P0A8M0 (SYN_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Asparagine--tRNA ligase
EC=6.1.1.22

Alternative name(s):
Asparaginyl-tRNA synthetase
Short name=AsnRS

Gene names

Name:	asnS
Synonyms:	tss
Ordered Locus Names:	b0930, JW0913

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	466 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-asparagine + tRNA(Asn) = AMP + diphosphate + L-asparaginyl-tRNA(Asn). HAMAP MF_00534
Subunit structure	Homodimer.
Subcellular location	Cytoplasm HAMAP MF_00534.
Sequence similarities	Belongs to the class-II aminoacyl-tRNA synthetase family.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Aminoacyl-tRNA synthetase Ligase
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	asparaginyl-tRNA aminoacylation Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW asparagine-tRNA ligase activity Inferred from electronic annotation. Source: EC nucleic acid binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.1 Ref.6
	Chain	2 – 466	465	Asparagine--tRNA ligase HAMAP MF_00534		PRO_0000176406
Natural variations
	Natural variant	231	1	P → L in temperature-sensitive mutant HO202.
Experimental info
	Mutagenesis	426	1	Y → F: No effect.
	Mutagenesis	426	1	Y → S: 15-fold increase in Km for ATP.

Sequences

	Sequence		Length	Mass (Da)
	P0A8M0 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 1E477CB5467B772F	FASTA	466	52,570
	10 20 30 40 50 60 MSVVPVADVL QGRVAVDSEV TVRGWVRTRR DSKAGISFLA VYDGSCFDPV QAVINNSLPN 70 80 90 100 110 120 YNEDVLRLTT GCSVIVTGKV VASPGQGQQF EIQASKVEVA GWVEDPDTYP MAAKRHSIEY 130 140 150 160 170 180 LREVAHLRPR TNLIGAVARV RHTLAQALHR FFNEQGFFWV STPLITASDT EGAGEMFRVS 190 200 210 220 230 240 TLDLENLPRN DQGKVDFDKD FFGKESFLTV SGQLNGETYA CALSKIYTFG PTFRAENSNT 250 260 270 280 290 300 SRHLAEFWML EPEVAFANLN DIAGLAEAML KYVFKAVLEE RADDMKFFAE RVDKDAVSRL 310 320 330 340 350 360 ERFIEADFAQ VDYTDAVTIL ENCGRKFENP VYWGVDLSSE HERYLAEEHF KAPVVVKNYP 370 380 390 400 410 420 KDIKAFYMRL NEDGKTVAAM DVLAPGIGEI IGGSQREERL DVLDERMLEM GLNKEDYWWY 430 440 450 460 RDLRRYGTVP HSGFGLGFER LIAYVTGVQN VRDVIPFPRT PRNASF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Asparaginyl-tRNA synthetase from Escherichia coli has significant sequence homologies with yeast aspartyl-tRNA synthetase." Anselme J., Haertlein M. Gene 84:481-485(1989) [PubMed: 2693216] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-12 AND 243-256. Strain: CE1215.
[2]	"The asparaginyl-tRNA synthetase gene encodes one of the complementing factors for thermosensitive translation in the Escherichia coli mutant strain, N4316." Aoki H., Yaworsky P.J., Patel S.D., Margolin-Brzezinski D., Park K.S., Ganoza M.C. Eur. J. Biochem. 209:511-521(1992) [PubMed: 1425658] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[3]	"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map." Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K. , Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M., Horiuchi T. DNA Res. 3:137-155(1996) [PubMed: 8905232] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[5]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]	"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Link A.J., Robison K., Church G.M. Electrophoresis 18:1259-1313(1997) [PubMed: 9298646] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-13. Strain: K12 / EMG2.
[7]	"Tyr-426 of the Escherichia coli asparaginyl-tRNA synthetase, an amino acid in a C-terminal conserved motif, is involved in ATP binding." Anselme J., Haertlein M. FEBS Lett. 280:163-166(1991) [PubMed: 2009959] [Abstract] Cited for: ATP-BINDING SITE.
[8]	"Asparaginyl-tRNA synthetase from the Escherichia coli temperature-sensitive strain HO202. A proline replacement in motif 2 is responsible for a large increase in Km for asparagine and ATP." Madern D., Anselme J., Haertlein M. FEBS Lett. 299:85-89(1992) [PubMed: 1544480] [Abstract] Cited for: MUTANT TEMPERATURE-SENSITIVE HO202.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M33145 Genomic DNA. Translation: AAA24666.1. X68192 Genomic DNA. Translation: CAA48274.1. U00096 Genomic DNA. Translation: AAC74016.1. AP009048 Genomic DNA. Translation: BAA35682.1.
PIR	SYECNT. JS0396.
RefSeq	NP_415450.1. NC_000913.2.
3D structure databases
ProteinModelPortal	P0A8M0.
SMR	P0A8M0. Positions 6-465.
ModBase	Search...
Protein-protein interaction databases
IntAct	P0A8M0. 3 interactions.
MINT	MINT-1319001.
PTM databases
PhosSite	P0A8M0.
2D gel databases
SWISS-2DPAGE	P0A8M0.
ECO2DBASE	G099.0. 6TH EDITION.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBESCT00000000421; EBESCP00000000421; EBESCG00000000348. EBESCT00000017949; EBESCP00000017240; EBESCG00000017005.
GeneID	945555.
GenomeReviews	Gene locus JW0913 in contig AP009048_GR. Gene locus b0930 in contig U00096_GR.
KEGG	ecj:JW0913. eco:b0930.
PATRIC	32117077. VBIEscCol129921_0963.
Organism-specific databases
EchoBASE	EB0092.
EcoGene	EG10094. asnS.
Phylogenomic databases
eggNOG	COG0017.
GeneTree	EBGT00050000009271.
HOGENOM	HBG745843.
OMA	AIHRFFH.
PhylomeDB	P0A8M0.
ProtClustDB	PRK03932.
Enzyme and pathway databases
BioCyc	EcoCyc:ASNS-MONOMER. MetaCyc:ASNS-MONOMER.
Gene expression databases
Genevestigator	P0A8M0.
Family and domain databases
HAMAP	MF_00534. Asn_tRNA_synth. [Tree]
InterPro	IPR004364. aa-tRNA-synt_II. IPR018150. aa-tRNA-synt_II-like. IPR006195. aa-tRNA-synth_II. IPR004522. Asn-tRNA-synth_IIb. IPR002312. Asp/Asn-tRNA-synth_IIb. IPR012340. NA-bd_OB-fold. IPR016027. NA-bd_OB-fold-like. IPR004365. NA-bd_OB_tRNA-helicase. [Graphical view]
Gene3D	G3DSA:2.40.50.140. OB_NA_bd_sub. 1 hit.
KO	K01893.
PANTHER	PTHR22594. aa-tRNA-synt_II. 1 hit. PTHR22594:SF6. PTHR22594:SF6. 1 hit.
Pfam	PF00152. tRNA-synt_2. 1 hit. PF01336. tRNA_anti. 1 hit. [Graphical view]
PRINTS	PR01042. TRNASYNTHASP.
SUPFAM	SSF50249. Nucleic_acid_OB. 1 hit.
TIGRFAMs	TIGR00457. AsnS. 1 hit.
PROSITE	PS50862. AA_TRNA_LIGASE_II. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYN_ECOLI

Accession

Primary (citable) accession number: P0A8M0
Secondary accession number(s): P17242

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 7, 2005
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 65 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program