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Protein

Bifunctional purine biosynthesis protein ADE16

Gene

ADE16

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

Functioni

Miscellaneous

Present with 7700 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
  • aerobic respiration Source: SGD
  • ascospore formation Source: SGD
  • purine nucleotide biosynthetic process Source: SGD

Keywordsi

Molecular functionHydrolase, Multifunctional enzyme, Transferase
Biological processPurine biosynthesis

Enzyme and pathway databases

BioCyciMetaCyc:YLR028C-MONOMER
YEAST:YLR028C-MONOMER
UniPathwayiUPA00074; UER00133
UPA00074; UER00135

Names & Taxonomyi

Protein namesi
Recommended name:
Bifunctional purine biosynthesis protein ADE16
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:ADE16
Ordered Locus Names:YLR028C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XII

Organism-specific databases

EuPathDBiFungiDB:YLR028C
SGDiS000004018 ADE16

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_00001921591 – 591Bifunctional purine biosynthesis protein ADE16Add BLAST591

Proteomic databases

MaxQBiP54113
PaxDbiP54113
PRIDEiP54113
TopDownProteomicsiP54113

PTM databases

CarbonylDBiP54113
iPTMnetiP54113

Interactioni

Subunit structurei

Homodimer (Possible).

Binary interactionsi

Show more details

Protein-protein interaction databases

BioGridi31302, 179 interactors
DIPiDIP-4657N
IntActiP54113, 20 interactors
MINTiP54113
STRINGi4932.YLR028C

Structurei

3D structure databases

ProteinModelPortaliP54113
SMRiP54113
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

GeneTreeiENSGT00390000004553
HOGENOMiHOG000230372
InParanoidiP54113
KOiK00602
OMAiHPGKTNL
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.

P54113-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGKYTKTAIL SVYDKTGLLD LAKGLVENNV RILASGGTAN MVREAGFPVD
60 70 80 90 100
DVSSITHAPE MLGGRVKTLH PAVHAGILAR NLEGDEKDLK EQHIDKVDFV
110 120 130 140 150
VCNLYPFKET VAKIGVTVQE AVEEIDIGGV TLLRAAAKNH SRVTILSDPN
160 170 180 190 200
DYSIFLQDLS KDGEISQDLR NRFALKAFEH TADYDAAISD FFRKQYSEGK
210 220 230 240 250
AQLPLRYGCN PHQRPAQAYI TQQEELPFKV LCGTPGYINL LDALNSWPLV
260 270 280 290 300
KELSASLNLP AAASFKHVSP AGAAVGLPLS DVERQVYFVN DMEDLSPLAC
310 320 330 340 350
AYARARGADR MSSFGDFIAL SNIVDVATAK IISKEVSDGV IAPGYEPEAL
360 370 380 390 400
NILSKKKNGK YCILQIDPNY VPGQMESREV FGVTLQQKRN DAIINQSTFK
410 420 430 440 450
EIVSKNKALT EQAVIDLTVA TLVLKYTQSN SVCYAKNGMV VGLGAGQQSR
460 470 480 490 500
IHCTRLAGDK TDNWWLRQHP KVLNMKWAKG IKRADKSNAI DLFVTGQRIE
510 520 530 540 550
GPEKVDYESK FEEVPEPFTK EERLEWLSKL NNVSLSSDAF FPFPDNVYRA
560 570 580 590
VQSGVKFITA PSGSVMDKVV FQAADSFDIV YVENPIRLFH H
Length:591
Mass (Da):65,282
Last modified:October 1, 1996 - v1
Checksum:iDEC06684BFED7CA7
GO

Sequence cautioni

The sequence CAA97551 differs from that shown. Reason: Erroneous translation. Wrong choice of frame.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U62402 Genomic DNA Translation: AAB57774.1
Z73199 Genomic DNA Translation: CAA97551.2 Sequence problems.
Z73200 Genomic DNA Translation: CAA97552.1
BK006945 Genomic DNA Translation: DAA09346.1
PIRiS77707
RefSeqiNP_013128.1, NM_001181915.1

Genome annotation databases

EnsemblFungiiYLR028C; YLR028C; YLR028C
GeneIDi850715
KEGGisce:YLR028C

Similar proteinsi

Entry informationi

Entry nameiPUR91_YEAST
AccessioniPrimary (citable) accession number: P54113
Secondary accession number(s): D6VY30, E9PAG6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: April 25, 2018
This is version 159 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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Main funding by: National Institutes of Health