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Protein

Phosphoribosylaminoimidazole carboxylase

Gene

ADE2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate = 5-amino-1-(5-phospho-D-ribosyl)imidazole + CO2.

Pathwayi: IMP biosynthesis via de novo pathway

This protein is involved in step 1 of the subpathway that synthesizes 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate from 5-amino-1-(5-phospho-D-ribosyl)imidazole (carboxylase route).
Proteins known to be involved in this subpathway in this organism are:
  1. Phosphoribosylaminoimidazole carboxylase (ADE2)
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-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate from 5-amino-1-(5-phospho-D-ribosyl)imidazole (carboxylase route), the pathway IMP biosynthesis via de novo pathway and in Purine metabolism.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi138 – 19356ATPPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • metal ion binding Source: InterPro
  • phosphoribosylaminoimidazole carboxylase activity Source: SGD

GO - Biological processi

  • 'de novo' IMP biosynthetic process Source: SGD
  • purine nucleobase metabolic process Source: SGD
  • purine nucleotide biosynthetic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Decarboxylase, Lyase

Keywords - Biological processi

Purine biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:YOR128C-MONOMER.
YEAST:YOR128C-MONOMER.
BRENDAi4.1.1.21. 984.
UniPathwayiUPA00074; UER00130.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoribosylaminoimidazole carboxylase (EC:4.1.1.21)
Alternative name(s):
AIR carboxylase
Short name:
AIRC
Gene namesi
Name:ADE2
Ordered Locus Names:YOR128C
ORF Names:O3293, YOR3293C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XV

Organism-specific databases

EuPathDBiFungiDB:YOR128C.
SGDiS000005654. ADE2.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 571571Phosphoribosylaminoimidazole carboxylasePRO_0000075028Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei37 – 371PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP21264.
PeptideAtlasiP21264.
TopDownProteomicsiP21264.

PTM databases

iPTMnetiP21264.

Interactioni

Protein-protein interaction databases

BioGridi34523. 42 interactions.
DIPiDIP-1171N.
IntActiP21264. 11 interactions.
MINTiMINT-387849.

Structurei

3D structure databases

ProteinModelPortaliP21264.
SMRiP21264. Positions 16-376, 403-571.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini110 – 298189ATP-graspPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

In the C-terminal section; belongs to the AIR carboxylase family. Class I subfamily.Curated
Contains 1 ATP-grasp domain.PROSITE-ProRule annotation

Phylogenomic databases

HOGENOMiHOG000034027.
InParanoidiP21264.
KOiK11808.
OMAiACETSQY.
OrthoDBiEOG7FJH8G.

Family and domain databases

Gene3Di3.30.1490.20. 1 hit.
3.30.470.20. 1 hit.
3.40.50.20. 1 hit.
3.40.50.7700. 1 hit.
HAMAPiMF_01928. PurK.
MF_01929. PurE_classI.
InterProiIPR016301. AIR_COase.
IPR011761. ATP-grasp.
IPR003135. ATP-grasp_carboxylate-amine.
IPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR016185. PreATP-grasp_dom.
IPR000031. PurE_dom.
IPR005875. PurK.
IPR011054. Rudment_hybrid_motif.
[Graphical view]
PfamiPF00731. AIRC. 1 hit.
PF02222. ATP-grasp. 1 hit.
[Graphical view]
PIRSFiPIRSF001340. AIR_carboxylase. 1 hit.
SMARTiSM01001. AIRC. 1 hit.
[Graphical view]
SUPFAMiSSF51246. SSF51246. 1 hit.
SSF52255. SSF52255. 1 hit.
SSF52440. SSF52440. 1 hit.
TIGRFAMsiTIGR01162. purE. 1 hit.
TIGR01161. purK. 1 hit.
PROSITEiPS50975. ATP_GRASP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P21264-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDSRTVGILG GGQLGRMIVE AANRLNIKTV ILDAENSPAK QISNSNDHVN
60 70 80 90 100
GSFSNPLDIE KLAEKCDVLT IEIEHVDVPT LKNLQVKHPK LKIYPSPETI
110 120 130 140 150
RLIQDKYIQK EHLIKNGIAV TQSVPVEQAS ETSLLNVGRD LGFPFVLKSR
160 170 180 190 200
TLAYDGRGNF VVKNKEMIPE ALEVLKDRPL YAEKWAPFTK ELAVMIVRSV
210 220 230 240 250
NGLVFSYPIV ETIHKDNICD LCYAPARVPD SVQLKAKLLA ENAIKSFPGC
260 270 280 290 300
GIFGVEMFYL ETGELLINEI APRPHNSGHY TIDACVTSQF EAHLRSILDL
310 320 330 340 350
PMPKNFTSFS TITTNAIMLN VLGDKHTKDK ELETCERALA TPGSSVYLYG
360 370 380 390 400
KESRPNRKVG HINIIASSMA ECEQRLNYIT GRTDIPIKIS VAQKLDLEAM
410 420 430 440 450
VKPLVGIIMG SDSDLPVMSA ACAVLKDFGV PFEVTIVSAH RTPHRMSAYA
460 470 480 490 500
ISASKRGIKT IIAGAGGAAH LPGMVAAMTP LPVIGVPVKG SCLDGVDSLH
510 520 530 540 550
SIVQMPRGVP VATVAINNST NAALLAVRLL GAYDSSYTTK MEQFLLKQEE
560 570
EVLVKAQKLE TVGYEAYLEN K
Length:571
Mass (Da):62,339
Last modified:May 1, 1991 - v1
Checksum:i62D2693916F97AA0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti101 – 1011R → G in AAA34407 (PubMed:1514324).Curated
Sequence conflicti186 – 1861A → G in AAA34407 (PubMed:1514324).Curated
Sequence conflicti206 – 2061S → F in AAA34407 (PubMed:1514324).Curated
Sequence conflicti241 – 25313ENAIK…GCGIF → KMQSNFSRLWYI (PubMed:1514324).CuratedAdd
BLAST
Sequence conflicti387 – 3871I → L in AAA34407 (PubMed:1514324).Curated
Sequence conflicti407 – 4071I → V in AAA34407 (PubMed:1514324).Curated
Sequence conflicti431 – 4311P → T in AAA34407 (PubMed:1514324).Curated
Sequence conflicti434 – 4341V → L in AAA34407 (PubMed:1514324).Curated
Sequence conflicti502 – 5021I → T in AAA34407 (PubMed:1514324).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M59824 Genomic DNA. Translation: AAA34401.1.
M58324 Genomic DNA. Translation: AAA34407.1.
X90518 Genomic DNA. Translation: CAA62125.1.
X94335 Genomic DNA. Translation: CAA64047.1.
Z75036 Genomic DNA. Translation: CAA99327.1.
BK006948 Genomic DNA. Translation: DAA10902.1.
PIRiJN0098. DEBYP.
RefSeqiNP_014771.3. NM_001183547.3.

