Q0A9W8 (GUAA_ALHEH) 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:	Mlg_1016

Organism

Alkalilimnicola ehrlichei (strain MLHE-1) [Complete proteome] [HAMAP]

Taxonomic identifier

187272 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Chromatiales › Ectothiorhodospiraceae › Alkalilimnicola

Protein attributes

Sequence length	525 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 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
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 525	525	GMP synthase [glutamine-hydrolyzing] HAMAP MF_00344		PRO_1000120206
Regions
	Domain	9 – 207	199	Glutamine amidotransferase type-1
	Domain	208 – 400	193	GMPS ATP-PPase
	Nucleotide binding	235 – 241	7	ATP By similarity
Sites
	Active site	86	1	Nucleophile By similarity
	Active site	181	1	By similarity
	Active site	183	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q0A9W8 [UniParc]. Last modified October 17, 2006. Version 1. Checksum: 3E6CE4017F6B7BCA	FASTA	525	57,992
	10 20 30 40 50 60 MTQDIHAHRI LILDFGSQYT QLIARRVREA GVYCEIYAWD APETAIRDFG AAGFILSGGP 70 80 90 100 110 120 ESMTVDNGPR VPEAVFQAGV PVLGICYGMQ AMAGQLGGRV EASDHKEFGY ARVRARGHSR 130 140 150 160 170 180 LLRDIEDHAS PEGWGLLDVW MSHGDRVTGL PPGFKLIAST ESCPIAGIGD DERGYYGVQF 190 200 210 220 230 240 HPEVTHTPQG ARILSRFVHE ICGCPADWTP GNIVDDLIER VRRQVGGDKV LLGLSGGVDS 250 260 270 280 290 300 SVVAALLHRA IGDQLTCVFV DNGLLRKDEG DQVMATFARH MGVNVIRVDA EARFLEALKG 310 320 330 340 350 360 VDDPERKRKI IGNMFIEVFD EQAARLTEVD WLAQGTIYPD VIESAGSATG KAHVIKSHHN 370 380 390 400 410 420 VGGLPEDMTL KLVEPLRELF KDEVRRIGLE LGLPADMVYR HPFPGPGLGV RILGEVRKEY 430 440 450 460 470 480 ADLLREADAI FIEELRAHDL YDQVSQAFAV FLPVKSVGVT GDGRRYEYVV ALRAVETIDF 490 500 510 520 MTARWAHLPY EFLDHVSRRI INEIPGISRV AYDISGKPPA TIEWE

References

[1]

"Complete sequence of Alkalilimnicola ehrilichei MLHE-1." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. , Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Oremland R.S., Hoeft S.E., Switzer-Blum J., Kulp T., King G., Tabita R., Witte B., Santini J.M., Basu P., Hollibaugh J.T., Xie G., Stolz J.F., Richardson P. Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: MLHE-1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000453 Genomic DNA. Translation: ABI56369.1.
RefSeq	YP_741859.1. NC_008340.1.
3D structure databases
ProteinModelPortal	Q0A9W8.
SMR	Q0A9W8. Positions 3-525.
ModBase	Search...
Protein-protein interaction databases
STRING	Q0A9W8.
Protein family/group databases
MEROPS	C26.A17.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4270045.
GenomeReviews	Gene locus Mlg_1016 in contig CP000453_GR.
KEGG	aeh:Mlg_1016.
NMPDR	fig|187272.6.peg.980.
PATRIC	20861263. VBIAlkEhr114327_1016.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0519.
HOGENOM	HBG391775.
OMA	DGRTYEY.
PhylomeDB	Q0A9W8.
ProtClustDB	PRK00074.
Enzyme and pathway databases
BioCyc	AEHR187272:MLG_1016-MONOMER.
Family and domain databases
HAMAP	MF_00344. GMP_synthase. [Tree]
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_ALHEH

Accession

Primary (citable) accession number: Q0A9W8

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 14, 2009
Last sequence update:	October 17, 2006
Last modified:	January 25, 2012
This is version 48 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program