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Protein

Asparagine synthetase [glutamine-hydrolyzing] 2

Gene

ASN2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

ATP + L-aspartate + L-glutamine + H2O = AMP + diphosphate + L-asparagine + L-glutamate.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei2 – 21For GATase activityBy similarity
Binding sitei97 – 971GlutamineBy similarity
Binding sitei233 – 2331ATP; via carbonyl oxygenBy similarity
Binding sitei291 – 2911ATP; via amide nitrogen and carbonyl oxygenBy similarity
Sitei367 – 3671Important for beta-aspartyl-AMP intermediate formationBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi365 – 3662ATPBy similarity

GO - Molecular functioni

  • asparagine synthase (glutamine-hydrolyzing) activity Source: SGD
  • ATP binding Source: UniProtKB-KW

GO - Biological processi

  • asparagine biosynthetic process Source: SGD
  • glutamine metabolic process Source: UniProtKB-KW
  • L-asparagine biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Amino-acid biosynthesis, Asparagine biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:YGR124W-MONOMER.
ReactomeiREACT_288999. Amino acid synthesis and interconversion (transamination).
UniPathwayiUPA00134; UER00195.

Protein family/group databases

MEROPSiC44.976.

Names & Taxonomyi

Protein namesi
Recommended name:
Asparagine synthetase [glutamine-hydrolyzing] 2 (EC:6.3.5.4)
Alternative name(s):
Glutamine-dependent asparagine synthetase 2
Gene namesi
Name:ASN2
Ordered Locus Names:YGR124W
ORF Names:G6358
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome VII

Organism-specific databases

EuPathDBiFungiDB:YGR124W.
SGDiS000003356. ASN2.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 572571Asparagine synthetase [glutamine-hydrolyzing] 2PRO_0000056918Add
BLAST

Proteomic databases

MaxQBiP49090.
PaxDbiP49090.
PeptideAtlasiP49090.

2D gel databases

UCD-2DPAGEP49090.

Expressioni

Gene expression databases

GenevestigatoriP49090.

Interactioni

Protein-protein interaction databases

BioGridi33372. 25 interactions.
DIPiDIP-5189N.
IntActiP49090. 4 interactions.
MINTiMINT-501384.
STRINGi4932.YGR124W.

Structurei

3D structure databases

ProteinModelPortaliP49090.
SMRiP49090. Positions 4-543.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 186185Glutamine amidotransferase type-2PROSITE-ProRule annotationAdd
BLAST
Domaini194 – 545352Asparagine synthetaseAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni49 – 535Glutamine bindingBy similarity
Regioni74 – 763Glutamine bindingBy similarity

Sequence similaritiesi

Contains 1 asparagine synthetase domain.Curated
Contains 1 glutamine amidotransferase type-2 domain.PROSITE-ProRule annotation

Keywords - Domaini

Glutamine amidotransferase

Phylogenomic databases

eggNOGiCOG0367.
GeneTreeiENSGT00390000001994.
HOGENOMiHOG000027493.
InParanoidiP49090.
KOiK01953.
OMAiVEPAYAC.
OrthoDBiEOG73JM46.

