(data stored in SCRATCH zone)

SWISSPROT: D1CDD3_THET1

ID   D1CDD3_THET1            Unreviewed;       316 AA.
AC   D1CDD3;
DT   19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2010, sequence version 1.
DT   08-MAY-2019, entry version 64.
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=Tter_0016 {ECO:0000313|EMBL:ACZ40939.1};
OS   Thermobaculum terrenum (strain ATCC BAA-798 / YNP1).
OC   Bacteria; Thermobaculum.
OX   NCBI_TaxID=525904 {ECO:0000313|EMBL:ACZ40939.1, ECO:0000313|Proteomes:UP000000323};
RN   [1] {ECO:0000313|EMBL:ACZ40939.1, ECO:0000313|Proteomes:UP000000323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-798 / YNP1 {ECO:0000313|Proteomes:UP000000323};
RX   PubMed=21304745;
RA   Kiss H., Cleland D., Lapidus A., Lucas S., Del Rio T.G., Nolan M.,
RA   Tice H., Han C., Goodwin L., Pitluck S., Liolios K., Ivanova N.,
RA   Mavromatis K., Ovchinnikova G., Pati A., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Lu M., Brettin T.,
RA   Detter J.C., Goker M., Tindall B.J., Beck B., McDermott T.R.,
RA   Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P., Cheng J.F.;
RT   "Complete genome sequence of 'Thermobaculum terrenum' type strain
RT   (YNP1).";
RL   Stand. Genomic Sci. 3:153-162(2010).
RN   [2] {ECO:0000313|Proteomes:UP000000323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-798 / YNP1 {ECO:0000313|Proteomes:UP000000323};
RX   DOI=10.4056/sigs.1153107;
RA   Kiss H., Cleland D., Lapidus A., Lucas S., Glavina Del Rio T.,
RA   Nolan M., Tice H., Han C., Goodwin L., Pitluck S., Liolios K.,
RA   Ivanova N., Mavromatis K., Ovchinnikova G., Pati A., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y., Jeffries C., Lu M.,
RA   Brettin T., Detter J., Goker M., Tindall B., Beck B., McDermott T.,
RA   Woyke T., Bristow J., Eisen J., Markowitz V., Hugenholtz P.,
RA   Kyrpides N., Klenk H., Cheng J.;
RT   "Complete genome sequence of Thermobaculum terrenum type strain
RT   (YNP1T).";
RL   Stand. Genomic Sci. 3:153-162(2010).
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}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00583}.
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DR   EMBL; CP001825; ACZ40939.1; -; Genomic_DNA.
DR   RefSeq; WP_012873974.1; NC_013525.1.
DR   STRING; 525904.Tter_0016; -.
DR   EnsemblBacteria; ACZ40939; ACZ40939; Tter_0016.
DR   KEGG; ttr:Tter_0016; -.
DR   eggNOG; ENOG4105C5T; Bacteria.
DR   eggNOG; COG0462; LUCA.
DR   HOGENOM; HOG000210449; -.
DR   KO; K00948; -.
DR   OMA; FGWARQD; -.
DR   OrthoDB; 1011035at2; -.
DR   BioCyc; TTER525904:G1GGS-16-MONOMER; -.
DR   UniPathway; UPA00087; UER00172.
DR   Proteomes; UP000000323; Chromosome 1.
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; 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.
PE   3: Inferred from homology;
DR   PRODOM; D1CDD3.
DR   SWISS-2DPAGE; D1CDD3.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00583,
KW   ECO:0000256|SAAS:SAAS00956731};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000323};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00583};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00583,
KW   ECO:0000256|SAAS:SAAS00956744, ECO:0000313|EMBL:ACZ40939.1};
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:UP000000323};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00583,
KW   ECO:0000256|SAAS:SAAS00956753, ECO:0000313|EMBL:ACZ40939.1}.
FT   DOMAIN        4    120       Pribosyltran_N. {ECO:0000259|Pfam:
FT                                PF13793}.
FT   NP_BIND      37     39       ATP. {ECO:0000256|HAMAP-Rule:MF_00583}.
FT   ACT_SITE    192    192       {ECO:0000256|HAMAP-Rule:MF_00583}.
FT   METAL       130    130       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00583}.
FT   METAL       169    169       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00583}.
FT   BINDING     194    194       Ribose-5-phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00583}.
FT   BINDING     218    218       Ribose-5-phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00583}.
SQ   SEQUENCE   316 AA;  34390 MW;  E6E359912933C717 CRC64;
     MNRLRIFTGN ANRKLACDIA RNLDIEIGDA LVTTFKNGET RVRLEENVRG CDVFIIQSTS
     MPVDHHIMEL LLMIDAARRA SASRITAVIP YYGYAKQEKK TTGREPISAK LVANIIMQAG
     ADRVLAVDLH APAIEGFFDI PVDHLRAAPL LVDYYKRNPL PDAVVVSPDP GGVLRANDFR
     FRLGVPLAII AKQRPRPDTA EVLDMVGDVQ GKNAIIVDDL IGTGGTLAKA ADMLLSRGAK
     SVHAVATHAA FVGSPAAEEV KKILEGNTIE KIVVTDTIYI PPEEVDSKIE IVSVASLLAE
     AIMRIHKDLS VSELFR
//

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