PUR6_DROME
ID PUR6_DROME Reviewed; 429 AA.
AC Q9I7S8; Q9TVK1;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Bifunctional phosphoribosylaminoimidazole carboxylase/phosphoribosylaminoimidazole succinocarboxamide synthetase {ECO:0000305|PubMed:10757766};
DE Short=PAICS {ECO:0000250|UniProtKB:P22234};
DE AltName: Full=Protein adenosine-5 {ECO:0000303|PubMed:10757766};
DE Includes:
DE RecName: Full=Phosphoribosylaminoimidazole-succinocarboxamide synthase {ECO:0000305|PubMed:10757766};
DE EC=6.3.2.6 {ECO:0000269|PubMed:10757766};
DE AltName: Full=SAICAR synthetase {ECO:0000303|PubMed:10757766};
DE Includes:
DE RecName: Full=Phosphoribosylaminoimidazole carboxylase {ECO:0000305|PubMed:10757766};
DE EC=4.1.1.21 {ECO:0000269|PubMed:10757766};
DE AltName: Full=AIR carboxylase {ECO:0000303|PubMed:10757766};
DE Short=AIRC {ECO:0000303|PubMed:10757766};
GN Name=Paics {ECO:0000312|FlyBase:FBgn0020513};
GN Synonyms=ade5 {ECO:0000303|PubMed:10757766};
GN ORFNames=CG3989 {ECO:0000312|FlyBase:FBgn0020513};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1] {ECO:0000312|EMBL:AAF06356.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=Canton-S {ECO:0000312|EMBL:AAF06356.1};
RX PubMed=10757766; DOI=10.1093/genetics/154.3.1239;
RA O'Donnell A.F., Tiong S., Nash D., Clark D.V.;
RT "The Drosophila melanogaster ade5 gene encodes a bifunctional enzyme for
RT two steps in the de novo purine synthesis pathway.";
RL Genetics 154:1239-1253(2000).
RN [2] {ECO:0000312|EMBL:AAG22346.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAG22346.2};
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAG22346.2}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4] {ECO:0000305, ECO:0000312|EMBL:AAM12252.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAM12252.1};
RC TISSUE=Head {ECO:0000269|PubMed:12537569};
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
CC -!- FUNCTION: Bifunctional phosphoribosylaminoimidazole carboxylase and
CC phosphoribosylaminoimidazole succinocarboxamide synthetase catalyzing
CC two reactions of the de novo purine biosynthetic pathway.
CC {ECO:0000269|PubMed:10757766}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + ATP +
CC L-aspartate = (2S)-2-[5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-
CC 4-carboxamido]succinate + ADP + 2 H(+) + phosphate;
CC Xref=Rhea:RHEA:22628, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58443,
CC ChEBI:CHEBI:77657, ChEBI:CHEBI:456216; EC=6.3.2.6;
CC Evidence={ECO:0000269|PubMed:10757766};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22629;
CC Evidence={ECO:0000305|PubMed:10757766};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + H(+)
CC = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + CO2;
CC Xref=Rhea:RHEA:10792, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:77657, ChEBI:CHEBI:137981; EC=4.1.1.21;
CC Evidence={ECO:0000269|PubMed:10757766};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:10794;
CC Evidence={ECO:0000305|PubMed:10757766};
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5-
CC amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-
CC phospho-D-ribosyl)imidazole-4-carboxylate: step 1/2.
CC {ECO:0000250|UniProtKB:P22234}.
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5-
CC amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate from 5-amino-1-(5-
CC phospho-D-ribosyl)imidazole (carboxylase route): step 1/1.
CC {ECO:0000250|UniProtKB:P22234}.
CC -!- SUBUNIT: Homooctamer. {ECO:0000250|UniProtKB:P22234}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the SAICAR synthetase
CC family. {ECO:0000255}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the AIR carboxylase
CC family. Class II subfamily. {ECO:0000255}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF102579; AAF06355.1; -; mRNA.
DR EMBL; AF102580; AAF06356.1; -; Genomic_DNA.
DR EMBL; AE014298; AAG22346.2; -; Genomic_DNA.
DR EMBL; AY095520; AAM12252.1; -; mRNA.
DR RefSeq; NP_572826.1; NM_132598.4.
DR AlphaFoldDB; Q9I7S8; -.
DR SMR; Q9I7S8; -.
DR BioGRID; 58620; 6.
DR IntAct; Q9I7S8; 6.
DR STRING; 7227.FBpp0073538; -.
DR PaxDb; Q9I7S8; -.
DR PRIDE; Q9I7S8; -.
DR DNASU; 32228; -.
