PUR6_MOUSE
ID PUR6_MOUSE Reviewed; 425 AA.
AC Q9DCL9; Q9CQ38;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 4.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Bifunctional phosphoribosylaminoimidazole carboxylase/phosphoribosylaminoimidazole succinocarboxamide synthetase {ECO:0000250|UniProtKB:P22234};
DE Short=PAICS {ECO:0000250|UniProtKB:P22234};
DE Includes:
DE RecName: Full=Phosphoribosylaminoimidazole carboxylase {ECO:0000250|UniProtKB:P22234};
DE EC=4.1.1.21 {ECO:0000250|UniProtKB:P22234};
DE AltName: Full=AIR carboxylase {ECO:0000250|UniProtKB:P22234};
DE Short=AIRC {ECO:0000250|UniProtKB:P22234};
DE Includes:
DE RecName: Full=Phosphoribosylaminoimidazole succinocarboxamide synthetase {ECO:0000250|UniProtKB:P22234};
DE EC=6.3.2.6 {ECO:0000250|UniProtKB:P22234};
DE AltName: Full=SAICAR synthetase {ECO:0000250|UniProtKB:P22234};
GN Name=Paics {ECO:0000312|MGI:MGI:1914304};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Heart, Kidney, and Mammary gland;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and Czech II; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-22, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-36, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Bifunctional phosphoribosylaminoimidazole carboxylase and
CC phosphoribosylaminoimidazole succinocarboxamide synthetase catalyzing
CC two reactions of the de novo purine biosynthetic pathway.
CC {ECO:0000250|UniProtKB:P22234}.
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:0000250|UniProtKB:P22234};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22629;
CC Evidence={ECO:0000250|UniProtKB:P22234};
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:0000250|UniProtKB:P22234};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:10794;
CC Evidence={ECO:0000250|UniProtKB:P22234};
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:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the AIR carboxylase
CC family. Class II subfamily. {ECO:0000305}.
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DR EMBL; AK002669; BAB22273.1; -; mRNA.
DR EMBL; AK010462; BAB26957.1; -; mRNA.
DR EMBL; AK012118; BAB28044.1; -; mRNA.
DR EMBL; AK146722; BAE27385.1; -; mRNA.
DR EMBL; AK159398; BAE35051.1; -; mRNA.
DR EMBL; AK166264; BAE38669.1; -; mRNA.
DR EMBL; CH466524; EDL37918.1; -; Genomic_DNA.
DR EMBL; BC018153; AAH18153.1; -; mRNA.
DR EMBL; BC052691; AAH52691.1; -; mRNA.
DR CCDS; CCDS19367.1; -.
DR RefSeq; NP_080215.1; NM_025939.2.
DR RefSeq; XP_006535243.1; XM_006535180.2.
DR RefSeq; XP_006535244.1; XM_006535181.3.
DR RefSeq; XP_006535245.1; XM_006535182.3.
DR RefSeq; XP_006535246.1; XM_006535183.3.
DR AlphaFoldDB; Q9DCL9; -.
DR SMR; Q9DCL9; -.
DR BioGRID; 211906; 26.
DR IntAct; Q9DCL9; 3.
DR STRING; 10090.ENSMUSP00000031160; -.
DR iPTMnet; Q9DCL9; -.
DR PhosphoSitePlus; Q9DCL9; -.
DR SwissPalm; Q9DCL9; -.
DR CPTAC; non-CPTAC-3741; -.
DR EPD; Q9DCL9; -.
DR jPOST; Q9DCL9; -.
DR MaxQB; Q9DCL9; -.
DR PaxDb; Q9DCL9; -.
DR PeptideAtlas; Q9DCL9; -.
DR PRIDE; Q9DCL9; -.
DR ProteomicsDB; 302032; -.
DR Antibodypedia; 24027; 347 antibodies from 31 providers.
DR DNASU; 67054; -.
DR Ensembl; ENSMUST00000031160; ENSMUSP00000031160; ENSMUSG00000029247.
DR Ensembl; ENSMUST00000117536; ENSMUSP00000112879; ENSMUSG00000029247.
DR Ensembl; ENSMUST00000120912; ENSMUSP00000113483; ENSMUSG00000029247.
DR GeneID; 67054; -.
DR KEGG; mmu:67054; -.
DR UCSC; uc008xvn.2; mouse.
DR CTD; 10606; -.
