Q6CEF3 (GUAA_YARLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
GMP synthase [glutamine-hydrolyzing]
EC=6.3.5.2

Alternative name(s):
GMP synthetase
Glutamine amidotransferase

Gene names

Name:	GUA1
Ordered Locus Names:	YALI0B16104g

Organism

Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica)

Taxonomic identifier

284591 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	527 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	ATP + xanthosine 5'-phosphate + L-glutamine + H2O = AMP + diphosphate + GMP + L-glutamate.
Pathway	Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln route): step 1/1.
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Contains 1 glutamine amidotransferase type-1 domain. Contains 1 GMPS ATP-PPase (ATP pyrophosphatase) domain.

Ontologies

Keywords
Biological process	GMP biosynthesis Purine biosynthesis
Cellular component	Cytoplasm
Domain	Glutamine amidotransferase
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	GMP biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW glutamine metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW GMP synthase (glutamine-hydrolyzing) 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 – 527	527	GMP synthase [glutamine-hydrolyzing]		PRO_0000286156
Regions
	Domain	13 – 202	190	Glutamine amidotransferase type-1
	Domain	203 – 402	200	GMPS ATP-PPase
	Nucleotide binding	231 – 237	7	ATP By similarity
Sites
	Active site	89	1	For GATase activity By similarity
	Active site	176	1	For GATase activity By similarity
	Active site	178	1	For GATase activity By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6CEF3 [UniParc]. Last modified August 16, 2004. Version 1. Checksum: F885D9227D29BB5D	FASTA	527	58,350
	10 20 30 40 50 60 MPAPVNIPSM FDTILVLDFG SQYSHLITRR LREFNVYAEM LPCTQKIAEL PWKPKGVILS 70 80 90 100 110 120 GGPYSVYAEG SPHVDHAVFD LGVPILGICY GMQELAWING KGVHAGEKKE FGHATIHVEK 130 140 150 160 170 180 PSDPLFHGID NFQVWMSHGD KLNALPTGYE VVATSDNSPY AGIAHTSEKI WGIQFHPEVT 190 200 210 220 230 240 HTTKGKQLLQ NFAVDICGAA QKWSMENFVD TEIQRIRDLV GPHAEVIGAV SGGVDSTVGA 250 260 270 280 290 300 KLMKEAIGDR FHAILVDNGV MRLNECENVK KTLGEGLGIN LNVVDAADLF LGKLKGVTDP 310 320 330 340 350 360 EKKRKIIGNT FIEVFEEEAA KIQPTHPEAG EIEFLLQGTL YPDVIESISF KGPSQTIKTH 370 380 390 400 410 420 HNVGGLLDNM KLKLIEPLRE LFKDEVRKLG EIMGIPHDLV WRHPFPGPGI AIRVLGEVTP 430 440 450 460 470 480 SQVEIARKAD FIYIEEIKKA GIYEEISQAF ACLLPVKSVG VMGDQRTYEQ VIALRAIETV 490 500 510 520 DFMTADWYIF DANFLKTVAR RIVNEVPGVA RVVYDITSKP PATVEWE

References

[1]

"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
EMBL GenBank DDBJ	CR382128 Genomic DNA. Translation: CAG83212.1.
RefSeq	XP_500959.1. XM_500959.1.
3D structure databases
HSSP	HSSP built from PDB template 1GPM based on UniProtKB P04079.
ProteinModelPortal	Q6CEF3.
ModBase	Search...
Protein-protein interaction databases
STRING	Q6CEF3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2906785.
GenomeReviews	Gene locus YALI0B16104g in contig CR382128_GR.
KEGG	yli:YALI0B16104g.
Phylogenomic databases
eggNOG	fuNOG07551.
HOGENOM	HBG391775.
OMA	DGRTYEY.
OrthoDB	EOG4WWVST.
Family and domain databases
InterPro	IPR017926. GATASE_1. IPR001674. GMP_synth_C. IPR004739. GMP_synth_N. IPR022955. GMP_synthase. IPR022310. NAD/GMP_synthase. IPR014729. Rossmann-like_a/b/a_fold. [Graphical view]
Gene3D	G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
KO	K01951.
Pfam	PF00117. GATase. 1 hit. PF00958. GMP_synt_C. 1 hit. PF02540. NAD_synthase. 1 hit. [Graphical view]
TIGRFAMs	TIGR00884. GuaA_Cterm. 1 hit. TIGR00888. GuaA_Nterm. 1 hit.
PROSITE	PS51273. GATASE_TYPE_1. 1 hit. PS51553. GMPS_ATP_PPASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GUAA_YARLI

Accession

Primary (citable) accession number: Q6CEF3

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 2007
Last sequence update:	August 16, 2004
Last modified:	January 25, 2012
This is version 59 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program