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Q7VLE9 (GUAA_HAEDU) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHaemophilus ducreyi (strain 35000HP / ATCC 700724) [Complete proteome] [HAMAP]
Taxonomic identifier233412 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus

Protein attributes

Sequence length523 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the synthesis of GMP from XMP By similarity. HAMAP-Rule MF_00344

Catalytic activity

ATP + XMP + 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. HAMAP-Rule MF_00344

Sequence similarities

Contains 1 glutamine amidotransferase type-1 domain.

Contains 1 GMPS ATP-PPase (ATP pyrophosphatase) domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 523523GMP synthase [glutamine-hydrolyzing] HAMAP-Rule MF_00344
PRO_0000140130

Regions

Domain8 – 205198Glutamine amidotransferase type-1
Domain206 – 398193GMPS ATP-PPase
Nucleotide binding233 – 2397ATP By similarity

Sites

Active site851Nucleophile By similarity
Active site1791 By similarity
Active site1811 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7VLE9 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: 590F209389B0B3EA

FASTA52358,283
        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 

« Hide

References

« Hide '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.
PIRT31103.
RefSeqNP_873910.1. NC_002940.2.

3D structure databases

ProteinModelPortalQ7VLE9.
SMRQ7VLE9. Positions 3-523.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING233412.HD1504.

Proteomic databases

PRIDEQ7VLE9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAP96299; AAP96299; HD_1504.
GeneID1491382.
KEGGhdu:HD1504.
PATRIC20179248. VBIHaeDuc133973_1257.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0519.
KOK01951.
OMAKIYGLQF.
OrthoDBEOG6JHRJV.

Enzyme and pathway databases

BioCycHDUC233412:GH5F-1358-MONOMER.
UniPathwayUPA00189; UER00296.

Family and domain databases

Gene3D3.40.50.620. 1 hit.
3.40.50.880. 1 hit.
HAMAPMF_00344. GMP_synthase.
InterProIPR029062. Class_I_gatase-like.
IPR017926. GATASE.
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]
PfamPF00117. GATase. 1 hit.
PF00958. GMP_synt_C. 1 hit.
PF02540. NAD_synthase. 1 hit.
[Graphical view]
SUPFAMSSF52317. SSF52317. 1 hit.
TIGRFAMsTIGR00884. guaA_Cterm. 1 hit.
TIGR00888. guaA_Nterm. 1 hit.
PROSITEPS51273. GATASE_TYPE_1. 1 hit.
PS51553. GMPS_ATP_PPASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGUAA_HAEDU
AccessionPrimary (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: June 11, 2014
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways