Reviewed, UniProtKB/Swiss-Prot Q99148 (PUR2_YARLI)

Names and origin

Protein names

Recommended name:
    Bifunctional purine biosynthetic protein ADE1
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:	ADE1
Ordered Locus Names:	YALI0F21010g

Organism

Yarrowia lipolytica (Candida lipolytica) [Complete proteome]

Taxonomic identifier

4952 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Dipodascaceae › Yarrowia

Protein attributes

Sequence length	788 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

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 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 – 788	788	Bifunctional purine biosynthetic protein ADE1		PRO_0000074940
Regions
	Domain	114 – 323	210	ATP-grasp
	Nucleotide binding	140 – 201	62	ATP By similarity
	Region	1 – 432	432	GARS
	Region	442 – 752	311	AIRS
Sites
	Metal binding	291	1	Manganese By similarity
	Metal binding	293	1	Manganese By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q99148-1 [UniParc]. Last modified November 1, 1997. Version 1. Checksum: 6EC170ECB27AFCF4	FASTA	788	83,759
	10 20 30 40 50 60 MSLRILLVGN GGREHALAWK LAQSPLVERI FVAPGNGGTD NPQGKIENIA IGSSQKDFAK 70 80 90 100 110 120 LVEFAQSKDV GLVIPGPEQP LVEGIETHFR KVGIPVFGPS EKAAVMEGSK TFSKDFMKKH 130 140 150 160 170 180 NIPTAAFENF TDYNKAVDYV KKVGHRVVIK ASGLAAGKGV LIPTSTEEAI AAVKEVMQDK 190 200 210 220 230 240 AFGEAGDEVV IEEFLEGDEL SILAFSDGYT VVDMPPAQDH KRIGDGDQGL NTGGMGAYCP 250 260 270 280 290 300 APIGTPALLQ EIKESILQPT IDGMRRDGIP FVGMLFTGIM LTPDGKPKVL EYNVRFGDPE 310 320 330 340 350 360 TQTILPLLSD DTDLAEVMLA CVERRLDAVT LRVKPDAHAV TVVMSAGGYP ESYKKGDAIT 370 380 390 400 410 420 VGGLPEQTYI FHAGTASENG QVITAGGRVI ASTAVAPTLK DAVAQAYKGA DAVEFNGKYN 430 440 450 460 470 480 RKDIAYKAFR DAEKTSGGIT YAQAGVSIDN GNKLVQQIKE KVKSTARPGT DSVIGGFGGL 490 500 510 520 530 540 FDLKAAGFRD PLLVGATDGV GTKLKIAQSI DKHDTVGIDL VAMNVNDLVV QGAEPLVFLD 550 560 570 580 590 600 YYATGKLDVN AAAAFVGGVA DGCIQAGCAL IGGETAEMPG IYYGNDYDAN GTSIGAVERD 610 620 630 640 650 660 AVLPRMDEIA KGDAILGLAS SGVHSNGFSL VRKIIEHAGL TYTDACPWDQ SKSLGEALLT 670 680 690 700 710 720 PTRIYVKQLL PVINAKLTSA LAHITGGGLV ENIPRILPEN YSAKIDVSTW PLPPVFQWLG 730 740 750 760 770 780 KAGNVPKEDI SKTLNMGIGM ILVVKQEKVA EVTQLLEKVG EKVYQIGEIV PDNDVDEKTV LINTENWY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Strick C.A., James L.C., Cole K.E., Elsenboss L.A. Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Genome evolution in yeasts." Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S. , Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., Wincker P., Souciet J.-L. Nature 430:35-44(2004) [PubMed: 15229592] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CLIB 122 / E 150.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U40565 Genomic DNA. Translation: AAA85393.1. CR382132 Genomic DNA. Translation: CAG78498.1.
RefSeq	XP_505689.1.
3D structure databases
HSSP	HSSP built from PDB template 1GSO based on UniProtKB P15640.
ModBase	Search...
Protein-protein interaction databases
STRING	Q99148.
Genome annotation databases
GeneID	2907698.
GenomeReviews	Gene locus YALI0F21010g in contig CR382132_GR.
KEGG	yli:YALI0F21010g.
Phylogenomic databases
HOGENOM	Q99148.
OMA	GETSEMP.
Enzyme and pathway databases
BRENDA	6.3.3.1. 3602. 6.3.4.13. 3602.
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. IPR020561. PRibGlycinamid_synth_ATP-grasp. IPR000115. PRibGlycinamide_synth. IPR020560. PRibGlycinamide_synth_C-dom. IPR020559. PRibGlycinamide_synth_CS. IPR020562. PRibGlycinamide_synth_N-dom. IPR004733. PurM_cligase. [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:3.40.50.20. 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. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PUR2_YARLI

Accession

Primary (citable) accession number: Q99148

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	November 3, 2009
This is version 61 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)