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P41390 (PUR1_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 112. 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:
Amidophosphoribosyltransferase

Short name=ATase
EC=2.4.2.14
Alternative name(s):
Glutamine phosphoribosylpyrophosphate amidotransferase
Gene names
Name:ade4
ORF Names:SPAC4D7.08c
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length533 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O.

Cofactor

Binds 1 magnesium ion per subunit.

Pathway

Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/2.

Sequence similarities

In the C-terminal section; belongs to the purine/pyrimidine phosphoribosyltransferase family.

Contains 1 glutamine amidotransferase type-2 domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 533532Amidophosphoribosyltransferase
PRO_0000139646

Regions

Domain2 – 238237Glutamine amidotransferase type-2

Sites

Active site21For GATase activity By similarity
Metal binding3831Magnesium By similarity
Metal binding3841Magnesium By similarity

Amino acid modifications

Modified residue5061Phosphoserine Ref.3

Sequences

Sequence LengthMass (Da)Tools
P41390 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 53C7C99F30A68B57

FASTA53359,832
        10         20         30         40         50         60 
MCGILALMLA DPHQQACPEI YEGLYSLQHR GQDAAGIVTA GNKGRLYQCK GSGMVADVFS 

        70         80         90        100        110        120 
QHQLRQLVGS MGIGHLRYPT AGSCAHSEAQ PFYVNSPYGL VLGHNGNLIN GPELRRFLDT 

       130        140        150        160        170        180 
EAHRHVNTGS DSELLLNIFA YELQRLDKFR INENDIFEAL RNVYDRVNGG YACVAMIAGL 

       190        200        210        220        230        240 
GVLGFRDPNG IRPLVIGERD TPEGKDYMLA SESVVLTQFG YRTFRDIRPG ECVFIRRSNR 

       250        260        270        280        290        300 
EDILAGFRGP RLFSRQILPC LRFTPDIFEY VYFARPDSVI DGLSVYQSRL NMGEKLAHTI 

       310        320        330        340        350        360 
MKRFGPDYME KIDAVIPVPD SARTSALALA QTAQLPYVEA FIKNRYIGRT FIMPGQQIRR 

       370        380        390        400        410        420 
KSVRRKLNVQ PQEFFDKNVL IVDDSIVRGT TSREIVQMAR ESGAKNVYLA SCAPMITHPH 

       430        440        450        460        470        480 
VYGIDLADCK DLIAYGKTED EVAEAISADG VIYQTLEDLL DSCRTAELTE FEVGLFTGEY 

       490        500        510        520        530 
TTGASKEYLV HLEQMRIANN RARKHSFAED EEREAPEDIS LHNTHSDVTF DFV 

« Hide

References

« Hide 'large scale' references
[1]"The ade4 gene of Schizosaccharomyces pombe: cloning, sequence and regulation."
Ludin K.M., Hilti N., Schweingruber M.E.
Curr. Genet. 25:465-468(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The genome sequence of Schizosaccharomyces pombe."
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. expand/collapse author list , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 972 / ATCC 24843.
[3]"Phosphoproteome analysis of fission yeast."
Wilson-Grady J.T., Villen J., Gygi S.P.
J. Proteome Res. 7:1088-1097(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-506, IDENTIFICATION BY MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X72293 Genomic DNA. Translation: CAA51034.1.
CU329670 Genomic DNA. Translation: CAB11280.1.
PIRS43526.
RefSeqNP_594961.1. NM_001020392.2.

3D structure databases

ProteinModelPortalP41390.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid280040. 3 interactions.
MINTMINT-4690052.
STRING4896.SPAC4D7.08c-1.

Protein family/group databases

MEROPSC44.001.

Proteomic databases

PaxDbP41390.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPAC4D7.08c.1; SPAC4D7.08c.1:pep; SPAC4D7.08c.
GeneID2543626.
KEGGspo:SPAC4D7.08c.

Organism-specific databases

PomBaseSPAC4D7.08c.

Phylogenomic databases

eggNOGCOG0034.
HOGENOMHOG000033687.
KOK00764.
OMAYSPDIFE.
OrthoDBEOG74R20H.
PhylomeDBP41390.

Enzyme and pathway databases

UniPathwayUPA00074; UER00124.

Family and domain databases

InterProIPR005854. Amd_phspho_trans.
IPR017932. GATase_2_dom.
IPR000583. GATase_dom.
IPR000836. PRibTrfase_dom.
[Graphical view]
PfamPF00310. GATase_2. 1 hit.
PF00156. Pribosyltran. 1 hit.
[Graphical view]
PIRSFPIRSF000485. Amd_phspho_trans. 1 hit.
TIGRFAMsTIGR01134. purF. 1 hit.
PROSITEPS51278. GATASE_TYPE_2. 1 hit.
PS00103. PUR_PYR_PR_TRANSFER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20804632.
PROP41390.

Entry information

Entry namePUR1_SCHPO
AccessionPrimary (citable) accession number: P41390
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: April 16, 2014
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways