Reviewed, UniProtKB/Swiss-Prot Q9DCL9 (PUR6_MOUSE)

Names and origin

Protein names

Recommended name:
    Multifunctional protein ADE2
Including the following 2 domains:
    1- Recommended name:
            Phosphoribosylaminoimidazole-succinocarboxamide synthase
              EC=6.3.2.6
        Alternative name(s):
            SAICAR synthetase
    2- Recommended name:
            Phosphoribosylaminoimidazole carboxylase
              EC=4.1.1.21
        Alternative name(s):
            AIR carboxylase
              Short name=AIRC

Gene names

Name:

Paics

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	425 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate = ADP + phosphate + (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido)succinate. 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate = 5-amino-1-(5-phospho-D-ribosyl)imidazole + CO2.
Pathway	Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate: step 1/2. Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate from 5-amino-1-(5-phospho-D-ribosyl)imidazole (carboxylase route): step 1/1.
Subunit structure	Homooctamer By similarity.
Sequence similarities	In the N-terminal section; belongs to the SAICAR synthetase family. In the C-terminal section; belongs to the AIR carboxylase family.

Ontologies

Keywords
Biological process	Purine biosynthesis
Ligand	ATP-binding Nucleotide-binding
Molecular function	Decarboxylase Ligase Lyase
PTM	Acetylation Phosphoprotein
Technical term	Multifunctional enzyme
Gene Ontology (GO)
Biological process	'de novo' IMP biosynthetic process Inferred from electronic annotation. Source: InterPro
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW phosphoribosylaminoimidazole carboxylase activity Inferred from electronic annotation. Source: EC phosphoribosylaminoimidazolesuccinocarboxamide synthase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 425	424	Multifunctional protein ADE2		PRO_0000075031
Regions
	Region	2 – 260	259	SAICAR synthetase
	Region	261 – 425	165	AIR carboxylase
	Region	261 – 266	6	Linker By similarity
	Region	267 – 425	159	AIR carboxylase By similarity
Sites
	Active site	101	1	For SAICAR synthetase activity By similarity
	Active site	107	1	For SAICAR synthetase activity By similarity
	Active site	215	1	For SAICAR synthetase activity By similarity
	Active site	303	1	For AIR carboxylase activity By similarity
	Active site	332	1	For AIR carboxylase activity By similarity
	Site	334	1	Essential for AIR carboxylase activity By similarity
Amino acid modifications
	Modified residue	2	1	N-acetylalanine By similarity
	Modified residue	22	1	Phosphotyrosine Ref.2
	Modified residue	53	1	N6-acetyllysine By similarity
	Modified residue	105	1	Phosphothreonine By similarity
	Modified residue	107	1	Phosphoserine By similarity
	Modified residue	238	1	Phosphothreonine By similarity
	Modified residue	247	1	N6-acetyllysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9DCL9-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 302C64863937D017	FASTA	425	47,070
	10 20 30 40 50 60 MATAYVVNIG KKLYEGKTKE VYELLDTPGR VLLQSKDQIT AGNAARKNHL EGKAAISNKI 70 80 90 100 110 120 TSCIFQLLQE AGIKTAFTKK CGETAFIAPQ CEMIPIEWVC RRIATGSFLK RNPGVQEGYK 130 140 150 160 170 180 FYPPKVEMFF KDDANNDPQW SEEQLIAAKF CFAGLVIGQT EVDIMSHATQ AIFEILEKSW 190 200 210 220 230 240 LPQDCTLVDM KIEFGVDVTT KEIVLADVID NDSWRLWPSG DRSQQKDKQS YRDLKEVTPE 250 260 270 280 290 300 GLQMVKKNFE WVADRVELLL KSDSQCRVVV LMGSTSDLGH CEKIKKACGN FGIPCELRVT 310 320 330 340 350 360 SAHKGPDETL RIKAEYEGDG IPTVFVSVAG RSNGLGPVLS GNTAYPVISC PPITPDWGAQ 370 380 390 400 410 420 DVWSSLRLPS GIGCSTILSP EGSAQFAAQI FGLNNHLVWA KLRASILNTW ISLKQADKKV RQCNL

References

[1]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Kidney.
[2]	"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry." Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J. Mol. Cell. Proteomics 8:904-912(2009) [PubMed: 19131326] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-22, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK002669 mRNA. Translation: BAB22273.1.
IPI	IPI00322096.
UniGene	Mm.182931 Mm.431705
3D structure databases
SMR	Q9DCL9. Positions 7-425.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9DCL9.
PTM databases
PhosphoSite	Q9DCL9.
Proteomic databases
PRIDE	Q9DCL9.
Genome annotation databases
Ensembl	ENSMUST00000031160; ENSMUSP00000031160; ENSMUSG00000029247; Mus musculus. [Genome view] ENSMUST00000117536; ENSMUSP00000112879; ENSMUSG00000029247; Mus musculus. [Genome view] ENSMUST00000120912; ENSMUSP00000113483; ENSMUSG00000029247; Mus musculus. [Genome view]
Organism-specific databases
MGI	MGI:1914304. Paics.
Phylogenomic databases
HOGENOM	HBG306070.
HOVERGEN	Q9DCL9.
InParanoid	Q9DCL9.
PhylomeDB	Q9DCL9.
Enzyme and pathway databases
BRENDA	4.1.1.21. 244. 6.3.2.6. 244.
Gene expression databases
ArrayExpress	Q9DCL9.
Bgee	Q9DCL9.
Genevestigator	Q9DCL9.
GermOnline	ENSMUSG00000029247. Mus musculus.
Family and domain databases
InterPro	IPR000031. AIR_COase_core. IPR013816. ATP_grasp_subdomain_2. IPR001636. SAICAR_synt. IPR018236. SAICAR_synthetase_CS. [Graphical view]
Gene3D	G3DSA:3.40.50.7700. AIR_carboxyl. 1 hit. G3DSA:3.30.470.20. ATP_grasp_subdomain_2. 1 hit.
PANTHER	PTHR11609. SAICAR_synt. 1 hit.
Pfam	PF00731. AIRC. 1 hit. PF01259. SAICAR_synt. 1 hit. [Graphical view]
TIGRFAMs	TIGR01162. purE. 1 hit.
PROSITE	PS01057. SAICAR_SYNTHETASE_1. 1 hit. PS01058. SAICAR_SYNTHETASE_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
SOURCE	Search...

Entry information

Entry name

PUR6_MOUSE

Accession

Primary (citable) accession number: Q9DCL9

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 14, 2001
Last sequence update:	January 23, 2007
Last modified:	February 9, 2010
This is version 70 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)