DR EnsemblMetazoa; FBtr0073705; FBpp0073538; FBgn0020513.
DR GeneID; 32228; -.
DR KEGG; dme:Dmel_CG3989; -.
DR CTD; 10606; -.
DR FlyBase; FBgn0020513; Paics.
DR VEuPathDB; VectorBase:FBgn0020513; -.
DR eggNOG; KOG2835; Eukaryota.
DR GeneTree; ENSGT00390000010172; -.
DR HOGENOM; CLU_061495_1_0_1; -.
DR InParanoid; Q9I7S8; -.
DR PhylomeDB; Q9I7S8; -.
DR BRENDA; 6.3.2.6; 1994.
DR Reactome; R-DME-73817; Purine ribonucleoside monophosphate biosynthesis.
DR UniPathway; UPA00074; UER00130.
DR UniPathway; UPA00074; UER00131.
DR BioGRID-ORCS; 32228; 0 hits in 3 CRISPR screens.
DR ChiTaRS; ade5; fly.
DR GenomeRNAi; 32228; -.
DR PRO; PR:Q9I7S8; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0020513; Expressed in capitellum (Drosophila) and 44 other tissues.
DR ExpressionAtlas; Q9I7S8; baseline and differential.
DR Genevisible; Q9I7S8; DM.
DR GO; GO:0005737; C:cytoplasm; ISS:FlyBase.
DR GO; GO:0005829; C:cytosol; HDA:FlyBase.
DR GO; GO:0043727; F:5-amino-4-imidazole carboxylate lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004638; F:phosphoribosylaminoimidazole carboxylase activity; ISS:FlyBase.
DR GO; GO:0004639; F:phosphoribosylaminoimidazolesuccinocarboxamide synthase activity; IGI:FlyBase.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IMP:FlyBase.
DR HAMAP; MF_02045; PurE_classII; 1.
DR HAMAP; MF_00137; SAICAR_synth; 1.
DR InterPro; IPR033626; PurE_classII.
DR InterPro; IPR000031; PurE_dom.
DR InterPro; IPR028923; SAICAR_synt/ADE2_N.
DR InterPro; IPR018236; SAICAR_synthetase_CS.
DR Pfam; PF00731; AIRC; 1.
DR Pfam; PF01259; SAICAR_synt; 1.
DR SMART; SM01001; AIRC; 1.
DR TIGRFAMs; TIGR01162; purE; 1.
DR PROSITE; PS01057; SAICAR_SYNTHETASE_1; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Decarboxylase; Ligase; Lyase; Multifunctional enzyme;
KW Nucleotide-binding; Purine biosynthesis; Reference proteome.
FT CHAIN 1..429
FT /note="Bifunctional phosphoribosylaminoimidazole
FT carboxylase/phosphoribosylaminoimidazole succinocarboxamide
FT synthetase"
FT /id="PRO_0000075035"
FT REGION 7..264
FT /note="SAICAR synthetase"
FT /evidence="ECO:0000255"
FT REGION 7..264
FT /note="SAICAR synthetase domain"
FT /evidence="ECO:0000250|UniProtKB:P22234"
FT REGION 265..429
FT /note="AIR carboxylase"
FT /evidence="ECO:0000255"
FT REGION 270..429
FT /note="AIR carboxylase domain"
FT /evidence="ECO:0000250|UniProtKB:P22234"
FT BINDING 335
FT /ligand="CO2"
FT /ligand_id="ChEBI:CHEBI:16526"
FT /evidence="ECO:0000250|UniProtKB:P22234"
SQ SEQUENCE 429 AA; 47281 MW; CF490A1D20CA2C7F CRC64;
MSTTTTASIE GYKLGKVIIE GKTKQVYDLP EQPGLCLLLS KDRITAGDGV KAHDLAGKAE
ISNTTNGQVF RLLNEAGIRT AYVKQCGAKA FIARKCQMIP IEWVTRRLAT GSFLKRNVGV
PEGYRFSPPK QETFFKDDAN HDPQWSEEQI VSAKFELNGL VIGQDEVDIM RRTTLLVFEI
LERAWQTKNC ALIDMKVEFG ICDDGNIVLA DIIDSDSWRL WPAGDKRLMV DKQVYRNLAS
VTASDLDTVK RNFIWVAEQL ADIVPKKDHL VVILMGSASD ISHSEKIATS CRSLGLNVEL
RVSSAHKGPE ETLRIVREYE SVMSNLIFVA VAGRSNGLGP VVSGSTNYPV INCPPVKSDN
MQVDVWSSLN LPSGLGCATV LYPEAAALHA ATILGLGNFM VWSKLRVKAL NNFITLKKAD
KELRGVRNA
