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B2K7I9 (ASNA_YERPB) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 38. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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:YPTS_4168
OrganismYersinia pseudotuberculosis serotype IB (strain PB1/+) [Complete proteome] [HAMAP]
Taxonomic identifier502801 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeYersinia

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-Rule MF_00555

Pathway

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

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00555.

Sequence similarities

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

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Asparagine biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processL-asparagine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

tRNA aminoacylation for protein translation

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

aminoacyl-tRNA ligase activity

Inferred from electronic annotation. Source: InterPro

aspartate-ammonia ligase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 330330Aspartate--ammonia ligase HAMAP-Rule MF_00555
PRO_1000129138

Sequences

Sequence LengthMass (Da)Tools
B2K7I9 [UniParc].

Last modified June 10, 2008. Version 1.
Checksum: 7B11F8E203509300

FASTA33036,828
        10         20         30         40         50         60 
MKKQFIQKQQ QISFVKSFFS RQLEQQLGLI EVQAPILSRV GDGTQDNLSG SEKAVQVKVK 

        70         80         90        100        110        120 
SLPDSTFEVV HSLAKWKRKT LGRFDFGADQ GVYTHMKALR PDEDRLSAIH SVYVDQWDWE 

       130        140        150        160        170        180 
RVMGDGERNL AYLKSTVNKI YAAIKETEAA ISAEFGVKPF LPDHIQFIHS ESLRARFPDL 

       190        200        210        220        230        240 
DAKGRERAIA KELGAVFLIG IGGKLADGQS HDVRAPDYDD WTSPSAEGFS GLNGDIIVWN 

       250        260        270        280        290        300 
PILEDAFEIS SMGIRVDAEA LKRQLALTGD EDRLELEWHQ SLLRGEMPQT IGGGIGQSRL 

       310        320        330 
VMLLLQKQHI GQVQCGVWGP EISEKVDGLL 

« Hide

References

[1]"Complete sequence of Yersinia pseudotuberculosis PB1/+."
Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C., Han C., Tapia R., Schmutz J., Larimer F., Land M., Hauser L. expand/collapse author list , Challacombe J.F., Green L., Lindler L.E., Nikolich M.P., Richardson P.
Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PB1/+.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001048 Genomic DNA. Translation: ACC91111.1.
RefSeqYP_001874568.1. NC_010634.1.

3D structure databases

ProteinModelPortalB2K7I9.
SMRB2K7I9. Positions 5-330.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING502801.YPTS_4168.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACC91111; ACC91111; YPTS_4168.
GeneID6261782.
KEGGypb:YPTS_4168.
PATRIC18656664. VBIYerPse20639_4508.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2502.
HOGENOMHOG000284502.
KOK01914.
OMAQSRICMF.
OrthoDBEOG64V2FB.
ProtClustDBPRK05425.

Enzyme and pathway databases

BioCycYPSE502801:GHIH-4311-MONOMER.
UniPathwayUPA00134; UER00194.

Family and domain databases

HAMAPMF_00555. AsnA.
InterProIPR006195. aa-tRNA-synth_II.
IPR004618. AsnA.
[Graphical view]
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_YERPB
AccessionPrimary (citable) accession number: B2K7I9
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: June 10, 2008
Last modified: February 19, 2014
This is version 38 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways