIEAAGATRV VSMDMHAGQI QGFFNVPFDH LYAAPVLLEH MRKRFDGLTQ DLVIVSPDAG
     GVERARAYSK RLGAGLGIVD KRRTKPNVAE IMNVIGDVNG KVAVLLDDMI DTAGTLTQAA
     NALVDKGATR VFAYATHAVL SGPAVDRIMK SPIEEVVVTD SIQLAPPAAS CPKIRTLSVA
     GLLAEAIRRI HSADSLSSLF V
//

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