Genome annotation databases

EnsemblFungiiYOR128C; YOR128C; YOR128C.
GeneIDi854295.
KEGGisce:YOR128C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M59824 Genomic DNA. Translation: AAA34401.1.
M58324 Genomic DNA. Translation: AAA34407.1.
X90518 Genomic DNA. Translation: CAA62125.1.
X94335 Genomic DNA. Translation: CAA64047.1.
Z75036 Genomic DNA. Translation: CAA99327.1.
BK006948 Genomic DNA. Translation: DAA10902.1.
PIRiJN0098. DEBYP.
RefSeqiNP_014771.3. NM_001183547.3.

3D structure databases

ProteinModelPortaliP21264.
SMRiP21264. Positions 16-376, 403-571.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34523. 42 interactions.
DIPiDIP-1171N.
IntActiP21264. 11 interactions.
MINTiMINT-387849.

PTM databases

iPTMnetiP21264.

Proteomic databases

MaxQBiP21264.
PeptideAtlasiP21264.
TopDownProteomicsiP21264.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYOR128C; YOR128C; YOR128C.
GeneIDi854295.
KEGGisce:YOR128C.

Organism-specific databases

EuPathDBiFungiDB:YOR128C.
SGDiS000005654. ADE2.

Phylogenomic databases

HOGENOMiHOG000034027.
InParanoidiP21264.
KOiK11808.
OMAiACETSQY.
OrthoDBiEOG7FJH8G.

Enzyme and pathway databases

UniPathwayiUPA00074; UER00130.
BioCyciMetaCyc:YOR128C-MONOMER.
YEAST:YOR128C-MONOMER.
BRENDAi4.1.1.21. 984.

Miscellaneous databases

NextBioi976290.
PROiP21264.

Family and domain databases

Gene3Di3.30.1490.20. 1 hit.
3.30.470.20. 1 hit.
3.40.50.20. 1 hit.
3.40.50.7700. 1 hit.
HAMAPiMF_01928. PurK.
MF_01929. PurE_classI.
InterProiIPR016301. AIR_COase.
IPR011761. ATP-grasp.
IPR003135. ATP-grasp_carboxylate-amine.
IPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR016185. PreATP-grasp_dom.
IPR000031. PurE_dom.
IPR005875. PurK.
IPR011054. Rudment_hybrid_motif.
[Graphical view]
PfamiPF00731. AIRC. 1 hit.
PF02222. ATP-grasp. 1 hit.
[Graphical view]
PIRSFiPIRSF001340. AIR_carboxylase. 1 hit.
SMARTiSM01001. AIRC. 1 hit.
[Graphical view]
SUPFAMiSSF51246. SSF51246. 1 hit.
SSF52255. SSF52255. 1 hit.
SSF52440. SSF52440. 1 hit.
TIGRFAMsiTIGR01162. purE. 1 hit.
TIGR01161. purK. 1 hit.
PROSITEiPS50975. ATP_GRASP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The ADE2 gene from Saccharomyces cerevisiae: sequence and new vectors."
    Stotz A., Linder P.
    Gene 95:91-98(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Molecular cloning and analysis of autonomous replicating sequence of Candida maltosa."
    Sasnauskas K., Jomantiene R., Lebediene E., Lebedys J., Januska A., Janulaitis A.
    Yeast 8:253-259(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Sequencing and analysis of 51 kb on the right arm of chromosome XV from Saccharomyces cerevisiae reveals 30 open reading frames."
    Wiemann S., Rechmann S., Benes V., Voss H., Schwager C., Vlcek C., Stegemann J., Zimmermann J., Erfle H., Paces V., Ansorge W.
    Yeast 12:281-288(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 96604 / S288c / FY1679.
  4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  5. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
    Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D.
    , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
    Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  6. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  8. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPUR6_YEAST
AccessioniPrimary (citable) accession number: P21264
Secondary accession number(s): D6W2I6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: May 1, 1991
Last modified: May 11, 2016
This is version 159 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 5410 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, 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 XV
    Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names

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 one 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.