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Protein

Probable asparagine synthetase [glutamine-hydrolyzing]

Gene

asn1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Pathway: L-asparagine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes L-asparagine from L-aspartate (L-Gln route).
Proteins known to be involved in this subpathway in this organism are:
  1. Probable asparagine synthetase [glutamine-hydrolyzing] (asn1)
This subpathway is part of the pathway L-asparagine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-asparagine from L-aspartate (L-Gln route), the pathway L-asparagine biosynthesis and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei2 – 21For GATase activityBy similarity
Binding sitei99 – 991GlutamineBy similarity
Binding sitei235 – 2351ATP; via carbonyl oxygenBy similarity
Binding sitei280 – 2801ATP; via amide nitrogen and carbonyl oxygenBy similarity
Sitei356 – 3561Important for beta-aspartyl-AMP intermediate formationBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi354 – 3552ATPBy similarity

GO - Molecular functioni

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

GO - Biological processi

  • asparagine biosynthetic process Source: PomBase
  • 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

ReactomeiREACT_296172. Amino acid synthesis and interconversion (transamination).
UniPathwayiUPA00134; UER00195.

Protein family/group databases

MEROPSiC44.976.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable asparagine synthetase [glutamine-hydrolyzing] (EC:6.3.5.4)
Alternative name(s):
Glutamine-dependent asparagine synthetase
Gene namesi
Name:asn1
ORF Names:SPBC119.10
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
ProteomesiUP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBC119.10.
PomBaseiSPBC119.10. asn1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: PomBase
  • cytosol Source: PomBase
  • nucleus Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Disruption phenotypei

Causes asparagine auxotrophy.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 557556Probable asparagine synthetase [glutamine-hydrolyzing]PRO_0000056916Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei391 – 3911Phosphoserine1 Publication
Modified residuei489 – 4891Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP78753.
PaxDbiP78753.

Interactioni

Protein-protein interaction databases

MINTiMINT-4691132.
STRINGi4896.SPBC119.10.1.

Structurei

3D structure databases

ProteinModelPortaliP78753.
SMRiP78753. Positions 1-529.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 188187Glutamine amidotransferase type-2PROSITE-ProRule annotationAdd
BLAST
Domaini196 – 531336Asparagine synthetaseAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni50 – 545Glutamine bindingBy similarity
Regioni75 – 773Glutamine 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.
HOGENOMiHOG000027493.
InParanoidiP78753.
KOiK01953.
OMAiARKAAHY.
OrthoDBiEOG73JM46.
PhylomeDBiP78753.

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.

P78753-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MCGILAVHHV AEDIEAFKPK ALHLSKQLRH RGPDWSGKAI RNQTILCHER
60 70 80 90 100
LAIVGVESGA QPLVSDDGKL VLTVNGEIYN HLKLRENLKG NYKFKTYSDC
110 120 130 140 150
EVILYLYREH GPACANMLDG MFSWVLYDQD KDKVVAARDP IGITTLYQGF
160 170 180 190 200
SSDSPDTAYF ASELKALHPV CDKIIAFPPG HYYDSETKQT VRYFKPSWWD
210 220 230 240 250
ENKIPSNPVD YKLLRETLEA SVRKRLMAEV PYGVLLSGGL DSSLIASIAA
260 270 280 290 300
RETEKLANST SQSEEARTIT AWPKLHSFAI GLPGSPDLLA ARKVADFLHT
310 320 330 340 350
FHHEHTFTID EGLDALRDVI YHLETYDVTT IRASTPMYLL SRKIKAQGVK
360 370 380 390 400
MVLSGEGSDE IFGGYLYFGN APSREAFHSE CVRRVKNLHL SDCLRANKST
410 420 430 440 450
MAWGLEARVP FLDKDFLEVA LNIDPEEKMY INGRKEKYIL RKAFDTTHDS
460 470 480 490 500
SLQPYLPQDI LWRQKEQFSD GVGYSWIDAL KDTAELCISD DEFALPRREW
510 520 530 540 550
GDDIPTTKEA FWYRKLFDEI FPRQCADTVM RWVPKAEWGC PEDPSGRYQA

GHVAALK
Length:557
Mass (Da):63,241
Last modified:January 23, 2007 - v3
Checksum:iE561EF981A92FBAC
GO

Sequence cautioni

The sequence BAA13764.1 differs from that shown. Reason: Frameshift at position 313. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D89101 mRNA. Translation: BAA13764.1. Frameshift.
CU329671 Genomic DNA. Translation: CAA17925.1.
PIRiT39308.
RefSeqiNP_595291.1. NM_001021198.2.

Genome annotation databases

EnsemblFungiiSPBC119.10.1; SPBC119.10.1:pep; SPBC119.10.
GeneIDi2539704.
KEGGispo:SPBC119.10.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D89101 mRNA. Translation: BAA13764.1. Frameshift.
CU329671 Genomic DNA. Translation: CAA17925.1.
PIRiT39308.
RefSeqiNP_595291.1. NM_001021198.2.

3D structure databases

ProteinModelPortaliP78753.
SMRiP78753. Positions 1-529.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-4691132.
STRINGi4896.SPBC119.10.1.

Protein family/group databases

MEROPSiC44.976.

Proteomic databases

MaxQBiP78753.
PaxDbiP78753.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC119.10.1; SPBC119.10.1:pep; SPBC119.10.
GeneIDi2539704.
KEGGispo:SPBC119.10.

Organism-specific databases

EuPathDBiFungiDB:SPBC119.10.
PomBaseiSPBC119.10. asn1.

Phylogenomic databases

eggNOGiCOG0367.
HOGENOMiHOG000027493.
InParanoidiP78753.
KOiK01953.
OMAiARKAAHY.
OrthoDBiEOG73JM46.
PhylomeDBiP78753.

Enzyme and pathway databases

UniPathwayiUPA00134; UER00195.
ReactomeiREACT_296172. Amino acid synthesis and interconversion (transamination).

Miscellaneous databases

NextBioi20800856.
PROiP78753.

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. "Identification of open reading frames in Schizosaccharomyces pombe cDNAs."
    Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.
    DNA Res. 4:363-369(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: PR745.
  2. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  3. "ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe."
    Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.
    Nat. Biotechnol. 24:841-847(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  4. "Six new amino acid-auxotrophic markers for targeted gene integration and disruption in fission yeast."
    Ma Y., Sugiura R., Saito M., Koike A., Sio S.O., Fujita Y., Takegawa K., Kuno T.
    Curr. Genet. 52:97-105(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-391 AND SER-489, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiASNS_SCHPO
AccessioniPrimary (citable) accession number: P78753
Secondary accession number(s): O42902
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: January 23, 2007
Last modified: June 24, 2015
This is version 110 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families

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.