Aspartate--tRNA ligase - Escherichia coli (strain K12)

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P21889 (SYD_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 122. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Aspartate--tRNA ligase
EC=6.1.1.12

Alternative name(s):
Aspartyl-tRNA synthetase
Short name=AspRS

Gene names

Name:	aspS
Synonyms:	tls
Ordered Locus Names:	b1866, JW1855

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	590 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	ATP + L-aspartate + tRNA(Asp) = AMP + diphosphate + L-aspartyl-tRNA(Asp). HAMAP MF_00044_B
Subunit structure	Homodimer.
Subcellular location	Cytoplasm HAMAP MF_00044_B.
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	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	aspartyl-tRNA aminoacylation Inferred from direct assay. Source: EcoCyc
Cellular component	cytosol Inferred from direct assay. Source: UniProtKB
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW aspartate-tRNA ligase activity Inferred from direct assay. Source: EcoCyc 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

Chain

1 – 590

590

Aspartate--tRNA ligase HAMAP MF_00044_B

PRO_0000110868

Secondary structure

590

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P21889 [UniParc].

Last modified May 1, 1991. Version 1.
Checksum: A411D3E16D3A9284
Show »

FASTA

590

65,913

        10         20         30         40         50         60 
MRTEYCGQLR LSHVGQQVTL CGWVNRRRDL GSLIFIDMRD REGIVQVFFD PDRADALKLA 

        70         80         90        100        110        120 
SELRNEFCIQ VTGTVRARDE KNINRDMATG EIEVLASSLT IINRADVLPL DSNHVNTEEA 

       130        140        150        160        170        180 
RLKYRYLDLR RPEMAQRLKT RAKITSLVRR FMDDHGFLDI ETPMLTKATP EGARDYLVPS 

       190        200        210        220        230        240 
RVHKGKFYAL PQSPQLFKQL LMMSGFDRYY QIVKCFRDED LRADRQPEFT QIDVETSFMT 

       250        260        270        280        290        300 
APQVREVMEA LVRHLWLEVK GVDLGDFPVM TFAEAERRYG SDKPDLRNPM ELTDVADLLK 

       310        320        330        340        350        360 
SVEFAVFAGP ANDPKGRVAA LRVPGGASLT RKQIDEYGNF VKIYGAKGLA YIKVNERAKG 

       370        380        390        400        410        420 
LEGINSPVAK FLNAEIIEDI LDRTAAQDGD MIFFGADNKK IVADAMGALR LKVGKDLGLT 

       430        440        450        460        470        480 
DESKWAPLWV IDFPMFEDDG EGGLTAMHHP FTSPKDMTAA ELKAAPENAV ANAYDMVING 

       490        500        510        520        530        540 
YEVGGGSVRI HNGDMQQTVF GILGINEEEQ REKFGFLLDA LKYGTPPHAG LAFGLDRLTM 

       550        560        570        580        590 
LLTGTDNIRD VIAFPKTTAA ACLMTEAPSF ANPTALAELS IQVVKKAENN

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Aspartyl-tRNA synthetase from Escherichia coli: cloning and characterisation of the gene, homologies of its translated amino acid sequence with asparaginyl- and lysyl-tRNA synthetases." Eriani G., Dirheimer G., Gangloff J. Nucleic Acids Res. 18:7109-7118(1990) [PubMed: 2129559] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[2]	"A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 40.1-50.0 min region on the linkage map." Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S. Horiuchi T. DNA Res. 3:379-392(1996) [PubMed: 9097040] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]	"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.
[4]	"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.
[5]	"Location of a mutation in the aspartyl-tRNA synthetase gene of Escherichia coli K12." Sharples G.J., Lloyd R.G. Mutat. Res. 264:93-96(1991) [PubMed: 1944398] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 382-590. Strain: K12.
[6]	"Molecular analysis of the Escherichia coli ruvC gene, which encodes a Holliday junction-specific endonuclease." Takahagi M., Iwasaki H., Nakata A., Shinagawa H. J. Bacteriol. 173:5747-5753(1991) [PubMed: 1885548] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 461-590.
[7]	"Synthesis of aspartyl-tRNA(Asp) in Escherichia coli - a snapshot of the second step." Eiler S., Dock-Bregeon A.-C., Moulinier L., Thierry J.-C., Moras D. EMBO J. 18:6532-6541(1999) [PubMed: 10562565] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
[8]	"Aspartyl tRNA-synthetase from Escherichia coli: flexibility and adaptability to the substrates." Rees B., Webster G., Delarue M., Boeglin M., Moras D. J. Mol. Biol. 299:1157-1164(2000) [PubMed: 10873442] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X53863 Genomic DNA. Translation: CAA37856.1.
U00096 Genomic DNA. Translation: AAC74936.1.
AP009048 Genomic DNA. Translation: BAA15677.1.
X53984 Genomic DNA. Translation: CAA37932.1.
D10165 Genomic DNA. No translation available.

