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Database: UniProt
Entry: A0A182QBZ0_9DIPT
LinkDB: A0A182QBZ0_9DIPT
Original site: A0A182QBZ0_9DIPT 
ID   A0A182QBZ0_9DIPT        Unreviewed;       448 AA.
AC   A0A182QBZ0;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   RecName: Full=ribose-phosphate diphosphokinase {ECO:0000256|ARBA:ARBA00013247};
DE            EC=2.7.6.1 {ECO:0000256|ARBA:ARBA00013247};
OS   Anopheles farauti.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=69004 {ECO:0000313|EnsemblMetazoa:AFAF007128-PA, ECO:0000313|Proteomes:UP000075886};
RN   [1] {ECO:0000313|Proteomes:UP000075886}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FAR1 {ECO:0000313|Proteomes:UP000075886};
RG   The Broad Institute Genomics Platform;
RA   Neafsey D.E., Besansky N., Howell P., Walton C., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Anopheles farauti FAR1 (V2).";
RL   Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:AFAF007128-PA}
RP   IDENTIFICATION.
RC   STRAIN=FAR1 {ECO:0000313|EnsemblMetazoa:AFAF007128-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) to UniProtKB.
CC   -!- FUNCTION: Catalyzes the synthesis of phosphoribosylpyrophosphate (PRPP)
CC       that is essential for nucleotide synthesis.
CC       {ECO:0000256|ARBA:ARBA00003018}.
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}.
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DR   EMBL; AXCN02001913; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; A0A182QBZ0; -.
DR   STRING; 69004.A0A182QBZ0; -.
DR   EnsemblMetazoa; AFAF007128-RA; AFAF007128-PA; AFAF007128.
DR   VEuPathDB; VectorBase:AFAF007128; -.
DR   OrthoDB; 276387at2759; -.
DR   UniPathway; UPA00087; UER00172.
DR   Proteomes; UP000075886; 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:SF36; RIBOSE-PHOSPHATE DIPHOSPHOKINASE; 1.
DR   PANTHER; PTHR10210; RIBOSE-PHOSPHATE DIPHOSPHOKINASE FAMILY MEMBER; 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   Transferase {ECO:0000256|ARBA:ARBA00022777}.
FT   DOMAIN          134..250
FT                   /note="Ribose-phosphate pyrophosphokinase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13793"
FT   REGION          15..39
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          85..121
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        85..116
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   448 AA;  48243 MW;  08520D84D60A2F69 CRC64;
     LSSLRASADR AQILSKANNM GRKGAKHSTT DPEDCVMPVR SSNPIRARTL VRSNLEKASV
     ISNACSTSQA SRGNLVHSLP SAVHNIRSSS DSSTTVDSSS SSSSGSSDSK HPTDSISVPS
     VDPHRLLQSR MPNIKVFSGS SHPDLASRIV DRLGIDLGKV VTKKFSNLET CVEIGESVRG
     EDVYIVQSGS GEINDNLMEL LIMINACKIA SASRVTAVIP CFPYARQDKK DKSRAPISAK
     LVANMLSVAG ADHIITMDLH ASQIQGFFDI PVDNLYAEPA VLKWIRENIA EWRNSIIVSP
     DAGGAKRVTS IADRLNVEFA LIHKERKKAN EVASMVLVGD VKDRVAILVD DMADTCGTIC
     HAADKLVEAG ATKVYAILTH GIFSGPAISR INNACFEAVV VTNTIPQDGH MKDCPKIQCI
     DVSMMFAEAV RRTHNGESVS YLFSNVPY
//
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