Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q4WFT3 (GUAA_ASPFU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 59. 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
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:gua1
ORF Names:AFUA_3G01110
OrganismNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Taxonomic identifier330879 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus

Protein attributes

Sequence length557 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

ATP + xanthosine 5'-phosphate + L-glutamine + H2O = AMP + diphosphate + GMP + L-glutamate.

Pathway

Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln route): step 1/1.

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Contains 1 glutamine amidotransferase type-1 domain.

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

Ontologies

Keywords
   Biological processGMP biosynthesis
Purine biosynthesis
   Cellular componentCytoplasm
   DomainGlutamine amidotransferase
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processGMP biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

glutamine metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP 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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 557557GMP synthase [glutamine-hydrolyzing]
PRO_0000286144

Regions

Domain13 – 209197Glutamine amidotransferase type-1
Domain210 – 414205GMPS ATP-PPase
Nucleotide binding238 – 2447ATP By similarity

Sites

Active site891For GATase activity By similarity
Active site1831For GATase activity By similarity
Active site1851For GATase activity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q4WFT3 [UniParc].

Last modified July 5, 2005. Version 1.
Checksum: 232BECD7648F3CBF

FASTA55761,432
        10         20         30         40         50         60 
MAEEQNPSAT FDTILTLDFG SQYTHLITRR LREIGVYSEM LPCTQKLADL PFKPKGIILS 

        70         80         90        100        110        120 
GGPYSVYEDG APHADPAVFE LGVPVLGICY GLQEIAYRLG KDNVVAGTAR EYGHADLNAQ 

       130        140        150        160        170        180 
RLDNQGHVDK LFAGLEEHVK VWMSHGDKLV KLPEGFHTIA TTANSEYAGI AHETKPVYGI 

       190        200        210        220        230        240 
QFHPEVTHTP DGAKLLRNFA VDICGANPNW TMSKFVDQEI LRIRKLVGET DHVLGAVSGG 

       250        260        270        280        290        300 
VDSTVAAKLM KEAIGDRFHA VLVNNGCMRL NECETVAETL NKHLGINLTV VDASKRFLDG 

       310        320        330        340        350        360 
LKGVTDPEKK RMFIGATFID VFEEEAEKIE ALAENSGAKV KWFLQGTLYP DVIESISFKG 

       370        380        390        400        410        420 
PSATIKTHHN VGALPKRMIE GQGMKLIEPL RELFKDEVRQ LGRELGIAHE LVMRHPFPGP 

       430        440        450        460        470        480 
GIAIRVLGEV TPERVDIARK ADHIFISMIR EAGLYDKISQ AYAALDPSKA VGVMGDKRVY 

       490        500        510        520        530        540 
AEIIILRAVE TTDCKLTLGI DGDFVLRYII SVMTARAFPF DNEFLSKCAT RIINEVHGVS 

       550 
RVLYDISSKP PATIEME

« Hide

References

[1]"Genomic sequence of the pathogenic and allergenic filamentous fungus Aspergillus fumigatus."
Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L. expand/collapse author list , Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.G., Denning D.W.
Nature 438:1151-1156(2005) [PubMed: 16372009] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AAHF01000010 Genomic DNA. Translation: EAL86394.1.
RefSeqXP_748432.1. XM_743339.1.

3D structure databases

HSSPHSSP built from PDB template 1GPM based on UniProtKB P04079.
ProteinModelPortalQ4WFT3.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ4WFT3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADAFUAT00000194; CADAFUAP00000194; CADAFUAG00000194.
GeneID3505905.
GenomeReviewsGene locus gua1 in contig CM000171_GR.
KEGGafm:AFUA_3G01110.

Phylogenomic databases

eggNOGfuNOG07551.
GeneTreeEFGT00050000004027.
HOGENOMHBG391775.
OMANECETVA.
OrthoDBEOG4WWVST.

Family and domain databases

InterProIPR017926. 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]
Gene3DG3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
KOK01951.
PfamPF00117. GATase. 1 hit.
PF00958. GMP_synt_C. 2 hits.
PF02540. NAD_synthase. 1 hit.
[Graphical view]
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_ASPFU
AccessionPrimary (citable) accession number: Q4WFT3
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 2007
Last sequence update: July 5, 2005
Last modified: January 25, 2012
This is version 59 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents