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Q9RWJ4 (ASSY_DEIRA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 94. 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:DR_0674
OrganismDeinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422) [Reference proteome] [HAMAP]
Taxonomic identifier243230 [NCBI]
Taxonomic lineageBacteriaDeinococcus-ThermusDeinococciDeinococcalesDeinococcaceaeDeinococcus

Protein attributes

Sequence length402 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
Reference 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 – 402402Argininosuccinate synthase HAMAP-Rule MF_00005
PRO_0000148591

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
Q9RWJ4 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 8694AD1424A99835

FASTA40244,877
        10         20         30         40         50         60 
MSKEKIVLAY SGGLDTSIIL KWLQTERNYD VVCFTADLGQ GDEVEEARVK ALNTGAVAAY 

        70         80         90        100        110        120 
ALDLREEFVR DYVFPMMRSS ALYEGYYLLG TSIARPLIAK KMVEIAEKEG AVAISHGATG 

       130        140        150        160        170        180 
KGNDQVRFEM SAYALKPDIV TVAPWRDWDF QGRADLEAFA REHGIPVPTT KKDPWSMDAN 

       190        200        210        220        230        240 
MLHISYEGGP LEDPWTEPPT HMFKLTVNPE DAPSEAEYVE IEYVNGDPVS INGEQLSPAA 

       250        260        270        280        290        300 
LLTKANEIAG RHGVGRIDLV ENRFVGMKSR GVYETPGGTL LYHARRAVES LTLDREVLHQ 

       310        320        330        340        350        360 
RDALGPKYAE LVYNGFWFAP EREALQVYFD HVAKSVTGTA RLKLYKGNCI VAGRKAERSL 

       370        380        390        400 
YDKDLVSFEA GGDYNQHDAG AFIKLNSLRM RVQKRVEDKG KK 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000513 Genomic DNA. Translation: AAF10250.1.
PIRD75490.
RefSeqNP_294397.1. NC_001263.1.

3D structure databases

ProteinModelPortalQ9RWJ4.
SMRQ9RWJ4. Positions 5-397.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243230.DR_0674.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAF10250; AAF10250; DR_0674.
GeneID1798545.
KEGGdra:DR_0674.
PATRIC21628888. VBIDeiRad64572_0850.

Phylogenomic databases

eggNOGCOG0137.
HOGENOMHOG000230093.
KOK01940.
OMAAPPEEAY.
OrthoDBEOG6K9QCV.

Enzyme and pathway databases

BioCycDRAD243230:GH46-695-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_DEIRA
AccessionPrimary (citable) accession number: Q9RWJ4
Entry history
Integrated into UniProtKB/Swiss-Prot: October 19, 2002
Last sequence update: May 1, 2000
Last modified: May 14, 2014
This is version 94 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