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P49089 (ASNS1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 129. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Asparagine synthetase [glutamine-hydrolyzing] 1

EC=6.3.5.4
Alternative name(s):
Glutamine-dependent asparagine synthetase 1
Gene names
Name:ASN1
Ordered Locus Names:YPR145W
ORF Names:P9659.3
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length572 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Pathway

Amino-acid biosynthesis; L-asparagine biosynthesis; L-asparagine from L-aspartate (L-Gln route): step 1/1.

Sequence similarities

Contains 1 asparagine synthetase domain.

Contains 1 glutamine amidotransferase type-2 domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 572571Asparagine synthetase [glutamine-hydrolyzing] 1
PRO_0000056917

Regions

Domain2 – 186185Glutamine amidotransferase type-2
Domain194 – 546353Asparagine synthetase
Nucleotide binding366 – 3672ATP By similarity
Region49 – 535Glutamine binding By similarity
Region74 – 763Glutamine binding By similarity

Sites

Active site21For GATase activity By similarity
Binding site971Glutamine By similarity
Binding site2331ATP; via carbonyl oxygen By similarity
Binding site2921ATP; via amide nitrogen and carbonyl oxygen By similarity
Site3681Important for beta-aspartyl-AMP intermediate formation By similarity

Amino acid modifications

Modified residue2651Phosphoserine Ref.4
Modified residue5091Phosphoserine Ref.4

Sequences

Sequence LengthMass (Da)Tools
P49089 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 39F2873F0E689FC9

FASTA57264,470
        10         20         30         40         50         60 
MCGIFAAFRH EDVHRYKPKA LQLSKRIRHR GPDWSGNAIK NSTIFVHERL AIVGVESGAQ 

        70         80         90        100        110        120 
PITSSDGEYM LCVNGEIYNH IQLREECADY EFGTLSDCEP IIPMYLKHDI DAPKYLDGMF 

       130        140        150        160        170        180 
AWTLYDAKQD RIVAARDPIG ITTLYMGRSS ASPKTVYFAS ELKCLTDDCD TITAFPPGHV 

       190        200        210        220        230        240 
YDSKTDKITR YFTPDWLDEK RIPSTPIDYM AIRHSLEKAV RKRLMAEVPY GVLLSGGLDS 

       250        260        270        280        290        300 
SLIASIAARE TAKATNDVEP STYDSKARHL AGIDDDGKLH TAGWTSLHSF AIGLPNAPDL 

       310        320        330        340        350        360 
QAARKVAKFI GSIHHEHTFT LQEGLDALDD VIYHLETYDV TTIRASTPMF LLSRKIKAQG 

       370        380        390        400        410        420 
VKMVLSGEGS DEIFGGYLYF AQAPSAAEFH TESVQRVKNL HLADCLRANK STMAWGLEAR 

       430        440        450        460        470        480 
VPFLDREFLQ LCMNIDPNEK MIKPKEGRIE KYILRKAFDT TGEPDAKPYL PEEILWRQKE 

       490        500        510        520        530        540 
QFSDGVGYSW IDGLKDTAEA VISDEMFASP KAEWGSDIPT TKEAFWYRLK FDALFPQKTV 

       550        560        570 
ADTVMRWIPK ADWGCAEDPS GRYAQIHEKH IE 

« Hide

References

« Hide 'large scale' references
[1]"Cloning of the ASN1 and ASN2 genes encoding asparagine synthetases in Saccharomyces cerevisiae: differential regulation by the CCAAT-box-binding factor."
Dang V.D., Valens M., Bolotin-Fukuhara M., Daignan-Fornier B.
Mol. Microbiol. 22:681-692(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."
Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M. expand/collapse author list , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J.
Nature 387:103-105(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-265 AND SER-509, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[5]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z48675 Genomic DNA. Translation: CAA88594.1.
U40829 Genomic DNA. Translation: AAB68284.1.
BK006949 Genomic DNA. Translation: DAA11558.1.
PIRS52694.
RefSeqNP_015471.1. NM_001184242.1.

3D structure databases

ProteinModelPortalP49089.
SMRP49089. Positions 4-544.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid36314. 27 interactions.
DIPDIP-3810N.
IntActP49089. 3 interactions.
MINTMINT-537542.
STRING4932.YPR145W.

Protein family/group databases

MEROPSC44.976.

Proteomic databases

MaxQBP49089.
PaxDbP49089.
PeptideAtlasP49089.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYPR145W; YPR145W; YPR145W.
GeneID856268.
KEGGsce:YPR145W.

Organism-specific databases

SGDS000006349. ASN1.

Phylogenomic databases

eggNOGCOG0367.
GeneTreeENSGT00390000001994.
HOGENOMHOG000027493.
KOK01953.
OMARAAGHTF.
OrthoDBEOG73JM46.

Enzyme and pathway databases

BioCycYEAST:YPR145W-MONOMER.
UniPathwayUPA00134; UER00195.

Gene expression databases

GenevestigatorP49089.

Family and domain databases

Gene3D3.40.50.620. 2 hits.
3.60.20.10. 1 hit.
InterProIPR006426. 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]
PfamPF00733. Asn_synthase. 1 hit.
PF13537. GATase_7. 1 hit.
[Graphical view]
PIRSFPIRSF001589. Asn_synthetase_glu-h. 1 hit.
SUPFAMSSF56235. SSF56235. 1 hit.
TIGRFAMsTIGR01536. asn_synth_AEB. 1 hit.
PROSITEPS51278. GATASE_TYPE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio981571.
PROP49089.

Entry information

Entry nameASNS1_YEAST
AccessionPrimary (citable) accession number: P49089
Secondary accession number(s): D6W4E2
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: January 23, 2007
Last modified: June 11, 2014
This is version 129 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XVI

Yeast (Saccharomyces cerevisiae) chromosome XVI: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways