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Q18E36 (ASSY_HALWD) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 55. 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:HQ_3711A
OrganismHaloquadratum walsbyi (strain DSM 16790 / HBSQ001) [Complete proteome] [HAMAP]
Taxonomic identifier362976 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaHalobacteriaHalobacterialesHalobacteriaceaeHaloquadratum

Protein attributes

Sequence length397 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 – 397397Argininosuccinate synthase HAMAP-Rule MF_00005
PRO_0000263993

Regions

Nucleotide binding7 – 159ATP By similarity

Sites

Binding site841Citrulline By similarity
Binding site1141ATP; via amide nitrogen By similarity
Binding site1161Aspartate By similarity
Binding site1201Aspartate By similarity
Binding site1201Citrulline By similarity
Binding site1211Aspartate By similarity
Binding site1241Citrulline By similarity
Binding site1701Citrulline By similarity
Binding site1791Citrulline By similarity
Binding site2541Citrulline By similarity
Binding site2661Citrulline By similarity

Sequences

Sequence LengthMass (Da)Tools
Q18E36 [UniParc].

Last modified July 25, 2006. Version 1.
Checksum: 9B940224699A24EB

FASTA39743,158
        10         20         30         40         50         60 
MTRVALAFSG GLDTTVCVSL LKEEYGYDEV IGVTVDVGQP ATEFEEAQAT ADAHGIDLHV 

        70         80         90        100        110        120 
VDATAEFVDL CFDSVRANAT YQGYPLGTAL ARPIIAESIV SVAKAENCDA LAHGCTGKGN 

       130        140        150        160        170        180 
DQLRFEAVWR NSDLTVIAPI RELELTREWE QEYAAEHNLP VQAGNDGVWS IDTNLWSRSI 

       190        200        210        220        230        240 
EGGKLEDPNY TPPEDVYEWT ADPATTTETE LITIGFESGY PVSINDNAHD PVELVETLNE 

       250        260        270        280        290        300 
VAGEHGVGRT DMMEDRMLGL KVRENYEHPA ATTLLNAHKA LEGLVLTKDE RDFKRHIDSE 

       310        320        330        340        350        360 
WAQKGYEGLV DHPLMDALEG FIDATQQRVT GTVTIKFEGG QARPVGRESA AAAYSADAAS 

       370        380        390 
FNTSSIGEIT QQDATGIAKY HGYQGRIANA ATETDTK 

« Hide

References

[1]"The genome of the square archaeon Haloquadratum walsbyi: life at the limits of water activity."
Bolhuis H., Palm P., Wende A., Falb M., Rampp M., Rodriguez-Valera F., Pfeiffer F., Oesterhelt D.
BMC Genomics 7:169-169(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 16790 / HBSQ001.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM180088 Genomic DNA. Translation: CAJ53797.1.
RefSeqYP_659371.1. NC_008212.1.

3D structure databases

ProteinModelPortalQ18E36.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING362976.HQ3711A.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAJ53797; CAJ53797; HQ_3711A.
GeneID4193713.
KEGGhwa:HQ3711A.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0137.
HOGENOMHOG000230093.
KOK01940.
OMAIYNGYWW.
ProtClustDBPRK13820.

Enzyme and pathway databases

BioCycHWAL362976:GJSR-2847-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_HALWD
AccessionPrimary (citable) accession number: Q18E36
Entry history
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: July 25, 2006
Last modified: February 19, 2014
This is version 55 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