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C1CXR6 (ASSY_DEIDV) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 37. 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:Deide_00720
OrganismDeinococcus deserti (strain VCD115 / DSM 17065 / LMG 22923) [Complete proteome] [HAMAP]
Taxonomic identifier546414 [NCBI]
Taxonomic lineageBacteriaDeinococcus-ThermusDeinococciDeinococcalesDeinococcaceaeDeinococcus

Protein attributes

Sequence length408 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 – 408408Argininosuccinate synthase HAMAP-Rule MF_00005
PRO_1000201678

Regions

Nucleotide binding9 – 179ATP By similarity

Sites

Binding site361ATP; via amide nitrogen and carbonyl oxygen By similarity
Binding site871Citrulline By similarity
Binding site921Citrulline By similarity
Binding site1171ATP; via amide nitrogen By similarity
Binding site1191Aspartate By similarity
Binding site1231Aspartate By similarity
Binding site1231Citrulline By similarity
Binding site1241Aspartate By similarity
Binding site1271Citrulline By similarity
Binding site1761Citrulline By similarity
Binding site1851Citrulline By similarity
Binding site2611Citrulline By similarity
Binding site2731Citrulline By similarity

Sequences

Sequence LengthMass (Da)Tools
C1CXR6 [UniParc].

Last modified May 26, 2009. Version 1.
Checksum: C79786C440520B27

FASTA40845,133
        10         20         30         40         50         60 
MAKDKIVLAY SGGLDTSIIL KWLQTERNYD VVCFTADLGQ GDEVEEARVK ALNTGAVAAY 

        70         80         90        100        110        120 
ALDLREEFVR DYVFPMFRSS ALYEGYYLLG TSIARPLIAK KMVEIAQKEG AVAVSHGATG 

       130        140        150        160        170        180 
KGNDQVRFEM TAYALQPDIV TVAPWRDWEF QGRADLEAFA HEHGIPVPTT KKDPWSTDAN 

       190        200        210        220        230        240 
MLHISYEGGI LEDPWAEPPA HMFKLTVAPE EAPDEAEYVE IEFLNGDAVA INGETLSPAA 

       250        260        270        280        290        300 
LLDRANEIGG RHGVGRVDLV ENRFVGMKSR GVYETPGGTL LYHARRAVES LTLDREVLHQ 

       310        320        330        340        350        360 
RDALGPKYAE LVYNGFWFAP EREALQVYMD HVAKAVTGTA RLKLYKGNCI VAGRKAERSL 

       370        380        390        400 
YDKDLVSFEA GGDYNQHDAG AFIKLNALRM RVQARVEAKA GQKDKAGD 

« Hide

References

[1]"Alliance of proteomics and genomics to unravel the specificities of Sahara bacterium Deinococcus deserti."
de Groot A., Dulermo R., Ortet P., Blanchard L., Guerin P., Fernandez B., Vacherie B., Dossat C., Jolivet E., Siguier P., Chandler M., Barakat M., Dedieu A., Barbe V., Heulin T., Sommer S., Achouak W., Armengaud J.
PLoS Genet. 5:E1000434-E1000434(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: VCD115 / DSM 17065 / LMG 22923.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001114 Genomic DNA. Translation: ACO44872.1.
RefSeqYP_002784626.1. NC_012526.1.

3D structure databases

ProteinModelPortalC1CXR6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING546414.Deide_00720.

Proteomic databases

PaxDbC1CXR6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACO44872; ACO44872; Deide_00720.
GeneID7739183.
KEGGddr:Deide_00720.
PATRIC21613506. VBIDeiDes121019_0075.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycDDES546414:GHOM-80-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_DEIDV
AccessionPrimary (citable) accession number: C1CXR6
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: May 26, 2009
Last modified: February 19, 2014
This is version 37 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