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Database: UniProt
Entry: A3MV85_PYRCJ
LinkDB: A3MV85_PYRCJ
Original site: A3MV85_PYRCJ 
ID   A3MV85_PYRCJ            Unreviewed;       297 AA.
AC   A3MV85;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   27-MAR-2024, entry version 81.
DE   RecName: Full=ribose-phosphate diphosphokinase {ECO:0000256|ARBA:ARBA00013247};
DE            EC=2.7.6.1 {ECO:0000256|ARBA:ARBA00013247};
GN   OrderedLocusNames=Pcal_1127 {ECO:0000313|EMBL:ABO08552.1};
OS   Pyrobaculum calidifontis (strain DSM 21063 / JCM 11548 / VA1).
OC   Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Pyrobaculum.
OX   NCBI_TaxID=410359 {ECO:0000313|EMBL:ABO08552.1, ECO:0000313|Proteomes:UP000001431};
RN   [1] {ECO:0000313|EMBL:ABO08552.1, ECO:0000313|Proteomes:UP000001431}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21063 / JCM 11548 / VA1
RC   {ECO:0000313|Proteomes:UP000001431};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Cozen A.E.,
RA   Fitz-Gibbon S.T., House C.H., Saltikov C., Lowe T.M., Richardson P.;
RT   "Complete sequence of Pyrobaculum calidifontis JCM 11548.";
RL   Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the ribose-phosphate pyrophosphokinase family.
CC       {ECO:0000256|RuleBase:RU004324}.
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DR   EMBL; CP000561; ABO08552.1; -; Genomic_DNA.
DR   AlphaFoldDB; A3MV85; -.
DR   SMR; A3MV85; -.
DR   STRING; 410359.Pcal_1127; -.
DR   KEGG; pcl:Pcal_1127; -.
DR   eggNOG; arCOG00067; Archaea.
DR   HOGENOM; CLU_033546_2_2_2; -.
DR   BRENDA; 2.7.6.1; 7282.
DR   Proteomes; UP000001431; Chromosome.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0004749; F:ribose phosphate diphosphokinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009165; P:nucleotide biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd06223; PRTases_typeI; 1.
DR   Gene3D; 3.40.50.2020; -; 2.
DR   InterPro; IPR029099; Pribosyltran_N.
DR   InterPro; IPR000836; PRibTrfase_dom.
DR   InterPro; IPR029057; PRTase-like.
DR   InterPro; IPR005946; Rib-P_diPkinase.
DR   NCBIfam; TIGR01251; ribP_PPkin; 1.
DR   PANTHER; PTHR10210:SF32; RIBOSE-PHOSPHATE DIPHOSPHOKINASE; 1.
DR   PANTHER; PTHR10210; RIBOSE-PHOSPHATE DIPHOSPHOKINASE FAMILY MEMBER; 1.
DR   Pfam; PF00156; Pribosyltran; 1.
DR   Pfam; PF13793; Pribosyltran_N; 1.
DR   SMART; SM01400; Pribosyltran_N; 1.
DR   SUPFAM; SSF53271; PRTase-like; 1.
PE   3: Inferred from homology;
KW   Kinase {ECO:0000313|EMBL:ABO08552.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022727,
KW   ECO:0000256|RuleBase:RU004324}; Transferase {ECO:0000313|EMBL:ABO08552.1}.
FT   DOMAIN          33..122
FT                   /note="Ribose-phosphate pyrophosphokinase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13793"
FT   DOMAIN          164..265
FT                   /note="Phosphoribosyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00156"
SQ   SEQUENCE   297 AA;  32741 MW;  C8E32EA56215038A CRC64;
     MDKINSRALY TPMHILTFQN ALDIAEHFEG LGKVVQVEER TFPDGEVLVR VPEAGPVVVL
     VARLYPGVND SVFKLFLALD ALNDMGVGRV VVVAPYLPYA RQDRRFRPGE PISAKALLKT
     LANLSVGALV AVDLHKPYIA DYVPRVAVRN VYPAEEFAER LKGVDAVVSP DFGSLHRAEA
     VARILGVPYT YFEKYRDRET GAITLMPRRD LELRGARVAI VDDILSTGGT LVDACKAART
     LGASEVYAAV THCQLLKDAR EKAKSCVDRL ICTDSILNEF AEVKVGPLLR REVEKLL
//
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