P32073 (GUAA_DICDI) 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:	guaA
Synonyms:	gua2
ORF Names:	DDB_G0281551

Organism

Dictyostelium discoideum (Slime mold) [Reference proteome]

Taxonomic identifier

44689 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium

Protein attributes

Sequence length	718 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

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.
Developmental stage	Produced during growth but not during development.
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
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 sequence or structural similarity Ref.1. Source: dictyBase glutamine metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	phagocytic vesicle Inferred from direct assay Ref.3. Source: dictyBase
Molecular_function	ATP binding Inferred from sequence or structural similarity Ref.1. Source: dictyBase GMP synthase (glutamine-hydrolyzing) activity Inferred from sequence or structural similarity Ref.1. Source: dictyBase pyrophosphatase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 718	718	GMP synthase [glutamine-hydrolyzing]		PRO_0000140256
Regions
	Domain	43 – 247	205	Glutamine amidotransferase type-1
	Domain	248 – 457	210	GMPS ATP-PPase
	Nucleotide binding	275 – 281	7	ATP By similarity
Sites
	Active site	128	1	For GATase activity By similarity
	Active site	221	1	For GATase activity By similarity
	Active site	223	1	For GATase activity By similarity
Experimental info
	Sequence conflict	535	1	G → V in AAA33213. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P32073 [UniParc]. Last modified December 4, 2007. Version 2. Checksum: DCB5DCDE84793DEA	FASTA	718	79,562
	10 20 30 40 50 60 MTITSPVIKT PPLNSEIRLE SNLTVESGDI EINEKDIVNA SEVIVILDAG SQYSKVIDRR 70 80 90 100 110 120 VRELNVASEI HPLNIDLLEL IKIKSKSGST IKGIIISGGP ESVYGENAPK FDKSLFSEKL 130 140 150 160 170 180 NLPIFGICYG MQLMNYIFGG KVESNSQRED GVHNIEILKD ENQQLVSKLF KNLNQTEQVL 190 200 210 220 230 240 LTHGDSVTKI ADGFKIICKS DDGIVSGIEN ERLGYYGVQF HPEVDLTTNG KKMFSNFLID 250 260 270 280 290 300 ICGCSANYTL DDREQQAITY IKSIVSNKKV LVLVSGGVDS TVCAALISKA IGPENVIALH 310 320 330 340 350 360 IDNGFMRKDE SLNVEKALSV LGLHLIVVDA SQTFYNSTTT IKGHLTSSLK ETISPEERRK 370 380 390 400 410 420 IIGDTFMRVA ENEVKKLGLQ PEDVYLAQGT LRPDLIESSS KTVSGVADVI KTHHNDTELV 430 440 450 460 470 480 RILRDSGRVV EPLKDYHKDE VRELGKSLGL SDSLVWRQPF PGPGLAIRII CADEPYLVNY 490 500 510 520 530 540 DFTNNVVQYL VTGEASSELE SEVKIKIDKQ LTEMKCKRQD KITIKPVLLP IQTVGVQGDG 550 560 570 580 590 600 RTYSYLLGLY SSENSTIDQI PWSYIFNLAR TIPKICHNIN RVVFIFSQNA TKHTNIKVSN 610 620 630 640 650 660 EPVKHITPTR LTPDVIKQLQ HADSIVSEQL YKYNLIKSLS QVPVVSLPID FGVTGNRSIA 670 680 690 700 710 IRTFITNDFM TGVPAIPGKN ISFDCLQEIT NNILTSVNGI SKVLFDCTSK PPGTTEFL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Functional cloning of a Dictyostelium discoideum cDNA encoding GMP synthetase." van Lookeren Campagne M.M., Franke J., Kessin R.H. J. Biol. Chem. 266:16448-16452(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: AX3.
[2]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AX4.
[3]	"Proteomics fingerprinting of phagosome maturation and evidence for the role of a Galpha during uptake." Gotthardt D., Blancheteau V., Bosserhoff A., Ruppert T., Delorenzi M., Soldati T. Mol. Cell. Proteomics 5:2228-2243(2006) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Strain: AX2.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M64282 mRNA. Translation: AAA33213.1. AAFI02000042 Genomic DNA. Translation: EAL66537.1.
PIR	A41164.
RefSeq	XP_640534.1. XM_635442.1.
3D structure databases
ProteinModelPortal	P32073.
ModBase	Search...
Protein-protein interaction databases
STRING	44689.DDB_0215334.
Protein family/group databases
MEROPS	C26.962.
Proteomic databases
PRIDE	P32073.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblProtists	DDB0215334; DDB0215334; DDB_G0281551.
GeneID	8623144.
KEGG	ddi:DDB_G0281551.
Organism-specific databases
dictyBase	DDB_G0281551. guaA.
Phylogenomic databases
eggNOG	COG0519.
KO	K01951.
OMA	TCMFIDH.
ProtClustDB	CLSZ2430524.
Enzyme and pathway databases
UniPathway	UPA00189; UER00296.
Family and domain databases
Gene3D	3.40.50.620. 1 hit.
InterPro	IPR017926. GATASE_1. IPR001674. GMP_synth_C. IPR004739. GMP_synth_N. IPR025777. GMPS_ATP_PPase_dom. IPR022310. NAD/GMP_synthase. IPR014729. Rossmann-like_a/b/a_fold. [Graphical view]
Pfam	PF00117. GATase. 1 hit. PF00958. GMP_synt_C. 1 hit. PF02540. NAD_synthase. 1 hit. [Graphical view]
TIGRFAMs	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_DICDI

Accession

Primary (citable) accession number: P32073
Secondary accession number(s): Q54TQ7

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	December 4, 2007
Last modified:	May 1, 2013
This is version 96 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)