ID A0A2A2JBY8_9BILA Unreviewed; 397 AA.
AC A0A2A2JBY8;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Ribose-phosphate pyrophosphokinase 2 {ECO:0000256|ARBA:ARBA00040333};
DE EC=2.7.6.1 {ECO:0000256|ARBA:ARBA00013247};
DE AltName: Full=Phosphoribosyl pyrophosphate synthase II {ECO:0000256|ARBA:ARBA00041814};
GN ORFNames=WR25_18424 {ECO:0000313|EMBL:PAV59290.1};
OS Diploscapter pachys.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Diploscapter.
OX NCBI_TaxID=2018661 {ECO:0000313|EMBL:PAV59290.1, ECO:0000313|Proteomes:UP000218231};
RN [1] {ECO:0000313|EMBL:PAV59290.1, ECO:0000313|Proteomes:UP000218231}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PF1309 {ECO:0000313|EMBL:PAV59290.1};
RA Fradin H., Zegar C., Gutwein M., Lucas J., Kovtun M., Corcoran D.,
RA Baugh L.R., Kiontke K., Gunsalus K., Fitch D.H., Piano F.;
RT "Genome architecture and evolution of a unichromosomal asexual nematode.";
RL Curr. Biol. 0:0-0(2017).
CC -!- FUNCTION: Catalyzes the synthesis of phosphoribosylpyrophosphate (PRPP)
CC that is essential for nucleotide synthesis.
CC {ECO:0000256|ARBA:ARBA00003018}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; 5-phospho-alpha-D-ribose
CC 1-diphosphate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate from
CC D-ribose 5-phosphate (route I): step 1/1.
CC {ECO:0000256|ARBA:ARBA00004996}.
CC -!- SUBUNIT: Homodimer. The active form is probably a hexamer composed of 3
CC homodimers. {ECO:0000256|ARBA:ARBA00026067}.
CC -!- SIMILARITY: Belongs to the ribose-phosphate pyrophosphokinase family.
CC {ECO:0000256|ARBA:ARBA00006478}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PAV59290.1}.
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DR EMBL; LIAE01010535; PAV59290.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A2JBY8; -.
DR STRING; 2018661.A0A2A2JBY8; -.
DR UniPathway; UPA00087; UER00172.
DR Proteomes; UP000218231; Unassembled WGS sequence.
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:InterPro.
DR GO; GO:0004749; F:ribose phosphate diphosphokinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006015; P:5-phosphoribose 1-diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009165; P:nucleotide biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0009156; P:ribonucleoside monophosphate biosynthetic process; IEA:InterPro.
DR CDD; cd06223; PRTases_typeI; 1.
DR Gene3D; 3.40.50.2020; -; 2.
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 NCBIfam; TIGR01251; ribP_PPkin; 1.
DR PANTHER; PTHR10210; RIBOSE-PHOSPHATE DIPHOSPHOKINASE FAMILY MEMBER; 1.
DR PANTHER; PTHR10210:SF110; RIBOSE-PHOSPHATE PYROPHOSPHOKINASE 2; 1.
DR Pfam; PF14572; Pribosyl_synth; 1.
DR Pfam; PF13793; Pribosyltran_N; 1.
DR SMART; SM01400; Pribosyltran_N; 1.
DR SUPFAM; SSF53271; PRTase-like; 1.
DR PROSITE; PS00114; PRPP_SYNTHASE; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022727};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW Reference proteome {ECO:0000313|Proteomes:UP000218231};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 82..198
FT /note="Ribose-phosphate pyrophosphokinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF13793"
FT REGION 36..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..56
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 397 AA; 43772 MW; F14D416B3262BE74 CRC64;
MLSGRVPFHR RQRRQGCVHT SEEIFRGSWD NLKEAEEQEN IATQRGNSDT ENSPSSNVVQ
VADSVVTSCP LKEQHPVRMP NIKVFSGSSH RDLTQRICER LQLEVSKASL KKFSNKETNV
EIGESVRGED VYIIQSGAGE INDNLMELLI MINACKIASS CRVAAVIPCF PYARQDKKDK
SRAPISAKLV ANMLSVAGAD HIITMDLHAS QIQGFFDIPV DNLYAEPAIL KYIKESIPNW
QTSVIVSPDA GGAKRVTSIA DRLNVDFALI HKERKRANEV EKMTLVGSVE GKVAILVDDM
ADTCGTICMA ADKLVEAGAE KVYAFCVHGI FSGPALQRLN NSKFEAVVVT NTIPQEENMK
ACPKIQCIDI SMILAEAIRR THNGESVSYL FSHVPIC
//
