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B9DIU4 (ASSY_STACT) 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:
Argininosuccinate synthase

EC=6.3.4.5
Alternative name(s):
Citrulline--aspartate ligase
Gene names
Name:argG
Ordered Locus Names:Sca_0569
OrganismStaphylococcus carnosus (strain TM300) [Complete proteome] [HAMAP]
Taxonomic identifier396513 [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_1000116292

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
B9DIU4 [UniParc].

Last modified March 24, 2009. Version 1.
Checksum: 40B40D6BAEF8F16A

FASTA40144,697
        10         20         30         40         50         60 
MKEKIVLAYS GGLDTSVAVQ WLIDKGYDVV ACCLDVGEGK DLDEVYQKAL DMGAIECYII 

        70         80         90        100        110        120 
DATEEFSDEY VSYAIKGNLM YENTYPVVSA LSRPLISKKL VEIAEKTDAV GIAHGCTGKG 

       130        140        150        160        170        180 
NDQVRFEVAI KALNPELKVF APVRAWGWSR EEEIDYAIQH NIPVPINHDS PYSIDQNLWG 

       190        200        210        220        230        240 
RANECGILED PYAAPPADAF DLTREIEDTP DTPDEIVIHF EKGLPVSIDD KAFPLDELIL 

       250        260        270        280        290        300 
YLNDLAGKHG IGRIDHVENR LVGIKSREIY ETPGAEVILK AHKALETITL TKDVAHFKPV 

       310        320        330        340        350        360 
IEKQFAEQTY NGLWFSPLTD SLKLFIDSTQ EHVTGDVRVK LFKGNATVNG RRSPYSLYNE 

       370        380        390        400 
KLATYTKEDA FNQEAAVGFI EIYGLPTEVN SMLHGGYSNE Q 

« Hide

References

[1]"Genome analysis of the meat starter culture bacterium Staphylococcus carnosus TM300."
Rosenstein R., Nerz C., Biswas L., Resch A., Raddatz G., Schuster S.C., Goetz F.
Appl. Environ. Microbiol. 75:811-822(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: TM300.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM295250 Genomic DNA. Translation: CAL27483.1.
RefSeqYP_002633668.1. NC_012121.1.

3D structure databases

ProteinModelPortalB9DIU4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING396513.Sca_0569.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID7551414.
KEGGsca:Sca_0569.
PATRIC19601910. VBIStaCar105558_0572.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycSCAR396513:GJ9G-585-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_STACT
AccessionPrimary (citable) accession number: B9DIU4
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 24, 2009
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