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Q8TGG8 (GDA1_ASPFU) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Probable guanosine-diphosphatase
Short name=GDPase
EC=3.6.1.42
Gene names
Name:gda1
ORF Names:AfA14E5.03c, AFUA_1G12150
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 length503 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

After transfer of sugars to endogenous macromolecular acceptors, the enzyme converts nucleoside diphosphates to nucleoside monophosphates which in turn exit the Golgi lumen in a coupled antiporter reaction, allowing entry of additional nucleotide sugar from the cytosol By similarity.

Catalytic activity

GDP + H2O = GMP + phosphate.

Pathway

Protein modification; protein glycosylation.

Subcellular location

Golgi apparatus membrane; Single-pass type II membrane protein By similarity.

Sequence similarities

Belongs to the GDA1/CD39 NTPase family.

Sequence caution

The sequence CAD27295.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Cellular componentGolgi apparatus
Membrane
   DomainSignal-anchor
Transmembrane
Transmembrane helix
   Molecular functionHydrolase
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processprotein modification process

Inferred from electronic annotation. Source: InterPro

   Cellular componentGolgi membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionguanosine-diphosphatase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 503503Probable guanosine-diphosphatase
PRO_0000209915

Regions

Topological domain1 – 88Cytoplasmic Potential
Transmembrane9 – 2618Helical; Signal-anchor for type II membrane protein; Potential
Topological domain27 – 503477Lumenal Potential

Sites

Active site1941Proton acceptor By similarity

Amino acid modifications

Glycosylation3181N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q8TGG8 [UniParc].

Last modified December 6, 2005. Version 2.
Checksum: E49D642FA86CA04D

FASTA50355,250
        10         20         30         40         50         60 
MAQTQRSRYL KTGAIVAALL LMLLWISPSR PMHPSFPQGQ PSTSAPAKGK CSKPHDPKKP 

        70         80         90        100        110        120 
LIQYALMIDA GSQGSRIHVY RFNNCGPSPE LEDEVFFQTE PKKGGSGLSS YKEDAEGAAK 

       130        140        150        160        170        180 
SLDPLMEVAM KNVPDEYKSC SPIAVKATAG LRMLGPELSQ KILDAVRNRL ETVYPFPVVS 

       190        200        210        220        230        240 
KEKGGVEIMD GSDEGVYAWI TTNYLLGKIG GPDETPTAAV FDLGGGSTQI VFQPTFPKSK 

       250        260        270        280        290        300 
SGGMPERLSE GDHKYDLQFG GRHFELYQHS HLGYGLMAAR KAIHTSIIEN MLASSPKDLS 

       310        320        330        340        350        360 
WLKQPIPNPC IGPEMEKNVT LEFPEGHKLA PEVQVTMVGP KVGSTAAQCR GLAEKTLNKE 

       370        380        390        400        410        420 
AACTLAPCSF NGVHQPSLEK TFAREDVYIF SYFYDRTKPL GMPDSFTLDE LHQLTSTVCG 

       430        440        450        460        470        480 
GEDSWGIFAG IEGALKELRD RPEWCLDLNF MMSLLHTGYE MPLSREVKIA KKIKNRELGW 

       490        500 
CLGASLPLLS QESGWTCRIK EVS

« Hide

References

[1]"Insight into the genome of Aspergillus fumigatus: analysis of a 922 kb region encompassing the nitrate assimilation gene cluster."
Pain A., Woodward J.R., Quail M.A., Anderson M.J., Clark R., Collins M., Fosker N., Fraser A., Harris D.E., Larke N., Murphy L.D., Humphray S., O'Neil S., Pertea M., Price C., Rabbinowitsch E., Rajandream M.A., Salzberg S.L. expand/collapse author list , Saunders D., Seeger K., Sharp S., Warren T., Denning D.W., Barrell B.G., Hall N.
Fungal Genet. Biol. 41:443-453(2004) [PubMed: 14998527] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100.
[2]"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		AL683874 Genomic DNA. Translation: CAD27295.1. Different initiation.
BX649605 Genomic DNA. Translation: CAE47942.1.
AAHF01000004 Genomic DNA. Translation: EAL90545.1.
RefSeqXP_752583.1. XM_747490.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ8TGG8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADAFUAT00007135; CADAFUAP00007135; CADAFUAG00007135.
GeneID3510633.
GenomeReviewsGene locus gda1 in contig CM000169_GR.
KEGGafm:AFUA_1G12150.

Phylogenomic databases

eggNOGfuNOG05233.
GeneTreeEFGT00050000004211.
HOGENOMHBG736908.
OMAIDISANT.
OrthoDBEOG447K2K.

Family and domain databases

InterProIPR000407. GDA1_CD39_NTPase.
IPR015605. Guanosine_diphosphatase.
[Graphical view]
KOK01526.
PANTHERPTHR11782. GDA1_CD39_NTPase. 1 hit.
PTHR11782:SF9. Gda1p. 1 hit.
PfamPF01150. GDA1_CD39. 1 hit.
[Graphical view]
PROSITEPS01238. GDA1_CD39_NTPASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGDA1_ASPFU
AccessionPrimary (citable) accession number: Q8TGG8
Secondary accession number(s): Q4WSN7, Q6MYR7
Entry history
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: December 6, 2005
Last modified: December 14, 2011
This is version 65 of the entry and version 2 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