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Database: UniProt
Entry: A1RWZ6_THEPD
LinkDB: A1RWZ6_THEPD
Original site: A1RWZ6_THEPD 
ID   A1RWZ6_THEPD            Unreviewed;       276 AA.
AC   A1RWZ6;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   24-JAN-2024, entry version 90.
DE   RecName: Full=ribose-phosphate diphosphokinase {ECO:0000256|ARBA:ARBA00013247};
DE            EC=2.7.6.1 {ECO:0000256|ARBA:ARBA00013247};
GN   OrderedLocusNames=Tpen_0317 {ECO:0000313|EMBL:ABL77726.1};
OS   Thermofilum pendens (strain DSM 2475 / Hrk 5).
OC   Archaea; Thermoproteota; Thermoprotei; Thermofilales; Thermofilaceae;
OC   Thermofilum.
OX   NCBI_TaxID=368408 {ECO:0000313|EMBL:ABL77726.1, ECO:0000313|Proteomes:UP000000641};
RN   [1] {ECO:0000313|Proteomes:UP000000641}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2475 / Hrk 5 {ECO:0000313|Proteomes:UP000000641};
RX   PubMed=18263724; DOI=10.1128/JB.01949-07;
RA   Anderson I., Rodriguez J., Susanti D., Porat I., Reich C., Ulrich L.E.,
RA   Elkins J.G., Mavromatis K., Lykidis A., Kim E., Thompson L.S., Nolan M.,
RA   Land M., Copeland A., Lapidus A., Lucas S., Detter C., Zhulin I.B.,
RA   Olsen G.J., Whitman W., Mukhopadhyay B., Bristow J., Kyrpides N.;
RT   "Genome sequence of Thermofilum pendens reveals an exceptional loss of
RT   biosynthetic pathways without genome reduction.";
RL   J. Bacteriol. 190:2957-2965(2008).
CC   -!- SIMILARITY: Belongs to the ribose-phosphate pyrophosphokinase family.
CC       {ECO:0000256|RuleBase:RU004324}.
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DR   EMBL; CP000505; ABL77726.1; -; Genomic_DNA.
DR   AlphaFoldDB; A1RWZ6; -.
DR   STRING; 368408.Tpen_0317; -.
DR   EnsemblBacteria; ABL77726; ABL77726; Tpen_0317.
DR   KEGG; tpe:Tpen_0317; -.
DR   eggNOG; arCOG00067; Archaea.
DR   HOGENOM; CLU_033546_2_2_2; -.
DR   OMA; FGWARQD; -.
DR   Proteomes; UP000000641; Chromosome.
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   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   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022727,
KW   ECO:0000256|RuleBase:RU004324};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000641};
KW   Transferase {ECO:0000313|EMBL:ABL77726.1}.
FT   DOMAIN          5..97
FT                   /note="Ribose-phosphate pyrophosphokinase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13793"
FT   DOMAIN          137..243
FT                   /note="Phosphoribosyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00156"
SQ   SEQUENCE   276 AA;  29673 MW;  B5CC999F127B0D56 CRC64;
     MGDELVFVEK KVFPDGEIYV RVPSKPSGVA IVVSSTHPPQ ERRLLELLLT VEALSSYAQG
     SVIAVVPYLA YARQDKRFLE GEPISIKVVL KALEAAGASG LLAVDVHQPR VLSEWLSIPS
     KNVLPFEDIA GYLYGKVKNA VVLAPDMGAL ERARRVAELI GADFDYLVKE RDRVTGEVRV
     QPKSLEVNGR DVVIVDDIIS TGKTIALAAK SALAQGASSV TAVCTHAVMV QGALDLLYYS
     GVREVVATDT VPSPVSKISV APSVVRGLRE LLEDMI
//
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