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Reviewed, UniProtKB/Swiss-Prot O74928 (PUR9_SCHPO)

Last modified December 15, 2009. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Bifunctional purine biosynthesis protein ade10
Including the following 2 domains:
    1- Recommended name:
            Phosphoribosylaminoimidazolecarboxamide formyltransferase
              EC=2.1.2.3
        Alternative name(s):
            5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase
            AICAR transformylase
    2- Recommended name:
            IMP cyclohydrolase
              EC=3.5.4.10
        Alternative name(s):
            Inosinicase
            IMP synthetase
            ATIC
Gene names
Name: ade10
ORF Names: SPCPB16A4.03c
OrganismSchizosaccharomyces pombe (Fission yeast) [Complete proteome]
Taxonomic identifier4896 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length585 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Catalytic activity

10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide = tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide.

IMP + H2O = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide.

Pathway

Purine metabolism; IMP biosynthesis via de novo pathway; 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide (10-formyl THF route): step 1/1.

Purine metabolism; IMP biosynthesis via de novo pathway; IMP from 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide: step 1/1.

Subunit structure

Homodimer By similarity.

Domain

The IMP cyclohydrolase activity resides in the N-terminal region By similarity.

Sequence similarities

Belongs to the purH family.

Ontologies

Keywords
   Biological processPurine biosynthesis
   Molecular functionHydrolase
Transferase
   Technical termComplete proteome
Multifunctional enzyme
Gene Ontology (GO)
   Biological processIMP biosynthetic process Ref.1

Inferred from mutant phenotype. Source: GeneDB_SPombe

   Cellular componentcytosol

Inferred from direct assay. Source: GeneDB_SPombe

   Molecular functionIMP cyclohydrolase activity Ref.1

Inferred from mutant phenotype. Source: GeneDB_SPombe

phosphoribosylaminoimidazolecarboxamide formyltransferase activity Ref.1

Inferred from mutant phenotype. Source: GeneDB_SPombe

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 585585Bifunctional purine biosynthesis protein ade10
PRO_0000192158

Experimental info

Sequence conflict4041K → Q in BAA13904. Ref.3

Sequences

Sequence LengthMass (Da)Tools
O74928-1 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: 103031D3F957529F

FASTA58564,123
        10         20         30         40         50         60 
MYALLSVYDK TGLLELAKAL TSKGVKLLGS GGTAKMIRES GMEVADVSSI TNAPEILGGR 

        70         80         90        100        110        120 
VKTLHPAVHG GILARDIPSD EKDLVEQSIE KIDIVVCNLY PFRETIAKPN VTIPEAVEEI 

       130        140        150        160        170        180 
DIGGVTLLRA AAKNHARVTI LSDPADYATF TDKFLSDKLT QDDRNTYALK AFASTASYDA 

       190        200        210        220        230        240 
AITDYFRKQY AAGVDQLTLR YGANPHQSPA QAFMEQGPLP FKVLCGSPGY INLMDALNSW 

       250        260        270        280        290        300 
PLVKELRENI GIPAAASFKH VSPAGAAVGL PLSDVEKKVY FVSDITEFTP LACAYARARG 

       310        320        330        340        350        360 
ADRMSSFGDF IALSDTVDVC TARIISREVS DGVIAPGYEP EALELLKKKK GGKYCVLQMD 

       370        380        390        400        410        420 
PKYVPAEIET RQVYGISLQQ HRNHAKIDFS LFEKVVSKNK DLPKSALIDL VIATTALKYT 

       430        440        450        460        470        480 
QSNSVCYAKN GMVVGLGAGQ QSRIHCNRLA GDKADNWWLR HHPKVLGMQF KKSAKRPEKS 

       490        500        510        520        530        540 
NAIDLYVLDA VPAEGSEREQ WESAFETIPE PLTKKEREEF LATCKDVVCA SDAFFPFPDN 

       550        560        570        580 
IYRLAQSGVK YVAAPGGSVM DQAVRDTANE FNMVFSEIPL RLFHH 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning and sequence analysis of the Schizosaccharomyces pombe ade10+ gene."
Liedtke C., Schmidt H.
Yeast 14:1307-1310(1998) [PubMed: 9802209] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 38366 / 972.
[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: 11859360] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 38366 / 972.
[3]"Identification of open reading frames in Schizosaccharomyces pombe cDNAs."
Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.
DNA Res. 4:363-369(1997) [PubMed: 9501991] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 166-585.
Strain: PR745.

Cross-references

Sequence databases

Y16419 Genomic DNA. Translation: CAA76207.1.
CU329672 Genomic DNA. Translation: CAC39322.1.
D89243 mRNA. Translation: BAA13904.1.
PIRT43150.
RefSeqNP_588027.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGO74928.

Genome annotation databases

GeneID2539569.
GenomeReviewsGene locus ade10 in contig CU329672_GR.
KEGGspo:SPCPB16A4.03c.
NMPDRfig|4896.1.peg.365.

Organism-specific databases

GeneDB_SpombeSPCPB16A4.03c.

Phylogenomic databases

HOGENOMHBG498048.
OMAVVKHVKS.
OrthoDBEOG94BCJN.

Enzyme and pathway databases

BRENDA2.1.2.3. 653.
3.5.4.10. 653.

Gene expression databases

ArrayExpressO74928.

Family and domain databases

InterProIPR002695. AICARFT_IMPCHas.
IPR013982. AICARFT_IMPCHas_formly.
IPR011607. MGS.
[Graphical view]
PANTHERPTHR11692. AICARFT_IMPCHas. 1 hit.
PfamPF01808. AICARFT_IMPCHas. 1 hit.
PF02142. MGS. 1 hit.
[Graphical view]
PIRSFPIRSF000414. AICARFT_IMPCHas. 1 hit.
SMARTSM00798. AICARFT_IMPCHas. 1 hit.
SM00851. MGS. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePUR9_SCHPO
AccessionPrimary (citable) accession number: O74928
Secondary accession number(s): P78892
Entry history
Integrated into UniProtKB/Swiss-Prot: August 14, 2001
Last sequence update: November 1, 1998
Last modified: December 15, 2009
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents