Q0VNF0 (GUAA_ALCBS) 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:	ABO_1850

Organism

Alcanivorax borkumensis (strain SK2 / ATCC 700651 / DSM 11573) [Complete proteome] [HAMAP]

Taxonomic identifier

393595 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Oceanospirillales › Alcanivoracaceae › Alcanivorax

Protein attributes

Sequence length	523 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 – 523	523	GMP synthase [glutamine-hydrolyzing] HAMAP MF_00344		PRO_1000120205
Regions
	Domain	8 – 205	198	Glutamine amidotransferase type-1
	Domain	206 – 398	193	GMPS ATP-PPase
	Nucleotide binding	233 – 239	7	ATP By similarity
Sites
	Active site	85	1	Nucleophile By similarity
	Active site	179	1	By similarity
	Active site	181	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q0VNF0 [UniParc]. Last modified September 5, 2006. Version 1. Checksum: 56A33AB993CF8506	FASTA	523	57,751
	10 20 30 40 50 60 MTDIHAQRIL ILDFGSQYTQ LIARRVREIG VYCEIRAFDM TAEELAEFAP KGIILSGGPE 70 80 90 100 110 120 SVTAAQTPRA PQAVFEAGIP VLGICYGMQT MAEQLGGKVI AGEKHEFGYA RVEKAEPNAL 130 140 150 160 170 180 LDGIVDHEEQ GKEFLDVWMS HGDRVGEMPA GFVATATTGS CPIAGMANDE KRFYGIQFHP 190 200 210 220 230 240 EVTHTLQGGR LLERFIRELC ECEALWTPSN IISDAIDTIR EQVGTDEVIL GLSGGVDSSV 250 260 270 280 290 300 VAALLHKAIG DQLTCVFVDN GLLRHQEGDQ VMEMFADNMG VKVIRVDAED NFLGKLAGEA 310 320 330 340 350 360 DPEKKRKIIG NTFIDIFDDE ASKLQNANWL AQGTIYPDVI ESAASKTGKA HVIKSHHNVG 370 380 390 400 410 420 GLPEDMKLKL VEPLRELFKD EVRKIGLELG LPYDMVYRHP FPGPGLGVRI LGEVKKEYAD 430 440 450 460 470 480 TLRLADHIFI EELRAAGLYH KTSQAFAVFL PVKSVGVVGD ARRYEYVVAL RAVETIDFMT 490 500 510 520 ARWAHLPYDF LELVSSRIIN EIPGISRVTY DISSKPPATI EWE

References

[1]

"Genome sequence of the ubiquitous hydrocarbon-degrading marine bacterium Alcanivorax borkumensis." Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T., Brecht M., Buhrmester J., Chernikova T.N., Denaro R., Ferrer M., Gertler C., Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N., Lang S., Linke B., McHardy A.C., Meyer F. , Nechitaylo T., Puehler A., Regenhardt D., Rupp O., Sabirova J.S., Selbitschka W., Yakimov M.M., Timmis K.N., Vorhoelter F.-J., Weidner S., Kaiser O., Golyshin P.N. Nat. Biotechnol. 24:997-1004(2006) [PubMed: 16878126] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: SK2 / ATCC 700651 / DSM 11573.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AM286690 Genomic DNA. Translation: CAL17298.1.
RefSeq	YP_693570.1. NC_008260.1.
3D structure databases
ProteinModelPortal	Q0VNF0.
SMR	Q0VNF0. Positions 3-523.
ModBase	Search...
Protein-protein interaction databases
STRING	Q0VNF0.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4212661.
GenomeReviews	Gene locus ABO_1850 in contig AM286690_GR.
KEGG	abo:ABO_1850.
NMPDR	fig|393595.12.peg.1855.
PATRIC	20841535. VBIAlcBor124741_1942.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0519.
HOGENOM	HBG391775.
OMA	DGRTYEY.
PhylomeDB	Q0VNF0.
ProtClustDB	PRK00074.
Enzyme and pathway databases
BioCyc	ABOR393595:ABO_1850-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_ALCBS

Accession

Primary (citable) accession number: Q0VNF0

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 14, 2009
Last sequence update:	September 5, 2006
Last modified:	January 25, 2012
This is version 55 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program