PIR

SYECD. JT0942.

RefSeq

NP_416380.1. NC_000913.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1C0A	X-ray	2.40	A	1-585	[»]
1EQR	X-ray	2.70	A/B/C	1-590	[»]
1IL2	X-ray	2.60	A/B	1-590	[»]

ProteinModelPortal

P21889.

SMR

P21889. Positions 1-585.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-9182N.

IntAct

P21889. 28 interactions.

MINT

MINT-1249167.

2D gel databases

SWISS-2DPAGE

P21889.

ECO2DBASE

F058.5. 6TH EDITION.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBESCT00000000359; EBESCP00000000359; EBESCG00000000293.
EBESCT00000018446; EBESCP00000017737; EBESCG00000017500.

GeneID

946385.

GenomeReviews

Gene locus JW1855 in contig AP009048_GR.
Gene locus b1866 in contig U00096_GR.

KEGG

ecj:JW1855.
eco:b1866.

PATRIC

32119055. VBIEscCol129921_1945.

Organism-specific databases

EchoBASE

EB0095.

EcoGene

EG10097. aspS.

Phylogenomic databases

eggNOG

COG0173.

GeneTree

EBGT00050000009271.

HOGENOM

HBG396032.

OMA

AFPKTQQ.

PhylomeDB

P21889.

ProtClustDB

PRK00476.

Enzyme and pathway databases

BioCyc

EcoCyc:ASPS-MONOMER.
MetaCyc:ASPS-MONOMER.

Gene expression databases

Genevestigator

P21889.

Family and domain databases

HAMAP

MF_00044_B. Asp_tRNA_synth_B.
[Tree]

InterPro

IPR004364. aa-tRNA-synt_II.
IPR018150. aa-tRNA-synt_II-like.
IPR006195. aa-tRNA-synth_II.
IPR004524. Asp-tRNA-synth_IIb_bac/mt.
IPR002312. Asp/Asn-tRNA-synth_IIb.
IPR004115. GAD_dom.
IPR012340. NA-bd_OB-fold.
IPR016027. NA-bd_OB-fold-like.
IPR004365. NA-bd_OB_tRNA-helicase.
[Graphical view]

Gene3D

G3DSA:3.30.1360.30. GAD_dom. 1 hit.
G3DSA:2.40.50.140. OB_NA_bd_sub. 1 hit.

K01876.

PANTHER

PTHR22594. aa-tRNA-synt_II. 1 hit.
PTHR22594:SF5. AspS_bac. 1 hit.

Pfam

PF02938. GAD. 1 hit.
PF00152. tRNA-synt_2. 1 hit.
PF01336. tRNA_anti. 1 hit.
[Graphical view]

PRINTS

PR01042. TRNASYNTHASP.

SUPFAM

SSF50249. Nucleic_acid_OB. 1 hit.
SSF55261. SSF55261. 1 hit.

TIGRFAMs

TIGR00459. AspS_bact. 1 hit.

PROSITE

PS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P21889.

Entry information

Entry name

SYD_ECOLI

Accession

Primary (citable) accession number: P21889

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1991
Last sequence update:	May 1, 1991
Last modified:	January 25, 2012
This is version 122 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

2D gel databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents