Reviewed, UniProtKB/Swiss-Prot Q54GJ2 (PUR2_DICDI)

Names and origin

Protein names

Recommended name:
    Bifunctional purine biosynthetic protein purD
Including the following 2 domains:
    1- Recommended name:
            Phosphoribosylamine--glycine ligase
              EC=6.3.4.13
        Alternative name(s):
            Glycinamide ribonucleotide synthetase
              Short name=GARS
            Phosphoribosylglycinamide synthetase
    2- Recommended name:
            Phosphoribosylformylglycinamidine cyclo-ligase
              EC=6.3.3.1
        Alternative name(s):
            Phosphoribosyl-aminoimidazole synthetase
            AIR synthase
              Short name=AIRS

Gene names

Name:	purD
ORF Names:	DDB_G0290121

Organism

Dictyostelium discoideum (Slime mold) [Complete proteome]

Taxonomic identifier

44689 [NCBI]

Taxonomic lineage

Eukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium

Protein attributes

Sequence length	815 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	ATP + 5-phospho-D-ribosylamine + glycine = ADP + phosphate + N(1)-(5-phospho-D-ribosyl)glycinamide. ATP + 2-(formamido)-N(1)-(5-phospho-D-ribosyl)acetamidine = ADP + phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole.
Pathway	Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide: step 2/2. Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/2.
Sequence similarities	In the N-terminal section; belongs to the GARS family. In the C-terminal section; belongs to the AIR synthase family. Contains 1 ATP-grasp domain.

