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Protein

Bifunctional purine biosynthesis protein ade10

Gene

ade10

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Catalytic activityi

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.

Pathwayi

GO - Molecular functioni

  1. IMP cyclohydrolase activity Source: PomBase
  2. phosphoribosylaminoimidazolecarboxamide formyltransferase activity Source: PomBase

GO - Biological processi

  1. 'de novo' IMP biosynthetic process Source: PomBase
  2. IMP biosynthetic process Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Transferase

Keywords - Biological processi

Purine biosynthesis

Enzyme and pathway databases

ReactomeiREACT_207552. Purine ribonucleoside monophosphate biosynthesis.
UniPathwayiUPA00074; UER00133.
UPA00074; UER00135.

Names & Taxonomyi

Protein namesi
Recommended name:
Bifunctional purine biosynthesis protein ade10
Including the following 2 domains:
Phosphoribosylaminoimidazolecarboxamide formyltransferase (EC:2.1.2.3)
Alternative name(s):
5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase
AICAR transformylase
IMP cyclohydrolase (EC:3.5.4.10)
Alternative name(s):
ATIC
IMP synthase
Inosinicase
Gene namesi
Name:ade10
ORF Names:SPCPB16A4.03c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
ProteomesiUP000002485: Chromosome III

Organism-specific databases

PomBaseiSPCPB16A4.03c.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: PomBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 585585Bifunctional purine biosynthesis protein ade10PRO_0000192158Add
BLAST

Proteomic databases

MaxQBiO74928.
PaxDbiO74928.
PRIDEiO74928.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

BioGridi276129. 11 interactions.
MINTiMINT-4681916.
STRINGi4896.SPCPB16A4.03c-1.

Structurei

3D structure databases

ProteinModelPortaliO74928.
SMRiO74928. Positions 3-585.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

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

Sequence similaritiesi

Belongs to the PurH family.Curated

Phylogenomic databases

eggNOGiCOG0138.
HOGENOMiHOG000230372.
InParanoidiO74928.
KOiK00602.
OMAiTIAQPGC.
OrthoDBiEOG7HXD0J.
PhylomeDBiO74928.

Family and domain databases

Gene3Di1.10.287.440. 1 hit.
3.40.140.20. 3 hits.
3.40.50.1380. 1 hit.
HAMAPiMF_00139. PurH.
InterProiIPR024051. AICAR_Tfase_dom.
IPR024050. AICAR_Tfase_insert_dom.
IPR002695. AICARFT_IMPCHas.
IPR016193. Cytidine_deaminase-like.
IPR011607. MGS-like_dom.
[Graphical view]
PANTHERiPTHR11692. PTHR11692. 1 hit.
PfamiPF01808. AICARFT_IMPCHas. 1 hit.
PF02142. MGS. 1 hit.
[Graphical view]
PIRSFiPIRSF000414. AICARFT_IMPCHas. 1 hit.
SMARTiSM00798. AICARFT_IMPCHas. 1 hit.
SM00851. MGS. 1 hit.
[Graphical view]
SUPFAMiSSF52335. SSF52335. 1 hit.
SSF53927. SSF53927. 1 hit.
TIGRFAMsiTIGR00355. purH. 1 hit.

Sequencei

Sequence statusi: Complete.

