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Q2YWS4 (ASSY_STAAB) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 60. 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:
Argininosuccinate synthase

EC=6.3.4.5
Alternative name(s):
Citrulline--aspartate ligase
Gene names
Name:argG
Ordered Locus Names:SAB0829c
OrganismStaphylococcus aureus (strain bovine RF122 / ET3-1) [Complete proteome] [HAMAP]
Taxonomic identifier273036 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesStaphylococcus

Protein attributes

Sequence length401 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

ATP + L-citrulline + L-aspartate = AMP + diphosphate + N(omega)-(L-arginino)succinate. HAMAP-Rule MF_00005

Pathway

Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 2/3. HAMAP-Rule MF_00005

Subunit structure

Homotetramer By similarity. HAMAP-Rule MF_00005

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00005.

Sequence similarities

Belongs to the argininosuccinate synthase family. Type 1 subfamily.

Ontologies

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

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

argininosuccinate synthase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 401401Argininosuccinate synthase HAMAP-Rule MF_00005
PRO_0000263975

Regions

Nucleotide binding8 – 169ATP By similarity

Sites

Binding site851Citrulline By similarity
Binding site1151ATP; via amide nitrogen By similarity
Binding site1171Aspartate By similarity
Binding site1211Aspartate By similarity
Binding site1211Citrulline By similarity
Binding site1221Aspartate By similarity
Binding site1251Citrulline By similarity
Binding site1731Citrulline By similarity
Binding site2581Citrulline By similarity
Binding site2701Citrulline By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2YWS4 [UniParc].

Last modified December 20, 2005. Version 1.
Checksum: 75D16CF5EEA44EF0

FASTA40144,448
        10         20         30         40         50         60 
MKEKIVLAYS GGLDTSVAVQ WLIDKGYDVV ACCLDVGEGK DLDIVYKKAL DTGAIECHII 

        70         80         90        100        110        120 
DATKEFSDEY VSYAIKGNLM YENAYPLFSA LSRPLIAKKL VEIAEKTNSV GIAHGCTGKG 

       130        140        150        160        170        180 
NDQVRFEVAI KALNPSLKAF APVREWAWSR EEEIDYAIKH NIPVSINHDS PYSIDQNLWG 

       190        200        210        220        230        240 
RANECGILED PYAAPPEDAF DLTNALEETP DTADEIILTF VKGIPVQIDG KTYELDDLIL 

       250        260        270        280        290        300 
TLNALAGKHG IGRIDHVENR LVGIKSREIY EAPAAEVILK AHKALETITL TKDVAHFKPI 

       310        320        330        340        350        360 
IEKQFAEQLY NGLWFSPLTD SLKLFIDSTQ QYVSGDVRIK LFKGNAIVNG RKSPYTLYDE 

       370        380        390        400 
KLATYTKEDA FNQDAAVGFI DIYGLPTQVN AMLNGGYSNE Q 

« Hide

References

[1]"Molecular correlates of host specialization in Staphylococcus aureus."
Herron-Olson L., Fitzgerald J.R., Musser J.M., Kapur V.
PLoS ONE 2:E1120-E1120(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: bovine RF122 / ET3-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ938182 Genomic DNA. Translation: CAI80517.1.
RefSeqYP_416318.1. NC_007622.1.

3D structure databases

ProteinModelPortalQ2YWS4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING273036.SAB0829c.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAI80517; CAI80517; SAB0829c.
GeneID3794944.
KEGGsab:SAB0829c.
PATRIC19522467. VBIStaAur92441_0884.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0137.
HOGENOMHOG000230093.
KOK01940.
OMAIYNGYWW.
OrthoDBEOG6K9QCV.
ProtClustDBPRK00509.

Enzyme and pathway databases

BioCycSAUR273036:GJVS-849-MONOMER.
UniPathwayUPA00068; UER00113.

Family and domain databases

Gene3D3.40.50.620. 1 hit.
3.90.1260.10. 1 hit.
HAMAPMF_00005. Arg_succ_synth_type1.
InterProIPR001518. Arginosuc_synth.
IPR018223. Arginosuc_synth_CS.
IPR023434. Arginosuc_synth_type_1_subfam.
IPR024074. AS_cat/multimer_dom_body.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PfamPF00764. Arginosuc_synth. 1 hit.
[Graphical view]
TIGRFAMsTIGR00032. argG. 1 hit.
PROSITEPS00564. ARGININOSUCCIN_SYN_1. 1 hit.
PS00565. ARGININOSUCCIN_SYN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameASSY_STAAB
AccessionPrimary (citable) accession number: Q2YWS4
Entry history
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: December 20, 2005
Last modified: February 19, 2014
This is version 60 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