Reviewed, UniProtKB/Swiss-Prot P49089 (ASNS1_YEAST)

Names and origin

Protein names

Recommended 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

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	572 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Asparagine biosynthesis
Domain	Glutamine amidotransferase
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	asparagine biosynthetic process Ref.1 Inferred from genetic interaction. Source: SGD glutamine metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from direct assay. Source: SGD
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW asparagine synthase (glutamine-hydrolyzing) activity Inferred from direct assay. Source: SGD protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ASN2	P49090	1	EBI-3043,EBI-3048

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 572	571	Asparagine synthetase [glutamine-hydrolyzing] 1		PRO_0000056917
Regions
	Domain	2 – 186	185	Glutamine amidotransferase type-2
	Domain	194 – 546	353	Asparagine synthetase
Sites
	Active site	2	1	For GATase activity By similarity
Amino acid modifications
	Modified residue	204	1	Phosphoserine Ref.3 Ref.4
	Modified residue	205	1	Phosphothreonine Ref.4
	Modified residue	265	1	Phosphoserine Ref.4
	Modified residue	509	1	Phosphoserine Ref.4

Sequences

	Sequence		Length	Mass (Da)
	P49089-1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 39F2873F0E689FC9	FASTA	572	64,470
	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

References

	« Hide 'large scale' referencesShow '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: 8951815] [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. , 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: 9169875] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed: 17563356] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-204, MASS SPECTROMETRY.
[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: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-204; THR-205; SER-265 AND SER-509, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	Z48675 Genomic DNA. Translation: CAA88594.1. U40829 Genomic DNA. Translation: AAB68284.1.
PIR	S52694.
RefSeq	NP_015471.1.
3D structure databases
HSSP	HSSP built from PDB template 1CT9 based on UniProtKB P22106.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:3810N.
IntAct	P49089. 4 interactions.
STRING	P49089.
Protein family/group databases
MEROPS	C44.974.
Proteomic databases
PeptideAtlas	P49089.
PRIDE	P49089.
Genome annotation databases
Ensembl	YPR145W; YPR145W; YPR145W; Saccharomyces cerevisiae. [Genome view]
GeneID	856268.
GenomeReviews	Gene locus YPR145W in contig U00094_GR.
KEGG	sce:YPR145W.
NMPDR	fig|4932.3.peg.6610.
Organism-specific databases
CYGD	YPR145w.
SGD	S000006349. ASN1.
Phylogenomic databases
HOGENOM	P49089.
OMA	FSNEMKC.
Enzyme and pathway databases
BRENDA	6.3.5.4. 250.
Gene expression databases
ArrayExpress	P49089.
Genevestigator	P49089.
GermOnline	YPR145W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR006426. Asn_synth_AEB. IPR001962. Asn_synthase. IPR000583. GATase_2. IPR017932. GATase_II. IPR014729. Rossmann-like_a/b/a_fold. [Graphical view]
Gene3D	G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
Pfam	PF00733. Asn_synthase. 1 hit. PF00310. GATase_2. 1 hit. [Graphical view]
TIGRFAMs	TIGR01536. asn_synth_AEB. 1 hit.
PROSITE	PS51278. GATASE_TYPE_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	981571.

Entry information

Entry name

ASNS1_YEAST

Accession

Primary (citable) accession number: P49089

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	January 23, 2007
Last modified:	November 3, 2009
This is version 88 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)