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

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Reviewed, UniProtKB/Swiss-Prot P00963 (ASNA_ECOLI)

Last modified November 25, 2008. Version 86. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

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Protein attributes

Sequence length	330 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Catalytic activity	ATP + L-aspartate + NH(3) = AMP + diphosphate + L-asparagine.
Pathway	Amino-acid biosynthesis; L-asparagine biosynthesis; L-asparagine from L-aspartate (ammonia route): step 1/1.
Subunit structure	Homodimer.
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the class-II aminoacyl-tRNA synthetase family. AsnA subfamily.

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Ontologies

Keywords
Biological process	Amino-acid biosynthesis Asparagine biosynthesis
Cellular component	Cytoplasm
Molecular function	Ligase
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	asparagine biosynthetic process Inferred from electronic annotation. Source: HAMAP tRNA aminoacylation for protein translation Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: HAMAP
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 electronic annotation. Source: HAMAP protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

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Binary interactions

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

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 330

330

Aspartate--ammonia ligase

PRO_0000195873

Secondary structure

330

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P00963-1 [UniParc].

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

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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: 6117826] [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: 6357950] [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: 7686882] [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: 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]	"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: 383377] [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: 1369484] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-5. Strain: K12.
[8]	"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: 9437423] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS). Strain: K12.

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Cross-references

Sequence databases

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

AP_004043.1.
NP_418200.1.

3D structure databases

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	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:9176N.

IntAct

P00963.

2-D gel databases

SWISS-2DPAGE

P00963.

Genome annotation databases

GeneID

948258.

GenomeReviews

Gene locus b3744 in contig U00096_GR.
Gene locus JW3722 in contig AP009048_GR.

KEGG

ecj:JW3722.
eco:b3744.

Organism-specific databases

EchoBASE

EB0089.

EcoGene

EG10091. asnA.

CMR

Search...

Phylogenomic databases

HOGENOM

P00963.

Enzyme and pathway databases

BioCyc

EcoCyc:ASNSYNA-MON.
MetaCyc:ASNSYNA-MON.

Family and domain databases

HAMAP

MF_00555.
[Tree]

InterPro

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

Pfam

PF03590. AsnA. 1 hit.
[Graphical view]

PIRSF

PIRSF001555. Asp_ammon_ligase. 1 hit.

ProDom

PD024629. AsnA. 1 hit.
[Graphical view] [Entries sharing at least one domain]

TIGRFAMs

TIGR00669. asnA. 1 hit.

PROSITE

PS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

DrugBank

DB00131. Adenosine monophosphate.

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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:	November 25, 2008
This is version 86 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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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 and origin

Protein attributes

General annotation (Comments)

Ontologies

Keywords

Gene Ontology (GO)

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

2-D gel databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Other Resources

Entry information

Relevant documents