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

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P00963 (ASNA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 124. History...

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

Documents (4) |

Third-party data

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

Names and origin

Protein names

Recommended name:
Aspartate--ammonia ligase
EC=6.3.1.1

Alternative name(s):
Asparagine synthetase A

Gene names

Name:	asnA
Ordered Locus Names:	b3744, JW3722

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	330 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	May amidate Asp of the extracellular death factor precursor Asn-Asn-Trp-Asp-Asn to generate Asn-Asn-Trp-Asn-Asn Probable. Ref.8
Catalytic activity	ATP + L-aspartate + NH₃ = AMP + diphosphate + L-asparagine. HAMAP-Rule MF_00555
Pathway	Amino-acid biosynthesis; L-asparagine biosynthesis; L-asparagine from L-aspartate (ammonia route): step 1/1. HAMAP-Rule MF_00555
Subunit structure	Homodimer.
Subcellular location	Cytoplasm HAMAP-Rule MF_00555.
Disruption phenotype	Loss of production of extracellular death factor. Ref.8
Sequence similarities	Belongs to the class-II aminoacyl-tRNA synthetase family. AsnA subfamily.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Asparagine biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	L-asparagine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway asparagine biosynthetic process Inferred from direct assay PubMed 14490631. Source: EcoCyc response to DNA damage stimulus Inferred from expression pattern PubMed 11967071. Source: EcoliWiki tRNA aminoacylation for protein translation 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: HAMAP aminoacyl-tRNA ligase activity Inferred from electronic annotation. Source: InterPro aspartate-ammonia ligase activity Inferred from direct assay PubMed 4895361. Source: EcoCyc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
serC	P23721	1	EBI-1117481,EBI-557952

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 330

330

Aspartate--ammonia ligase HAMAP-Rule MF_00555

PRO_0000195873

Secondary structure

330

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P00963 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 2A8D2E3ECE523FDD
Show »

FASTA

330

36,651

        10         20         30         40         50         60 
MKTAYIAKQR QISFVKSHFS RQLEERLGLI EVQAPILSRV GDGTQDNLSG CEKAVQVKVK 

        70         80         90        100        110        120 
ALPDAQFEVV HSLAKWKRQT LGQHDFSAGE GLYTHMKALR PDEDRLSPLH SVYVDQWDWE 

       130        140        150        160        170        180 
RVMGDGERQF STLKSTVEAI WAGIKATEAA VSEEFGLAPF LPDQIHFVHS QELLSRYPDL 

       190        200        210        220        230        240 
DAKGRERAIA KDLGAVFLVG IGGKLSDGHR HDVRAPDYDD WSTPSELGHA GLNGDILVWN 

       250        260        270        280        290        300 
PVLEDAFELS SMGIRVDADT LKHQLALTGD EDRLELEWHQ ALLRGEMPQT IGGGIGQSRL 

       310        320        330 
TMLLLQLPHI GQVQCGVWPA AVRESVPSLL

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of the asnA gene coding for asparagine synthetase of E. coli K-12." Nakamura M., Yamada M., Hirota Y., Sugimoto K., Oka A., Takanami M. Nucleic Acids Res. 9:4669-4676(1981) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[2]	"The replication origin region of Escherichia coli: nucleotide sequence and functional units." Buhk H.-J., Messer W. Gene 24:265-279(1983) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"DNA sequence and analysis of 136 kilobases of the Escherichia coli genome: organizational symmetry around the origin of replication." Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R. Genomics 16:551-561(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]	"Structural and functional properties of the Escherichia coli origin of DNA replication." Hirota Y., Yasuda S., Yamada M., Nishimura A., Sugimoto K., Sugisaki H., Oka A., Takanami M. Cold Spring Harb. Symp. Quant. Biol. 43:129-138(1979) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-252.
[7]	"Overexpression and purification of asparagine synthetase from Escherichia coli." Sugiyama A., Kato H., Nishioka T., Oda J. Biosci. Biotechnol. Biochem. 56:376-379(1992) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-5. Strain: K12.
[8]	"A linear pentapeptide is a quorum-sensing factor required for mazEF-mediated cell death in Escherichia coli." Kolodkin-Gal I., Hazan R., Gaathon A., Carmeli S., Engelberg-Kulka H. Science 318:652-655(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PRODUCTION OF EXTRACELLULAR DEATH FACTOR (EDF), DISRUPTION PHENOTYPE.
[9]	"Crystal structure of asparagine synthetase reveals a close evolutionary relationship to class II aminoacyl-tRNA synthetase." Nakatsu T., Kato H., Oda J. Nat. Struct. Biol. 5:15-19(1998) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS). Strain: K12.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

V00263 Genomic DNA. Translation: CAA23512.1. Sequence problems.
K00826 Genomic DNA. Translation: AAA24253.1.
J01657 Genomic DNA. Translation: AAA24248.1.
L10328 Genomic DNA. Translation: AAA62096.1.
U00096 Genomic DNA. Translation: AAC76767.1.
AP009048 Genomic DNA. Translation: BAE77544.1.
M10679 Genomic DNA. Translation: AAA24249.1.

PIR

AJECNA. A01191.

RefSeq

NP_418200.1. NC_000913.2.
YP_006952153.1. NC_019049.1.
YP_491685.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
11AS	X-ray	2.50	A/B	1-330	[»]
12AS	X-ray	2.20	A/B	1-330	[»]

ProteinModelPortal

P00963.

SMR

P00963. Positions 4-330.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-9176N.

IntAct

P00963. 4 interactions.

STRING

511145.b3744.

2D gel databases

SWISS-2DPAGE

P00963.

Proteomic databases

PaxDb

P00963.

PRIDE

P00963.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC76767; AAC76767; b3744.
BAE77544; BAE77544; BAE77544.

GeneID

12934269.
13905103.
948258.

KEGG

ecj:Y75_p3423.
eco:b3744.

PATRIC

32122987. VBIEscCol129921_3869.

Organism-specific databases

EchoBASE

EB0089.

EcoGene

EG10091. asnA.

Phylogenomic databases

eggNOG

COG2502.

HOGENOM

HOG000284502.

K01914.

OMA

QSRICMF.

ProtClustDB

PRK05425.

Enzyme and pathway databases

BioCyc

EcoCyc:ASNSYNA-MONOMER.
ECOL316407:JW3722-MONOMER.
MetaCyc:ASNSYNA-MONOMER.

UniPathway

UPA00134; UER00194.

Gene expression databases

Genevestigator

P00963.

Family and domain databases

HAMAP

MF_00555. AsnA.

InterPro

IPR006195. aa-tRNA-synth_II.
IPR004618. AsnA.
[Graphical view]

Pfam

PF03590. AsnA. 1 hit.
[Graphical view]

PIRSF

PIRSF001555. Asp_ammon_ligase. 1 hit.

TIGRFAMs

TIGR00669. asnA. 1 hit.

PROSITE

PS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

DrugBank

DB00131. Adenosine monophosphate.

EvolutionaryTrace

P00963.

Entry information

Entry name

ASNA_ECOLI

Accession

Primary (citable) accession number: P00963
Secondary accession number(s): Q2M862

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	May 1, 2013
This is version 124 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

Escherichia coli

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

2D gel databases

Proteomic 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