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Protein

Bifunctional purine biosynthesis protein ADE17

Gene

ADE17

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Miscellaneous

Present with 60900 molecules/cell in log phase SD medium.1 Publication

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 ADE16 (ADE16), Bifunctional purine biosynthesis protein ADE17 (ADE17)
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 ADE16 (ADE16), Bifunctional purine biosynthesis protein ADE17 (ADE17)
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: SGD
  • phosphoribosylaminoimidazolecarboxamide formyltransferase activity Source: SGD

GO - Biological processi

  • 'de novo' IMP biosynthetic process Source: SGD
  • purine nucleotide biosynthetic process Source: SGD

Keywordsi

Molecular functionHydrolase, Multifunctional enzyme, Transferase
Biological processPurine biosynthesis

Enzyme and pathway databases

BioCyciMetaCyc:YMR120C-MONOMER
YEAST:YMR120C-MONOMER
UniPathwayiUPA00074; UER00133
UPA00074; UER00135

Names & Taxonomyi

Protein namesi
Recommended name:
Bifunctional purine biosynthesis protein ADE17
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:ADE17
Ordered Locus Names:YMR120C
ORF Names:YM8564.02C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XIII

Organism-specific databases

EuPathDBiFungiDB:YMR120C
SGDiS000004727 ADE17

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_00001921601 – 592Bifunctional purine biosynthesis protein ADE17Add BLAST592

Proteomic databases

MaxQBiP38009
PaxDbiP38009
PRIDEiP38009

PTM databases

iPTMnetiP38009

Interactioni

Subunit structurei

Homodimer (Possible).

Binary interactionsi

WithEntry#Exp.IntActNotes
ADE16P541133EBI-14223,EBI-14213

Protein-protein interaction databases

BioGridi35297, 108 interactors
DIPiDIP-6288N
IntActiP38009, 38 interactors
MINTiP38009
STRINGi4932.YMR120C

Structurei

3D structure databases

ProteinModelPortaliP38009
SMRiP38009
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 147MGS-likePROSITE-ProRule annotationAdd BLAST147

Domaini

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

Sequence similaritiesi

Belongs to the PurH family.Curated

Phylogenomic databases

GeneTreeiENSGT00910000146593
HOGENOMiHOG000230372
InParanoidiP38009
KOiK00602
OMAiDLLFAWK
OrthoDBiEOG092C14JK

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.

P38009-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MANYTKTAIL SVYDKTGLLD LARGLIEKNV RILASGGTAR MIRDAGFPIE
60 70 80 90 100
DVSAITHAPE MLGGRVKTLH PAVHGGILAR DIDSDEKDLK EQHIEKVDYV
110 120 130 140 150
VCNLYPFKET VAKVGVTIPE AVEEIDIGGV TLLRAAAKNH ARVTILSDPK
160 170 180 190 200
DYSEFLSELS SNGEISQDLR NRLALKAFEH TADYDAAISD FFRKQYSEGQ
210 220 230 240 250
AQITLRYGAN PHQKPAQAYV SQQDSLPFKV LCGSPGYINL LDALNSWPLV
260 270 280 290 300
KELSASLNLP AAASFKHVSP AGAAVGIPLS DVEKQVYFVA DIENLSPLAC
310 320 330 340 350
AYARARGADR MSSFGDWIAL SNIVDVPTAK IISREVSDGV IAPGYEPEAL
360 370 380 390 400
AILSKKKGGK YCILQIDPNY VPEAVERRQV YGVTLEQKRN DAIINQSTFK
410 420 430 440 450
EIVSQNKNLT EQAIIDLTVA TIAIKYTQSN SVCYARNGMV VGLGAGQQSR
460 470 480 490 500
IHCTRLAGDK ADNWWFRQHP RVLEIKWAKG VKRPEKSNAI DLFVTGQIPT
510 520 530 540 550
EEPELSEYQS KFEEIPKPFT PEERKEWLSK LTNVSLSSDA FFPFPDNVYR
560 570 580 590
AVKSGVKYIA APSGSVMDKV VFSAADSFDL VYVENPIRLF HH
Length:592
Mass (Da):65,263
Last modified:October 1, 1996 - v2
Checksum:i8ABA71761B512242
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti389R → A AA sequence (PubMed:7895733).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z49273 Genomic DNA Translation: CAA89269.1
BK006946 Genomic DNA Translation: DAA10017.1
PIRiS54489
RefSeqiNP_013839.1, NM_001182621.1

Genome annotation databases

EnsemblFungiiYMR120C; YMR120C; YMR120C
GeneIDi855149
KEGGisce:YMR120C

Similar proteinsi

Entry informationi

Entry nameiPUR92_YEAST
AccessioniPrimary (citable) accession number: P38009
Secondary accession number(s): D6VZU3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1996
Last modified: May 23, 2018
This is version 174 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XIII
    Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names

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