ID W5J2J7_ANODA Unreviewed; 421 AA.
AC W5J2J7;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 48.
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=AND_010458 {ECO:0000313|EMBL:ETN57966.1};
OS Anopheles darlingi (Mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=43151 {ECO:0000313|EMBL:ETN57966.1};
RN [1] {ECO:0000313|EMBL:ETN57966.1, ECO:0000313|Proteomes:UP000000673}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=20920257; DOI=10.1186/1471-2164-11-529;
RA Mendes N.D., Freitas A.T., Vasconcelos A.T., Sagot M.F.;
RT "Combination of measures distinguishes pre-miRNAs from other stem-loops in
RT the genome of the newly sequenced Anopheles darlingi.";
RL BMC Genomics 11:529-529(2010).
RN [2] {ECO:0000313|EMBL:ETN57966.1}
RP NUCLEOTIDE SEQUENCE.
RA Almeida L.G., Nicolas M.F., Souza R.C., Vasconcelos A.T.R.;
RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:ETN57966.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=23761445;
RA Marinotti O., Cerqueira G.C., de Almeida L.G., Ferro M.I., Loreto E.L.,
RA Zaha A., Teixeira S.M., Wespiser A.R., Almeida E Silva A.,
RA Schlindwein A.D., Pacheco A.C., Silva A.L., Graveley B.R., Walenz B.P.,
RA Lima Bde A., Ribeiro C.A., Nunes-Silva C.G., de Carvalho C.R., Soares C.M.,
RA de Menezes C.B., Matiolli C., Caffrey D., Araujo D.A., de Oliveira D.M.,
RA Golenbock D., Grisard E.C., Fantinatti-Garboggini F., de Carvalho F.M.,
RA Barcellos F.G., Prosdocimi F., May G., Azevedo Junior G.M., Guimaraes G.M.,
RA Goldman G.H., Padilha I.Q., Batista Jda S., Ferro J.A., Ribeiro J.M.,
RA Fietto J.L., Dabbas K.M., Cerdeira L., Agnez-Lima L.F., Brocchi M.,
RA de Carvalho M.O., Teixeira Mde M., Diniz Maia Mde M., Goldman M.H.,
RA Cruz Schneider M.P., Felipe M.S., Hungria M., Nicolas M.F., Pereira M.,
RA Montes M.A., Cantao M.E., Vincentz M., Rafael M.S., Silverman N.,
RA Stoco P.H., Souza R.C., Vicentini R., Gazzinelli R.T., Neves Rde O.,
RA Silva R., Astolfi-Filho S., Maciel T.E., Urmenyi T.P., Tadei W.P.,
RA Camargo E.P., de Vasconcelos A.T.;
RT "The genome of Anopheles darlingi, the main neotropical malaria vector.";
RL Nucleic Acids Res. 41:7387-7400(2013).
RN [4] {ECO:0000313|EnsemblMetazoa:ADAC010458-PA}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (JUN-2015) to UniProtKB.
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}.
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DR EMBL; ADMH02002184; ETN57966.1; -; Genomic_DNA.
DR AlphaFoldDB; W5J2J7; -.
DR STRING; 43151.W5J2J7; -.
DR EnsemblMetazoa; ADAC010458-RA; ADAC010458-PA; ADAC010458.
DR VEuPathDB; VectorBase:ADAC010458; -.
DR VEuPathDB; VectorBase:ADAR2_011218; -.
DR eggNOG; KOG1448; Eukaryota.
DR HOGENOM; CLU_033546_5_0_1; -.
DR OMA; DNLWTEP; -.
DR OrthoDB; 276387at2759; -.
DR UniPathway; UPA00087; UER00172.
DR Proteomes; UP000000673; 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, ECO:0000313|EMBL:ETN57966.1};
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:UP000000673};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 107..223
FT /note="Ribose-phosphate pyrophosphokinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF13793"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 81..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 421 AA; 45063 MW; 0DF2BAC578EC0B15 CRC64;
MPVRSSHPIP ARTTSTTAAR SSSSRSSSGS LETNETSVIS HPSSCASNLV CCGTQSQPDH
SIASSAKSGI NTETAAAAAA ATIRTDSSTD ELVSTDPRPL QSRMPNIKVF SGSSHPDLAS
RIVDRLGIDL GKVVTKKFSN LETCVEIGES VRGEDVYIVQ SGSGEINDNL MELLIMINAC
KIASASRVTA VIPCFPYARQ DKKDKSRAPI SAKLVANMLS VAGADHIITM DLHASQIQGF
FDIPVDNLYA EPAVLKWIRE NIAEWRNSII VSPDAGGAKR VTSIADRLNV EFALIHKERK
KANEVASMVL VGDVKDRVAI LVDDMADTCG TICHAADKLV EAGATKVYAI LTHGIFSGPA
ISRINDACFE AVVVTNTIPQ DGHMKDCPKI QCIDVSMMFA EAVRRTHNGE SVSYLFSNVP
Y
//