DR MGI; MGI:1914304; Paics.
DR VEuPathDB; HostDB:ENSMUSG00000029247; -.
DR eggNOG; KOG2835; Eukaryota.
DR GeneTree; ENSGT00390000010172; -.
DR HOGENOM; CLU_061495_1_0_1; -.
DR InParanoid; Q9DCL9; -.
DR OMA; WSDEQII; -.
DR OrthoDB; 566769at2759; -.
DR PhylomeDB; Q9DCL9; -.
DR TreeFam; TF106384; -.
DR Reactome; R-MMU-73817; Purine ribonucleoside monophosphate biosynthesis.
DR UniPathway; UPA00074; UER00130.
DR UniPathway; UPA00074; UER00131.
DR BioGRID-ORCS; 67054; 25 hits in 77 CRISPR screens.
DR ChiTaRS; Paics; mouse.
DR PRO; PR:Q9DCL9; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9DCL9; protein.
DR Bgee; ENSMUSG00000029247; Expressed in gonadal ridge and 265 other tissues.
DR ExpressionAtlas; Q9DCL9; baseline and differential.
DR Genevisible; Q9DCL9; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0004638; F:phosphoribosylaminoimidazole carboxylase activity; ISS:UniProtKB.
DR GO; GO:0004639; F:phosphoribosylaminoimidazolesuccinocarboxamide synthase activity; ISS:UniProtKB.
DR GO; GO:0044208; P:'de novo' AMP biosynthetic process; ISO:MGI.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; ISO:MGI.
DR GO; GO:0097294; P:'de novo' XMP biosynthetic process; ISO:MGI.
DR GO; GO:0006177; P:GMP biosynthetic process; ISO:MGI.
DR GO; GO:0009113; P:purine nucleobase biosynthetic process; ISS:UniProtKB.
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 PROSITE; PS01057; SAICAR_SYNTHETASE_1; 1.
DR PROSITE; PS01058; SAICAR_SYNTHETASE_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Decarboxylase; Ligase; Lyase;
KW Multifunctional enzyme; Nucleotide-binding; Phosphoprotein;
KW Purine biosynthesis; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P22234"
FT CHAIN 2..425
FT /note="Bifunctional phosphoribosylaminoimidazole
FT carboxylase/phosphoribosylaminoimidazole succinocarboxamide
FT synthetase"
FT /id="PRO_0000075031"
FT REGION 2..260
FT /note="SAICAR synthetase domain"
FT /evidence="ECO:0000250|UniProtKB:P22234"
FT REGION 261..266
FT /note="Linker"
FT /evidence="ECO:0000250|UniProtKB:P22234"
FT REGION 267..425
FT /note="AIR carboxylase domain"
FT /evidence="ECO:0000250|UniProtKB:P22234"
FT BINDING 332
FT /ligand="CO2"
FT /ligand_id="ChEBI:CHEBI:16526"
FT /evidence="ECO:0000250|UniProtKB:P22234"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P22234"
FT MOD_RES 22
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:19131326"
FT MOD_RES 36
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 107
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P22234"
FT MOD_RES 238
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P22234"
FT MOD_RES 247
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P22234"
FT MOD_RES 274
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P22234"
FT CONFLICT 5
FT /note="V -> Y (in Ref. 1; BAB22273)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 425 AA; 47006 MW; CD2A4323EC02B218 CRC64;
MATAVVVNIG KKLYEGKTKE VYELLDTPGR VLLQSKDQIT AGNAARKNHL EGKAAISNKI
TSCIFQLLQE AGIKTAFTKK CGETAFIAPQ CEMIPIEWVC RRIATGSFLK RNPGVQEGYK
FYPPKVEMFF KDDANNDPQW SEEQLIAAKF CFAGLVIGQT EVDIMSHATQ AIFEILEKSW
LPQDCTLVDM KIEFGVDVTT KEIVLADVID NDSWRLWPSG DRSQQKDKQS YRDLKEVTPE
GLQMVKKNFE WVADRVELLL KSDSQCRVVV LMGSTSDLGH CEKIKKACGN FGIPCELRVT
SAHKGPDETL RIKAEYEGDG IPTVFVSVAG RSNGLGPVLS GNTAYPVISC PPITPDWGAQ
DVWSSLRLPS GIGCSTILSP EGSAQFAAQI FGLNNHLVWA KLRASILNTW ISLKQADKKV
RQCNL
