Q3MEA8 (GUAA_ANAVT) 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
Ordered Locus Names:	Ava_1054

Organism

Anabaena variabilis (strain ATCC 29413 / PCC 7937) [Complete proteome] [HAMAP]

Taxonomic identifier

240292 [NCBI]

Taxonomic lineage

Bacteria › Cyanobacteria › Nostocales › Nostocaceae › Anabaena

Protein attributes

Sequence length	540 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the synthesis of GMP from XMP By similarity. HAMAP MF_00344
Catalytic activity	ATP + xanthosine 5'-phosphate + L-glutamine + H2O = AMP + diphosphate + GMP + L-glutamate. HAMAP MF_00344
Pathway	Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln route): step 1/1. HAMAP MF_00344
Subunit structure	Homodimer By similarity. HAMAP MF_00344
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
Gene Ontology (GO)
Biological process	GMP biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW asparagine biosynthetic process Inferred from electronic annotation. Source: InterPro glutamine metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW GMP synthase (glutamine-hydrolyzing) activity Inferred from electronic annotation. Source: EC asparagine synthase (glutamine-hydrolyzing) 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 – 540	540	GMP synthase [glutamine-hydrolyzing] HAMAP MF_00344		PRO_0000229397
Regions
	Domain	26 – 216	191	Glutamine amidotransferase type-1
	Domain	217 – 415	199	GMPS ATP-PPase
	Nucleotide binding	244 – 250	7	ATP By similarity
Sites
	Active site	103	1	Nucleophile By similarity
	Active site	190	1	By similarity
	Active site	192	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q3MEA8 [UniParc]. Last modified October 25, 2005. Version 1. Checksum: B91AC0FB0841C23D	FASTA	540	60,732
	10 20 30 40 50 60 MNTAVTLLTE QAPQPIEEFG QLERQIIIIL DFGSQYSELI ARRIRETQVY SEVLSYRTSA 70 80 90 100 110 120 EHLRQLNPKG IILSGGPSSV YSDRAPHCDP EIWNLGVPIL GVCYGMQLMV NQLGGEVAKA 130 140 150 160 170 180 DRGEYGKASL HIDDPTDLLT NVEDGTTMWM SHGDSVTKMP PGFEVLAHTD NTPCAAVADH 190 200 210 220 230 240 DKKLYGVQFH PEVVHSIGGL ALIRNFVYHI CECEPTWTTA AFVEEAIREV RAKVGDKRVL 250 260 270 280 290 300 LALSGGVDSS TLAFLMHKAI GDQLTCVFID QGFMRKYEPE RLVKLFQEQF HIPVEYVNAR 310 320 330 340 350 360 DRFLDIMVGV TDPEEKRRRI GHEFIQVFEE TSRNLGPFDY LAQGTLYPDV IESADTNVDP 370 380 390 400 410 420 QTGERVAVKI KSHHNVGGLP KDLRFKLVEP LRKLFKDEVR KVGRSVGLPE EIVQRQPFPG 430 440 450 460 470 480 PGLAIRILGE VTADRLNILR DADLIVRQEI NQRGLYNEYW QAFAVLLPIR SVGVMGDQRT 490 500 510 520 530 540 YAYPIVLRIV KSEDGMTADW ARVPYDVLEA ISNRIVNEVK GVNRVVFDIT SKPPGTIEWE

References

[1]

"Complete sequence of Anabaena variabilis ATCC 29413." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Saunders E.H., Schmutz J., Larimer F., Land M., Kyrpides N., Mavrommatis K., Richardson P. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 29413 / PCC 7937.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000117 Genomic DNA. Translation: ABA20678.1.
RefSeq	YP_321573.1. NC_007413.1.
3D structure databases
ProteinModelPortal	Q3MEA8.
ModBase	Search...
Protein-protein interaction databases
STRING	Q3MEA8.
Protein family/group databases
MEROPS	C26.A17.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3678606.
GenomeReviews	Gene locus Ava_1054 in contig CP000117_GR.
KEGG	ava:Ava_1054.
NMPDR	fig|240292.3.peg.264.
PATRIC	35422604. VBIAnaVar43351_1865.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0519.
HOGENOM	HBG391775.
OMA	DGRTYEY.
PhylomeDB	Q3MEA8.
ProtClustDB	PRK00074.
Enzyme and pathway databases
BioCyc	AVAR240292:AVA_1054-MONOMER.
Family and domain databases
HAMAP	MF_00344. GMP_synthase. [Tree]
InterPro	IPR001962. Asn_synthase. IPR017926. GATASE_1. IPR001674. GMP_synth_C. IPR004739. GMP_synth_N. IPR022955. 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	PF00733. Asn_synthase. 1 hit. PF00117. GATase. 1 hit. PF00958. GMP_synt_C. 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_ANAVT

Accession

Primary (citable) accession number: Q3MEA8

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 4, 2006
Last sequence update:	October 25, 2005
Last modified:	January 25, 2012
This is version 49 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program