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
3.60.20.10. 1 hit.
InterProiIPR006426. Asn_synth_AEB.
IPR001962. Asn_synthase.
IPR017932. GATase_2_dom.
IPR000583. GATase_dom.
IPR029055. Ntn_hydrolases_N.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PfamiPF00733. Asn_synthase. 1 hit.
PF13537. GATase_7. 1 hit.
[Graphical view]
SUPFAMiSSF56235. SSF56235. 1 hit.
TIGRFAMsiTIGR01536. asn_synth_AEB. 1 hit.
PROSITEiPS51278. GATASE_TYPE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P49090-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MCGIFAAFKH EDIHNFKPKA LQLSKKIRHR GPDWSGNAVM NSTIFVHERL
60 70 80 90 100
AIVGLDSGAQ PITSADGEYM LGVNGEIYNH IQLREMCSDY KFQTFSDCEP
110 120 130 140 150
IIPLYLEHDI DAPKYLDGMF AFCLYDSKKD RIVAARDPIG VVTLYMGRSS
160 170 180 190 200
QSPETVYFAS ELKCLTDVCD SIISFPPGHV YDSETDKITR YFTPDWLDEK
210 220 230 240 250
RIPSTPVDYH AIRHSLEKAV RKRLMAEVPY GVLLSGGLDS SLIAAIAARE
260 270 280 290 300
TEKANADANE DNNVDEKQLA GIDDQGHLHT SGWSRLHSFA IGLPNAPDLQ
310 320 330 340 350
AARKVAKFIG SIHHEHTFTL QEGLDALDDV IYHLETYDVT TIRASTPMFL
360 370 380 390 400
LSRKIKAQGV KMVLSGEGSD EIFGGYLYFA QAPSAAEFHT ESVQRVKNLH
410 420 430 440 450
LADCLRANKS TMAWGLEARV PFLDKDFLQL CMNIDPNEKM IKPKEGRIEK
460 470 480 490 500
YILRKAFDTT DEPDVKPYLP EEILWRQKEQ FSDGVGYSWI DGLRDTAERA
510 520 530 540 550
ISDAMFANPK ADWGDDIPTT KEAYWYRLKF DAWFPQKTAA DTVMRWIPKA
560 570
DWGCAEDPSG RYAKIHEKHV SA
Length:572
Mass (Da):64,593
Last modified:January 23, 2007 - v2
Checksum:i2809F3F0FEDE4183
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti560 – 5601G → S in AAT92877 (PubMed:17322287).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X83099 Genomic DNA. Translation: CAA58159.1.
Z72909 Genomic DNA. Translation: CAA97135.1.
AY692858 Genomic DNA. Translation: AAT92877.1.
BK006941 Genomic DNA. Translation: DAA08217.1.
PIRiS55982.
RefSeqiNP_011640.1. NM_001181253.1.

Genome annotation databases

EnsemblFungiiYGR124W; YGR124W; YGR124W.
GeneIDi853025.
KEGGisce:YGR124W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X83099 Genomic DNA. Translation: CAA58159.1.
Z72909 Genomic DNA. Translation: CAA97135.1.
AY692858 Genomic DNA. Translation: AAT92877.1.
BK006941 Genomic DNA. Translation: DAA08217.1.
PIRiS55982.
RefSeqiNP_011640.1. NM_001181253.1.

3D structure databases

ProteinModelPortaliP49090.
SMRiP49090. Positions 4-543.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33372. 25 interactions.
DIPiDIP-5189N.
IntActiP49090. 4 interactions.
MINTiMINT-501384.
STRINGi4932.YGR124W.

Protein family/group databases

MEROPSiC44.976.

2D gel databases

UCD-2DPAGEP49090.

Proteomic databases

MaxQBiP49090.
PaxDbiP49090.
PeptideAtlasiP49090.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYGR124W; YGR124W; YGR124W.
GeneIDi853025.
KEGGisce:YGR124W.

Organism-specific databases

EuPathDBiFungiDB:YGR124W.
SGDiS000003356. ASN2.

Phylogenomic databases

eggNOGiCOG0367.
GeneTreeiENSGT00390000001994.
HOGENOMiHOG000027493.
InParanoidiP49090.
KOiK01953.
OMAiVEPAYAC.
OrthoDBiEOG73JM46.

Enzyme and pathway databases

UniPathwayiUPA00134; UER00195.
BioCyciYEAST:YGR124W-MONOMER.
ReactomeiREACT_288999. Amino acid synthesis and interconversion (transamination).

Miscellaneous databases

NextBioi972902.
PROiP49090.

Gene expression databases

GenevestigatoriP49090.

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
3.60.20.10. 1 hit.
InterProiIPR006426. Asn_synth_AEB.
IPR001962. Asn_synthase.
IPR017932. GATase_2_dom.
IPR000583. GATase_dom.
IPR029055. Ntn_hydrolases_N.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PfamiPF00733. Asn_synthase. 1 hit.
PF13537. GATase_7. 1 hit.
[Graphical view]
SUPFAMiSSF56235. SSF56235. 1 hit.
TIGRFAMsiTIGR01536. asn_synth_AEB. 1 hit.
PROSITEiPS51278. GATASE_TYPE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "An 18.3 kb DNA fragment from yeast chromosome VII carries four unknown open reading frames, the gene for an Asn synthase, remnants of Ty and three tRNA genes."
    van Dyck L., Tettelin H., Purnelle B., Goffeau A.
    Yeast 13:171-176(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 96604 / S288c / FY1679.
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
    Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E.
    , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
    Nature 387:81-84(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: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  6. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  7. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
    Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
    Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiASNS2_YEAST
AccessioniPrimary (citable) accession number: P49090
Secondary accession number(s): D6VUQ6, E9P8Y0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: January 23, 2007
Last modified: April 29, 2015
This is version 132 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 58200 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 VII
    Yeast (Saccharomyces cerevisiae) chromosome VII: 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.