Ontologies

Keywords
Biological process	Purine biosynthesis
Ligand	ATP-binding Manganese Metal-binding Nucleotide-binding
Molecular function	Ligase
Technical term	Complete proteome Direct protein sequencing Multifunctional enzyme
Gene Ontology (GO)
Biological process	'de novo' IMP biosynthetic process Inferred from electronic annotation. Source: InterPro purine base biosynthetic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: InterPro
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW manganese ion binding Inferred from electronic annotation. Source: UniProtKB-KW phosphoribosylamine-glycine ligase activity Inferred from electronic annotation. Source: EC phosphoribosylformylglycinamidine cyclo-ligase 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
	Chain	1 – 815	815	Bifunctional purine biosynthetic protein purD		PRO_0000328326
Regions
	Domain	113 – 343	231	ATP-grasp
	Nucleotide binding	139 – 200	62	ATP By similarity
	Region	5 – 452	448	GARS
	Region	467 – 808	342	AIRS
Sites
	Metal binding	313	1	Manganese By similarity
	Metal binding	315	1	Manganese By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q54GJ2-1 [UniParc]. Last modified May 24, 2005. Version 1. Checksum: C24A183386A06FC6	FASTA	815	87,706
	10 20 30 40 50 60 MTIKNNILVI GSGSREHAIT WKLLESNQVD KVILVPGNAS SSTMERVITV ECSKIDAESI 70 80 90 100 110 120 SNICKEHNVE YVFVGPEVPL VDGIVDGLKR KGISCFGPTK KAAQLEGSKV FCKDFMARNN 130 140 150 160 170 180 IPSARYQTFT DYNKAKQYIE SLNYKIVLKA SGCAAGKGVL IPNNKEEELE GLKRIMVDKE 190 200 210 220 230 240 FGSAGDEIVI EEFLDGEECS LMCFSDGYSL VVMPPAQDHK RIFDGDKGAN TGGMGAYAPA 250 260 270 280 290 300 PFIVDCNNNA TTDKSKSKSS FGTIIDRCVE TILKPTINGM RKEGKPFVGV LFAGLMVSSS 310 320 330 340 350 360 SSTTNDKVIN VLEFNCRMGD PETQVVLPLL ETDLFEIVLA CIEGRLDGLD VKWSNKFAVT 370 380 390 400 410 420 VVAASKGYPD SYPKGLKING LLENKNTNDN IIFQAGTTVN GSNDIVTNGG RVLSCTSVSE 430 440 450 460 470 480 SLEDAIKNSY KLIETISFEG MQYRKDIGQK ALNHLERKKQ QQANSKQSVS YSESGVDIER 490 500 510 520 530 540 GDAVVDNIGP LAKATTRLGC VSDLGGFGAL FDTKAAGFRD PILVSGTDGV GTKLKIAQEL 550 560 570 580 590 600 GIHDSIGIDL VAMCVNDVVV QGAEPLFFLD YFATGRIHVD VATQVVSGIA RGCKESGCAL 610 620 630 640 650 660 IGGETAEMPG MYKDGEYDLA GFSVGAVERD QMLPSNIQEG NILLGLASSG VHSNGYSLVR 670 680 690 700 710 720 YLIETKSGGL TYNSIAPFDS SKTLGQVLLT PTKLYVLSCL AAIKSGGVNG LAHITGGGIT 730 740 750 760 770 780 ENLPRVIPDG LDCEVELGSW EILPIFKYLV ELGNMETEEL LKTFNSGIGM ILIVSPDKVD 790 800 810 SITKSLESNN EKVYKIGKII NSKTSKQSKS KVIYK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The genome of the social amoeba Dictyostelium discoideum." Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N. , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A. Nature 435:43-57(2005) [PubMed: 15875012] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AX4.
[2]	Bienvenut W.V., Ura S., Insall R.H. Submitted (JUL-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 515-533 AND 667-682, MASS SPECTROMETRY. Strain: AX2.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AAFI02000153 Genomic DNA. Translation: EAL62377.1.
RefSeq	XP_635881.1.
3D structure databases
HSSP	HSSP built from PDB template 1CLI based on UniProtKB P08178.
SMR	Q54GJ2. Positions 2-455, 468-804.
ModBase	Search...
Protein-protein interaction databases
STRING	Q54GJ2.
Genome annotation databases
GeneID	8627491.
KEGG	ddi:DDB_0230084.
Organism-specific databases
dictyBase	DDB_G0290121. purD.
Phylogenomic databases
eggNOG	KOG0237.
HOGENOM	HBG328156.
OMA	GETSEMP.
PhylomeDB	Q54GJ2.
Enzyme and pathway databases
BRENDA	6.3.3.1. 424. 6.3.4.13. 424.
Family and domain databases
InterPro	IPR000728. AIR_synth. IPR010918. AIR_synth_C. IPR011761. ATP-grasp. IPR013815. ATP_grasp_subdomain_1. IPR013816. ATP_grasp_subdomain_2. IPR013817. Pre-ATP_grasp. IPR016185. PreATP-grasp-like. IPR020561. PRibGlycinamid_synth_ATP-grasp. IPR000115. PRibGlycinamide_synth. IPR020560. PRibGlycinamide_synth_C-dom. IPR020562. PRibGlycinamide_synth_N-dom. IPR004733. PurM_cligase. IPR016188. PurM_N-like. IPR011054. Rudment_hybrid_motif. [Graphical view]
Gene3D	G3DSA:3.30.1490.20. ATP_grasp_subdomain_1. 1 hit. G3DSA:3.30.470.20. ATP_grasp_subdomain_2. 1 hit. G3DSA:3.90.600.10. Gars. 1 hit. G3DSA:3.40.50.20. Pre-ATP_grasp. 1 hit.
Pfam	PF00586. AIRS. 1 hit. PF02769. AIRS_C. 1 hit. PF01071. GARS_A. 1 hit. PF02843. GARS_C. 1 hit. PF02844. GARS_N. 1 hit. [Graphical view]
TIGRFAMs	TIGR00877. purD. 1 hit. TIGR00878. purM. 1 hit.
PROSITE	PS50975. ATP_GRASP. 1 hit. PS00184. GARS. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PUR2_DICDI

Accession

Primary (citable) accession number: Q54GJ2

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 8, 2008
Last sequence update:	May 24, 2005
Last modified:	February 9, 2010
This is version 40 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)