(data stored in ACNUC7421 zone)

SWISSPROT: C7QHI5_CATAD

ID   C7QHI5_CATAD            Unreviewed;       326 AA.
AC   C7QHI5;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   30-AUG-2017, entry version 60.
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=PRPP synthase {ECO:0000256|HAMAP-Rule:MF_00583};
DE            Short=PRPPase {ECO:0000256|HAMAP-Rule:MF_00583};
DE            Short=p-Rib-PP synthase {ECO:0000256|HAMAP-Rule:MF_00583};
GN   Name=prs {ECO:0000256|HAMAP-Rule:MF_00583};
GN   OrderedLocusNames=Caci_0169 {ECO:0000313|EMBL:ACU69124.1};
OS   Catenulispora acidiphila (strain DSM 44928 / NRRL B-24433 / NBRC
OS   102108 / JCM 14897).
OC   Bacteria; Actinobacteria; Catenulisporales; Catenulisporaceae;
OC   Catenulispora.
OX   NCBI_TaxID=479433 {ECO:0000313|EMBL:ACU69124.1, ECO:0000313|Proteomes:UP000000851};
RN   [1] {ECO:0000313|EMBL:ACU69124.1, ECO:0000313|Proteomes:UP000000851}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44928 / NRRL B-24433 / NBRC 102108 / JCM 14897
RC   {ECO:0000313|Proteomes:UP000000851};
RX   PubMed=21304647;
RA   Copeland A., Lapidus A., Glavina Del Rio T., Nolan M., Lucas S.,
RA   Chen F., Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S.,
RA   Mikhailova N., Pati A., Ivanova N., Mavromatis K., Chen A.,
RA   Palaniappan K., Chain P., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Chertkov O., Brettin T., Detter J.C., Han C., Ali Z.,
RA   Tindall B.J., Goker M., Bristow J., Eisen J.A., Markowitz V.,
RA   Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Catenulispora acidiphila type strain (ID
RT   139908).";
RL   Stand. Genomic Sci. 1:119-125(2009).
CC   -!- FUNCTION: Involved in the biosynthesis of ribose 1,5-bisphosphate.
CC       Catalyzes the transfer of pyrophosphoryl group from ATP to ribose-
CC       5-phosphate to yield phosphoribosyl diphosphate (PRPP) and AMP.
CC       {ECO:0000256|HAMAP-Rule:MF_00583}.
CC   -!- CATALYTIC ACTIVITY: ATP + D-ribose 5-phosphate = AMP + 5-phospho-
CC       alpha-D-ribose 1-diphosphate. {ECO:0000256|HAMAP-Rule:MF_00583}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00583};
CC       Note=Binds 1 Mg(2+) ion 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}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00583}.
CC   -!- SIMILARITY: Belongs to the ribose-phosphate pyrophosphokinase
CC       family. {ECO:0000256|HAMAP-Rule:MF_00583}.
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DR   EMBL; CP001700; ACU69124.1; -; Genomic_DNA.
DR   RefSeq; WP_012784419.1; NC_013131.1.
DR   ProteinModelPortal; C7QHI5; -.
DR   STRING; 479433.Caci_0169; -.
DR   EnsemblBacteria; ACU69124; ACU69124; Caci_0169.
DR   KEGG; cai:Caci_0169; -.
DR   eggNOG; ENOG4105C5T; Bacteria.
DR   eggNOG; COG0462; LUCA.
DR   HOGENOM; HOG000210449; -.
DR   KO; K00948; -.
DR   OMA; FGWARQD; -.
DR   OrthoDB; POG091H018X; -.
DR   UniPathway; UPA00087; UER00172.
DR   Proteomes; UP000000851; 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-HAMAP.
DR   GO; GO:0004749; F:ribose phosphate diphosphokinase activity; IEA:UniProtKB-HAMAP.
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-HAMAP.
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   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; C7QHI5.
DR   SWISS-2DPAGE; C7QHI5.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00583};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000851};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00583};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00583, ECO:0000313|EMBL:ACU69124.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00583};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00583};
KW   Nucleotide biosynthesis {ECO:0000256|HAMAP-Rule:MF_00583};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00583};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000851};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00583,
KW   ECO:0000313|EMBL:ACU69124.1}.
FT   DOMAIN       12    128       Pribosyltran_N. {ECO:0000259|Pfam:
FT                                PF13793}.
FT   NP_BIND      45     47       ATP. {ECO:0000256|HAMAP-Rule:MF_00583}.
FT   NP_BIND     104    107       ATP. {ECO:0000256|HAMAP-Rule:MF_00583}.
FT   NP_BIND     151    152       ATP. {ECO:0000256|HAMAP-Rule:MF_00583}.
FT   REGION      201    203       Ribose-5-phosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00583}.
FT   REGION      230    237       Ribose-5-phosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00583}.
FT   REGION      316    318       Ribose-5-phosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00583}.
FT   METAL       136    136       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00583}.
FT   METAL       138    138       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00583}.
FT   METAL       147    147       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00583}.
FT   METAL       151    151       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00583}.
FT   BINDING     112    112       Ribose-5-phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00583}.
FT   BINDING     138    138       ATP. {ECO:0000256|HAMAP-Rule:MF_00583}.
FT   BINDING     143    143       ATP. {ECO:0000256|HAMAP-Rule:MF_00583}.
FT   BINDING     178    178       Ribose-5-phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00583}.
SQ   SEQUENCE   326 AA;  36071 MW;  94E2D8CE7008C785 CRC64;
     MTGLKTTGEK KLMLFTGRAY PELAQEVAEE LGVEIAPMKA HDFANGEIYT RFEESVRGSD
     AFVIQCHSAP INHSIMEQLI MVDALKRASS KRITVITPFY GYARQDKKHK GREPISARLM
     ADFFATAGAD RLMAVDLHTD QIQGYFDGPV DHLFALPVLV DYIKGKYDTS KLTVVSPDAG
     RVRTADRWTD RLNTPLAIVH KRRDPNIPNT VSVHEIVGEV KGRTCVLVDD MVDTAGTICA
     AAEALFENGA AEVIIAATHA VLSDPATDRL KNSRISEVIF TNTLPIPDEK RFDKMTVLSI
     APMLARAIRE VFEDGSVTSM FDDHKH
//

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