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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: -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: IMP biosynthesis via de novo pathway

This protein is involved in step 1 of the subpathway that synthesizes 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).
Proteins known to be involved in this subpathway in this organism are:
  1. Bifunctional purine biosynthesis protein ade10 (ade10)
This subpathway is part of the pathway IMP biosynthesis via de novo pathway, which is itself part of Purine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 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), the pathway IMP biosynthesis via de novo pathway and in Purine metabolism.

Pathwayi: IMP biosynthesis via de novo pathway

This protein is involved in step 1 of the subpathway that synthesizes IMP from 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide.
Proteins known to be involved in this subpathway in this organism are:
  1. Bifunctional purine biosynthesis protein ade10 (ade10)
This subpathway is part of the pathway IMP biosynthesis via de novo pathway, which is itself part of Purine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes IMP from 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide, the pathway IMP biosynthesis via de novo pathway and in Purine metabolism.

GO - Molecular functioni

  • IMP cyclohydrolase activity Source: PomBase
  • phosphoribosylaminoimidazolecarboxamide formyltransferase activity Source: PomBase

GO - Biological processi

  • 'de novo' IMP biosynthetic process Source: PomBase
  • IMP biosynthetic process Source: PomBase

Keywordsi

Molecular functionHydrolase, Multifunctional enzyme, Transferase
Biological processPurine biosynthesis

Enzyme and pathway databases

ReactomeiR-SPO-73817 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
Proteomesi
  • UP000002485 Componenti: Chromosome III

Organism-specific databases

EuPathDBiFungiDB:SPCPB16A4.03c
PomBaseiSPCPB16A4.03c ade10

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001921581 – 585Bifunctional purine biosynthesis protein ade10Add BLAST585

Proteomic databases

MaxQBiO74928
PaxDbiO74928
PRIDEiO74928

PTM databases

iPTMnetiO74928

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

BioGridi276129, 9 interactors
STRINGi4896.SPCPB16A4.03c.1

Structurei

3D structure databases

ProteinModelPortaliO74928
SMRiO74928
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 142MGS-likePROSITE-ProRule annotationAdd BLAST142

Domaini

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

Sequence similaritiesi

Belongs to the PurH family.Curated

Phylogenomic databases

HOGENOMiHOG000230372
InParanoidiO74928
KOiK00602
OMAiDLLFAWK
OrthoDBiEOG092C14JK
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, 1 hit
InterProiView protein in InterPro
IPR024051 AICAR_Tfase_dup_dom_sf
IPR024050 AICAR_Tfase_insert_dom_sf
IPR016193 Cytidine_deaminase-like
IPR011607 MGS-like_dom
IPR036914 MGS-like_dom_sf
IPR002695 PurH-like
PANTHERiPTHR11692 PTHR11692, 1 hit
PfamiView protein in Pfam
PF01808 AICARFT_IMPCHas, 1 hit
PF02142 MGS, 1 hit
PIRSFiPIRSF000414 AICARFT_IMPCHas, 1 hit
SMARTiView protein in SMART
SM00798 AICARFT_IMPCHas, 1 hit
SM00851 MGS, 1 hit
SUPFAMiSSF52335 SSF52335, 1 hit
SSF53927 SSF53927, 1 hit
TIGRFAMsiTIGR00355 purH, 1 hit
PROSITEiView protein in PROSITE
PS51855 MGS, 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)DescriptionActionsGraphical viewLength
Sequence conflicti404K → Q in BAA13904 (PubMed:9501991).Curated1

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

Similar proteinsi

Entry informationi

Entry nameiPUR9_SCHPO
AccessioniPrimary (citable) accession number: O74928
Secondary accession number(s): P78892
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 14, 2001
Last sequence update: November 1, 1998
Last modified: April 25, 2018
This is version 133 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

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