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Q8CPU3 (ASSY_STAES) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 76. 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:
Argininosuccinate synthase
EC=6.3.4.5
Alternative name(s):
Citrulline--aspartate ligase
Gene names
Name:argG
Ordered Locus Names:SE_0657
OrganismStaphylococcus epidermidis (strain ATCC 12228) [Complete proteome] [HAMAP]
Taxonomic identifier176280 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Bacillales › Staphylococcus ›

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: HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: HAMAP

argininosuccinate synthase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 401401Argininosuccinate synthase HAMAP-Rule MF_00005
PRO_0000148641

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
Q8CPU3 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: D12C08924EA0C0E7

FASTA40144,742
        10         20         30         40         50         60 
MKDKIVLAYS GGLDTSVAVQ WLIDKGYDVV ACCLDVGEGK DLDVVYQKAL DMGAVECHII 

        70         80         90        100        110        120 
DATKEFSDDY VSYAIKGNLM YENAYPLVSA LSRPLIAKKL VEIAEKTNSI GIAHGCTGKG 

       130        140        150        160        170        180 
NDQVRFEVAI KALNPKLKAF APVREWAWSR EEEIDYAIKH NIPVSINYDS PYSIDQNLWG 

       190        200        210        220        230        240 
RANECGILED PYAAPPEDAF DLTTPLEETP DNADEIILTF KQGIPVQVDG KDYQLDDLIL 

       250        260        270        280        290        300 
YLNQLAGKHG IGRIDHVENR MVGIKSREIY ETPGAEVILK AHKALETITL TKDVAHFKPV 

       310        320        330        340        350        360 
IEKQFSEQIY NGLWFSPLTD SLKLFIDSTQ QYVEGDVRIK LFKGNAIVNG RQSPYTLYDE 

       370        380        390        400 
KLATYTKEDA FNQESAVGFI DIYGLPTQVN ALLHGGYSNE Q

« Hide

References

[1]"Genome-based analysis of virulence genes in a non-biofilm-forming Staphylococcus epidermidis strain (ATCC 12228)."
Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q., Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H., Zhao G.-P., Qu D., Danchin A., Wen Y.-M.
Mol. Microbiol. 49:1577-1593(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 12228.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE015929 Genomic DNA. Translation: AAO04254.1.
RefSeqNP_764212.1. NC_004461.1.

3D structure databases

ProteinModelPortalQ8CPU3.
ModBaseSearch...

Protein-protein interaction databases

STRING176280.SE0657.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAO04254; AAO04254; SE_0657.
GeneID1055838.
KEGGsep:SE0657.
PATRIC19607107. VBIStaEpi113981_0631.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0137.
KOK01940.
OMANDQFRFE.
ProtClustDBPRK00509.

Enzyme and pathway databases

BioCycSEPI176280:GCDG-660-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]
PANTHERPTHR11587. PTHR11587. 1 hit.
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_STAES
AccessionPrimary (citable) accession number: Q8CPU3
Entry history
Integrated into UniProtKB/Swiss-Prot: April 23, 2003
Last sequence update: March 1, 2003
Last modified: May 29, 2013
This is version 76 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

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