O74928-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MYALLSVYDK TGLLELAKAL TSKGVKLLGS GGTAKMIRES GMEVADVSSI
60 70 80 90 100
TNAPEILGGR VKTLHPAVHG GILARDIPSD EKDLVEQSIE KIDIVVCNLY
110 120 130 140 150
PFRETIAKPN VTIPEAVEEI DIGGVTLLRA AAKNHARVTI LSDPADYATF
160 170 180 190 200
TDKFLSDKLT QDDRNTYALK AFASTASYDA AITDYFRKQY AAGVDQLTLR
210 220 230 240 250
YGANPHQSPA QAFMEQGPLP FKVLCGSPGY INLMDALNSW PLVKELRENI
260 270 280 290 300
GIPAAASFKH VSPAGAAVGL PLSDVEKKVY FVSDITEFTP LACAYARARG
310 320 330 340 350
ADRMSSFGDF IALSDTVDVC TARIISREVS DGVIAPGYEP EALELLKKKK
360 370 380 390 400
GGKYCVLQMD PKYVPAEIET RQVYGISLQQ HRNHAKIDFS LFEKVVSKNK
410 420 430 440 450
DLPKSALIDL VIATTALKYT QSNSVCYAKN GMVVGLGAGQ QSRIHCNRLA
460 470 480 490 500
GDKADNWWLR HHPKVLGMQF KKSAKRPEKS NAIDLYVLDA VPAEGSEREQ
510 520 530 540 550
WESAFETIPE PLTKKEREEF LATCKDVVCA SDAFFPFPDN IYRLAQSGVK
560 570 580
YVAAPGGSVM DQAVRDTANE FNMVFSEIPL RLFHH
Length:585
Mass (Da):64,123
Last modified:November 1, 1998 - v1
Checksum:i103031D3F957529F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti404 – 4041K → Q in BAA13904. (PubMed:9501991)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y16419 Genomic DNA. Translation: CAA76207.1.
CU329672 Genomic DNA. Translation: CAC39322.1.
D89243 mRNA. Translation: BAA13904.1.
PIRiT43150.
RefSeqiNP_588027.1. NM_001023018.2.

Genome annotation databases

EnsemblFungiiSPCPB16A4.03c.1; SPCPB16A4.03c.1:pep; SPCPB16A4.03c.
GeneIDi2539569.
KEGGispo:SPCPB16A4.03c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y16419 Genomic DNA. Translation: CAA76207.1.
CU329672 Genomic DNA. Translation: CAC39322.1.
D89243 mRNA. Translation: BAA13904.1.
PIRiT43150.
RefSeqiNP_588027.1. NM_001023018.2.

3D structure databases

ProteinModelPortaliO74928.
SMRiO74928. Positions 3-585.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi276129. 11 interactions.
MINTiMINT-4681916.
STRINGi4896.SPCPB16A4.03c-1.

Proteomic databases

MaxQBiO74928.
PaxDbiO74928.
PRIDEiO74928.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPCPB16A4.03c.1; SPCPB16A4.03c.1:pep; SPCPB16A4.03c.
GeneIDi2539569.
KEGGispo:SPCPB16A4.03c.

Organism-specific databases

PomBaseiSPCPB16A4.03c.

Phylogenomic databases

eggNOGiCOG0138.
HOGENOMiHOG000230372.
InParanoidiO74928.
KOiK00602.
OMAiTIAQPGC.
OrthoDBiEOG7HXD0J.
PhylomeDBiO74928.

Enzyme and pathway databases

UniPathwayiUPA00074; UER00133.
UPA00074; UER00135.
ReactomeiREACT_207552. Purine ribonucleoside monophosphate biosynthesis.

Miscellaneous databases

NextBioi20800728.
PROiO74928.

Family and domain databases

Gene3Di1.10.287.440. 1 hit.
3.40.140.20. 3 hits.
3.40.50.1380. 1 hit.
HAMAPiMF_00139. PurH.
InterProiIPR024051. AICAR_Tfase_dom.
IPR024050. AICAR_Tfase_insert_dom.
IPR002695. AICARFT_IMPCHas.
IPR016193. Cytidine_deaminase-like.
IPR011607. MGS-like_dom.
[Graphical view]
PANTHERiPTHR11692. PTHR11692. 1 hit.
PfamiPF01808. AICARFT_IMPCHas. 1 hit.
PF02142. MGS. 1 hit.
[Graphical view]
PIRSFiPIRSF000414. AICARFT_IMPCHas. 1 hit.
SMARTiSM00798. AICARFT_IMPCHas. 1 hit.
SM00851. MGS. 1 hit.
[Graphical view]
SUPFAMiSSF52335. SSF52335. 1 hit.
SSF53927. SSF53927. 1 hit.
TIGRFAMsiTIGR00355. purH. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and sequence analysis of the Schizosaccharomyces pombe ade10+ gene."
    Liedtke C., Schmidt H.
    Yeast 14:1307-1310(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  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.
    , 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. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 166-585.
    Strain: PR745.

Entry informationi

Entry nameiPUR9_SCHPO
AccessioniPrimary (citable) accession number: O74928
Secondary accession number(s): P78892
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 14, 2001
Last sequence update: November 1, 1998
Last modified: January 7, 2015
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.