Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q5ZJU3 (ASNS_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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]

EC=6.3.5.4
Alternative name(s):
Glutamine-dependent asparagine synthetase
Gene names
Name:ASNS
ORF Names:RCJMB04_15l3
OrganismGallus gallus (Chicken) [Reference proteome]
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus

Protein attributes

Sequence length561 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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 – 561560Asparagine synthetase [glutamine-hydrolyzing]
PRO_0000056915

Regions

Domain2 – 191190Glutamine amidotransferase type-2
Domain213 – 536324Asparagine synthetase
Nucleotide binding363 – 3642ATP By similarity
Region49 – 535Glutamine binding By similarity
Region75 – 773Glutamine binding By similarity

Sites

Active site21For GATase activity By similarity
Binding site971Glutamine By similarity
Binding site2561ATP; via carbonyl oxygen By similarity
Binding site2881ATP; via amide nitrogen and carbonyl oxygen By similarity
Site3651Important for beta-aspartyl-AMP intermediate formation By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5ZJU3 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 94EFE934BED58FBF

FASTA56164,097
        10         20         30         40         50         60 
MCGIWALFGS DECLSVQCLS AMKIAHRGPD AFRFENVNGF TNCCFGFHRL AVVDQLYGMQ 

        70         80         90        100        110        120 
PIRVKKFPYL WLCYNGEIYN FKQLQEQFGF EYQTLVDGEV ILHLYNRGGI EQTASMLDGV 

       130        140        150        160        170        180 
FAFILLDTAN RKVFLARDTY GVRPLFKVLT DDGFLGVCSE AKGLINLKHS TSLFPKVEPF 

       190        200        210        220        230        240 
LPGHYEVLDL KPSGKVVSVE VVKFHSYKDE PLHAACDTVG NLPSGFDLET VKSNIRVLFE 

       250        260        270        280        290        300 
NAVRKRLMAH RRIGCLLSGG LDSSLVAAVL LKLMKEMNIK YPLQTFAIGM ENSPDLLAAR 

       310        320        330        340        350        360 
KVAAHIGSEH HEVIFNSEEG IQAVEEVIFS LETYDITTVR ASIGMYLVSK YIRKKTDSVV 

       370        380        390        400        410        420 
IFSGEGSDEL TQGYIYFHKA PSPEEAAEES ERLLKELYLF DVLRADRTTA AHGLELRVPF 

       430        440        450        460        470        480 
LDHRFTSYYL SLPAELRIPK NGIEKYLLRQ SFEDSNLLPK EILWRPKEAF SDGIASVKKS 

       490        500        510        520        530        540 
WFSILQDYID QQVDDLLLEK AAEKYPFNPP RTKESYYYRQ IFEKHYPGRS SWLPHYWMPR 

       550        560 
WVEATDPSAR TLKHYKSAIQ E 

« Hide

References

[1]"Full-length cDNAs from chicken bursal lymphocytes to facilitate gene function analysis."
Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P., Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P., Hayashizaki Y., Buerstedde J.-M.
Genome Biol. 6:R6.1-R6.9(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: CB.
Tissue: Bursa of Fabricius.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ720341 mRNA. Translation: CAG32000.1.
RefSeqNP_001026148.1. NM_001030977.1.
UniGeneGga.22299.

3D structure databases

ProteinModelPortalQ5ZJU3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid681517. 1 interaction.
STRING9031.ENSGALP00000015846.

Proteomic databases

PaxDbQ5ZJU3.
PRIDEQ5ZJU3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID420574.
KEGGgga:420574.

Organism-specific databases

CTD440.

Phylogenomic databases

eggNOGCOG0367.
HOGENOMHOG000027493.
HOVERGENHBG003103.
InParanoidQ5ZJU3.
KOK01953.
PhylomeDBQ5ZJU3.

Enzyme and pathway databases

UniPathwayUPA00134; UER00195.

Family and domain databases

Gene3D3.40.50.620. 1 hit.
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

NextBio20823466.
PROQ5ZJU3.

Entry information

Entry nameASNS_CHICK
AccessionPrimary (citable) accession number: Q5ZJU3
Entry history
Integrated into UniProtKB/Swiss-Prot: September 13, 2005
Last sequence update: January 23, 2007
Last modified: June 11, 2014
This is version 69 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways