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Q5APF2 (GUAA_CANAL) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 58. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:GUA1
ORF Names:CaO19.4813, CaO19.12276
OrganismCandida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Taxonomic identifier237561 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesmitosporic SaccharomycetalesCandida

Protein attributes

Sequence length530 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
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

soluble fraction

Inferred from direct assay. Source: CGD

   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 – 530530GMP synthase [glutamine-hydrolyzing]
PRO_0000286146

Regions

Domain18 – 207190Glutamine amidotransferase type-1
Domain208 – 405198GMPS ATP-PPase
Nucleotide binding236 – 2427ATP By similarity

Sites

Active site941For GATase activity By similarity
Active site1811For GATase activity By similarity
Active site1831For GATase activity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5APF2 [UniParc].

Last modified April 26, 2005. Version 1.
Checksum: 87BCD288C209DF46

FASTA53058,813
        10         20         30         40         50         60 
MSANIDDVPI EVSKVFDTIL VLDFGSQYSH LITRRLREFN VYAEMLPCTQ KIAELSWKPK 

        70         80         90        100        110        120 
GIILSGGPYS VYAEDAPHVD HDIFKLGVPI LGICYGMQEL AWINGKGVAR GDKREYGPAT 

       130        140        150        160        170        180 
LNVEDPECAL FKGVDHSQVW MSHGDKLHAL PTGFKVVATS DNSPFCGISN ESEHIYGIQF 

       190        200        210        220        230        240 
HPEVTHTVQG KKLLKNFAVD ICQAKTNWSM ENFIDTEIAR IKKLVGPTAE VIGAVSGGVD 

       250        260        270        280        290        300 
STVGAKIMKE AIGDRFHAIY VDNGVMRKNE TESVKKTLDE GLGINLTVVD AGDLFLGRLK 

       310        320        330        340        350        360 
GVTDPEKKRK IIGNTFIHVF EEEAAKIKPR DGSEIEYLLQ GTLYPDVIES ISFKGPSQTI 

       370        380        390        400        410        420 
KTHHNVGGLL EDMKLKLIEP LRELFKDEVR HLGELLGVPE DLVWRHPFPG PGLAIRVLGE 

       430        440        450        460        470        480 
VTKEQVKIAR EADAIFIEEI KKAGLYRQIS QAFAALLPVK SVGVMGDQRT YEQVIALRAI 

       490        500        510        520        530 
ETLDFMTADW FIFEAAFLKK VASRIVNEVD GVARVTYDIT SKPPATVEWE 

« Hide

References

[1]"The diploid genome sequence of Candida albicans."
Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B., Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W., Scherer S.
Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004) [PubMed: 15123810] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SC5314 / ATCC MYA-2876.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AACQ01000002 Genomic DNA. Translation: EAL04605.1.
AACQ01000001 Genomic DNA. Translation: EAL04801.1.
RefSeqXP_723309.1. XM_718216.1.
XP_723499.1. XM_718406.1.

3D structure databases

HSSPHSSP built from PDB template 1GPM based on UniProtKB P04079.
ProteinModelPortalQ5APF2.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ5APF2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3634763.
3634968.
KEGGcal:CaO19.12276.
cal:CaO19.4813.

Organism-specific databases

CGDCAL0005313. GUA1.

Phylogenomic databases

OMADGRTYEY.
PhylomeDBQ5APF2.

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. 1 hit.
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_CANAL
AccessionPrimary (citable) accession number: Q5APF2
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 2007
Last sequence update: April 26, 2005
Last modified: January 25, 2012
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Candida albicans

Candida albicans: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families