Q5ZJU3 (ASNS_CHICK) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Gallus gallus (Chicken) [Reference proteome]

Taxonomic identifier

9031 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Sauropsida › Sauria › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galliformes › Phasianidae › Phasianinae › Gallus

Protein attributes

Sequence length	561 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Asparagine biosynthesis
Domain	Glutamine amidotransferase
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	L-asparagine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway glutamine metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW asparagine synthase (glutamine-hydrolyzing) activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 561	560	Asparagine synthetase [glutamine-hydrolyzing]		PRO_0000056915
Regions
	Domain	2 – 191	190	Glutamine amidotransferase type-2
	Domain	213 – 536	324	Asparagine synthetase
	Nucleotide binding	363 – 364	2	ATP By similarity
	Region	49 – 53	5	Glutamine binding By similarity
	Region	75 – 77	3	Glutamine binding By similarity
Sites
	Active site	2	1	For GATase activity By similarity
	Binding site	97	1	Glutamine By similarity
	Binding site	256	1	ATP; via carbonyl oxygen By similarity
	Binding site	288	1	ATP; via amide nitrogen and carbonyl oxygen By similarity
	Site	365	1	Important for beta-aspartyl-AMP intermediate formation By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5ZJU3 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 94EFE934BED58FBF	FASTA	561	64,097
	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

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.
IPI	IPI00575723.
RefSeq	NP_001026148.1. NM_001030977.1.
UniGene	Gga.22299.
3D structure databases
ProteinModelPortal	Q5ZJU3.
ModBase	Search...
Protein-protein interaction databases
STRING	9031.ENSGALP00000015846.
Proteomic databases
PaxDb	Q5ZJU3.
PRIDE	Q5ZJU3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	420574.
KEGG	gga:420574.
Organism-specific databases
CTD	440.
Phylogenomic databases
eggNOG	COG0367.
HOGENOM	HOG000027493.
HOVERGEN	HBG003103.
InParanoid	Q5ZJU3.
KO	K01953.
OrthoDB	EOG4RV2R2.
Enzyme and pathway databases
UniPathway	UPA00134; UER00195.
Family and domain databases
Gene3D	3.40.50.620. 1 hit.
InterPro	IPR006426. Asn_synth_AEB. IPR001962. Asn_synthase. IPR017932. GATase_2_dom. IPR000583. GATase_dom. IPR014729. Rossmann-like_a/b/a_fold. [Graphical view]
Pfam	PF00733. Asn_synthase. 1 hit. PF13537. GATase_7. 1 hit. [Graphical view]
PIRSF	PIRSF001589. Asn_synthetase_glu-h. 1 hit.
TIGRFAMs	TIGR01536. asn_synth_AEB. 1 hit.
PROSITE	PS51278. GATASE_TYPE_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	20823466.

Entry information

Entry name

ASNS_CHICK

Accession

Primary (citable) accession number: Q5ZJU3

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 13, 2005
Last sequence update:	January 23, 2007
Last modified:	April 3, 2013
This is version 62 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program