Q7VLE9 (GUAA_HAEDU) 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:	HD_1504

Organism

Haemophilus ducreyi (strain 35000HP / ATCC 700724) [Complete proteome] [HAMAP]

Taxonomic identifier

233412 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Haemophilus › Haemophilus ducreyi

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.
Catalytic activity	ATP + xanthosine 5'-phosphate + L-glutamine + H2O = AMP + diphosphate + GMP + L-glutamate. HAMAP-Rule MF_00344
Pathway	Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln route): step 1/1. HAMAP-Rule MF_00344
Subunit structure	Homodimer 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
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: HAMAP glutamine metabolic process Inferred from electronic annotation. Source: HAMAP
Molecular_function	ATP binding Inferred from electronic annotation. Source: HAMAP GMP synthase (glutamine-hydrolyzing) activity Inferred from electronic annotation. Source: HAMAP 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 – 523	523	GMP synthase [glutamine-hydrolyzing] HAMAP-Rule MF_00344		PRO_0000140130
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)
	Q7VLE9 [UniParc]. Last modified October 1, 2003. Version 1. Checksum: 590F209389B0B3EA	FASTA	523	58,283
	10 20 30 40 50 60 MNNIHNHKIL ILDFGSQYTQ LIARRIREIG VYCELWAWDV TEKQIREFNP TGIILSGGPE 70 80 90 100 110 120 STTETNSPHA PEYVFKAGVP VLGICYGMQT MAMQLGGLTE ASEQREFGYA AVELQHADQL 130 140 150 160 170 180 FAKLNDDLTA SQPKLDVWMS HGDKVTRLPA GFQTTAVTPT CPIAAMSDEK RRFYGVQFHP 190 200 210 220 230 240 EVTHTKSGLA LLTNFVENIC GCARSWTPEN IIEDAVAKIK QKVGNDQVIL GLSGGVDSSV 250 260 270 280 290 300 TALLLHRAIG KNLHCVFVDN GLLRLNEGDQ VMEMFGDKFG LNIIRVNAEE RFLEALKGID 310 320 330 340 350 360 EPEAKRKIIG KVFIDIFDDE AKKLTDVKWL AQGTIYPDVI ESAASKTGKA HVIKSHHNVG 370 380 390 400 410 420 GLPDYMKLGL VEPLRELFKD EVRKIGLTLG LPAEMLNRHP FPGPGLGVRV LGEIKKEYCD 430 440 450 460 470 480 LLRNADAIFI EELYKSGWYY KVSQAFTVFL PVKSVGVMGD GRKYDWVVSL RAVETIDFMT 490 500 510 520 AHWAHLPYEL LGKISNRIIN EVNGISRVVY DVSGKPPATI EWE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The complete genome sequence of Haemophilus ducreyi." Munson R.S. Jr., Ray W.C., Mahairas G., Sabo P., Mungur R., Johnson L., Nguyen D., Wang J., Forst C., Hood L. Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 35000HP / ATCC 700724.
[2]	"Haemophilus ducreyi secretes a filamentous hemagglutinin-like protein." Ward C.K., Lumbley S.R., Latimer J.L., Cope L.D., Hansen E.J. J. Bacteriol. 180:6013-6022(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 156-523. Strain: 35000HP / ATCC 700724.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE017143 Genomic DNA. Translation: AAP96299.1. AF057695 Genomic DNA. Translation: AAC79759.1.
PIR	T31103.
RefSeq	NP_873910.1. NC_002940.2.
3D structure databases
ProteinModelPortal	Q7VLE9.
SMR	Q7VLE9. Positions 3-523.
ModBase	Search...
Protein-protein interaction databases
STRING	233412.HD1504.
Proteomic databases
PRIDE	Q7VLE9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAP96299; AAP96299; HD_1504.
GeneID	1491382.
KEGG	hdu:HD1504.
PATRIC	20179248. VBIHaeDuc133973_1257.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0519.
KO	K01951.
OMA	YDYVVAL.
ProtClustDB	PRK00074.
Enzyme and pathway databases
BioCyc	HDUC233412:GH5F-1310-MONOMER.
UniPathway	UPA00189; UER00296.
Family and domain databases
Gene3D	3.40.50.620. 1 hit.
HAMAP	MF_00344. GMP_synthase.
InterPro	IPR017926. GATASE_1. IPR001674. GMP_synth_C. IPR004739. GMP_synth_N. IPR022955. GMP_synthase. 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	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_HAEDU

Accession

Primary (citable) accession number: Q7VLE9
Secondary accession number(s): Q9ZHL2

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 2004
Last sequence update:	October 1, 2003
Last modified:	May 1, 2013
This is version 74 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program