Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Bifunctional purine biosynthesis protein ADE16

Gene

ADE16

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein 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: SGD
  2. phosphoribosylaminoimidazolecarboxamide formyltransferase activity Source: SGD

GO - Biological processi

  1. 'de novo' IMP biosynthetic process Source: SGD
  2. aerobic respiration Source: SGD
  3. ascospore formation Source: SGD
  4. purine nucleotide biosynthetic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Transferase

Keywords - Biological processi

Purine biosynthesis

Enzyme and pathway databases

BioCyciMetaCyc:YLR028C-MONOMER.
YEAST:YLR028C-MONOMER.
ReactomeiREACT_301060. Purine ribonucleoside monophosphate biosynthesis.
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
ProteomesiUP000002311 Componenti: Chromosome XII

Organism-specific databases

CYGDiYLR028c.
EuPathDBiFungiDB:YLR028C.
SGDiS000004018. ADE16.

Subcellular locationi

GO - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 591591Bifunctional purine biosynthesis protein ADE16PRO_0000192159Add
BLAST

Proteomic databases

MaxQBiP54113.
PaxDbiP54113.
PeptideAtlasiP54113.
PRIDEiP54113.

Expressioni

Gene expression databases

GenevestigatoriP54113.

Interactioni

Subunit structurei

Homodimer (Possible).

Binary interactionsi

WithEntry#Exp.IntActNotes
ADE17P380093EBI-14213,EBI-14223

Protein-protein interaction databases

BioGridi31302. 35 interactions.
DIPiDIP-4657N.
IntActiP54113. 16 interactions.
MINTiMINT-477775.
STRINGi4932.YLR028C.

Structurei

3D structure databases

ProteinModelPortaliP54113.
SMRiP54113. Positions 6-591.
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.
GeneTreeiENSGT00390000004553.
HOGENOMiHOG000230372.
InParanoidiP54113.
KOiK00602.
OMAiSNSVCYV.
OrthoDBiEOG7HXD0J.

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.

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 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.

Cross-referencesi

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.

3D structure databases

ProteinModelPortaliP54113.
SMRiP54113. Positions 6-591.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31302. 35 interactions.
DIPiDIP-4657N.
IntActiP54113. 16 interactions.
MINTiMINT-477775.
STRINGi4932.YLR028C.

Proteomic databases

MaxQBiP54113.
PaxDbiP54113.
PeptideAtlasiP54113.
PRIDEiP54113.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYLR028C; YLR028C; YLR028C.
GeneIDi850715.
KEGGisce:YLR028C.

Organism-specific databases

CYGDiYLR028c.
EuPathDBiFungiDB:YLR028C.
SGDiS000004018. ADE16.

Phylogenomic databases

eggNOGiCOG0138.
GeneTreeiENSGT00390000004553.
HOGENOMiHOG000230372.
InParanoidiP54113.
KOiK00602.
OMAiSNSVCYV.
OrthoDBiEOG7HXD0J.

Enzyme and pathway databases

UniPathwayiUPA00074; UER00133.
UPA00074; UER00135.
BioCyciMetaCyc:YLR028C-MONOMER.
YEAST:YLR028C-MONOMER.
ReactomeiREACT_301060. Purine ribonucleoside monophosphate biosynthesis.

Miscellaneous databases

NextBioi966781.
PROiP54113.

Gene expression databases

GenevestigatoriP54113.

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. Tibbetts A.S., Appling D.R.
    Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
    Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H.
    , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
    Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPUR91_YEAST
AccessioniPrimary (citable) accession number: P54113
Secondary accession number(s): D6VY30, E9PAG6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: April 29, 2015
This is version 131 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 7700 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Multifunctional enzyme, 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 XII
    Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

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.