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B1LL71 (ASNA_ECOSM) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 31. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Aspartate--ammonia ligase

EC=6.3.1.1
Alternative name(s):
Asparagine synthetase A
Gene names
Name:asnA
Ordered Locus Names:EcSMS35_4112
OrganismEscherichia coli (strain SMS-3-5 / SECEC) [Complete proteome] [HAMAP]
Taxonomic identifier439855 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length330 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

ATP + L-aspartate + NH3 = AMP + diphosphate + L-asparagine. HAMAP MF_00555

Pathway

Amino-acid biosynthesis; L-asparagine biosynthesis; L-asparagine from L-aspartate (ammonia route): step 1/1. HAMAP MF_00555

Subcellular location

Cytoplasm By similarity HAMAP MF_00555.

Sequence similarities

Belongs to the class-II aminoacyl-tRNA synthetase family. AsnA subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 330330Aspartate--ammonia ligase HAMAP MF_00555
PRO_1000129118

Sequences

Sequence LengthMass (Da)Tools
B1LL71 [UniParc].

Last modified April 29, 2008. Version 1.
Checksum: 3A440F0BD96746A2

FASTA33036,679
        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 
RVMADGERQF STLKSTVEAI WAGIKATEAA VSEEFGLAPF LPDQIHFVHS QELLSRYPNL 

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

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

       310        320        330 
TMLLLQLPHI GQVQCGVWSA AVRESVPSLL 

« Hide

References

[1]"Insights into the environmental resistance gene pool from the genome sequence of the multidrug-resistant environmental isolate Escherichia coli SMS-3-5."
Fricke W.F., Wright M.S., Lindell A.H., Harkins D.M., Baker-Austin C., Ravel J., Stepanauskas R.
J. Bacteriol. 190:6779-6794(2008) [PubMed: 18708504] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SMS-3-5 / SECEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000970 Genomic DNA. Translation: ACB19526.1.
RefSeqYP_001746074.1. NC_010498.1.

3D structure databases

ProteinModelPortalB1LL71.
SMRB1LL71. Positions 4-330.
ModBaseSearch...

Protein-protein interaction databases

STRINGB1LL71.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000061291; EBESCP00000058933; EBESCG00000060338.
GeneID6144321.
GenomeReviewsGene locus EcSMS35_4112 in contig CP000970_GR.
KEGGecm:EcSMS35_4112.
PATRIC18437148. VBIEscCol6161_4255.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000010820.
HOGENOMHBG288146.
OMALNDNLNG.
ProtClustDBPRK05425.

Enzyme and pathway databases

BioCycECOL439855:ECSMS35_4112-MONOMER.

Family and domain databases

HAMAPMF_00555. AsnA.
[Tree]
InterProIPR006195. aa-tRNA-synth_II.
IPR004618. AsnA.
[Graphical view]
KOK01914.
PfamPF03590. AsnA. 1 hit.
[Graphical view]
PIRSFPIRSF001555. Asp_ammon_ligase. 1 hit.
TIGRFAMsTIGR00669. AsnA. 1 hit.
PROSITEPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameASNA_ECOSM
AccessionPrimary (citable) accession number: B1LL71
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: April 29, 2008
Last modified: January 25, 2012
This is version 31 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families