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Q93JQ8 (ASSY_RHOFA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 58. 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
Synonyms:attB
OrganismRhodococcus fascians
Taxonomic identifier1828 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Nocardiaceae › Rhodococcus

Protein attributes

Sequence length395 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.

Subcellular location

Cytoplasm By similarity.

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
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 – 395395Argininosuccinate synthase HAMAP-Rule MF_00005
PRO_0000148632

Regions

Nucleotide binding6 – 149ATP By similarity

Sites

Binding site331ATP; via amide nitrogen and carbonyl oxygen By similarity
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 site1731Citrulline By similarity
Binding site1821Citrulline By similarity
Binding site2581Citrulline By similarity
Binding site2701Citrulline By similarity

Sequences

Sequence LengthMass (Da)Tools
Q93JQ8 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 851FA5BDD147AFDA

FASTA39542,769
        10         20         30         40         50         60 
MSIVLAYSGG LDTSVAVHWL KERYQTEVIA YCANLGQIED LEAVSKRATA AGASEVIVED 

        70         80         90        100        110        120 
VRDLFLHDYA IPALAAGAAY EGKYLLAAPL SRPLIAERLV SIARERGASA VAHGATGKGN 

       130        140        150        160        170        180 
DQVRFYTSVR ALAPELDILA PVIDWEMTSR GSEIAYADRH GIDVGVSKTT PYSIDTNIWG 

       190        200        210        220        230        240 
TSIECGDLDL IDHAPPPDAW QITTAPVQAP DRPTTITIEF EAGIPVALDG RKLDLIDLVS 

       250        260        270        280        290        300 
ELGDTAAANG IGRTEILESR IVGFKSRGIY EAPAATVLLA ARTDLEALVL DRETLHHKRS 

       310        320        330        340        350        360 
IADQYAELVY YGYWFTDLRA ALDAYCARLA HRVTGTVTVE LYKGSARCIG RTSPKYGRYS 

       370        380        390 
SALADYEEAD TFLHEAGAGF AYCWALPLTE GVVTR

« Hide

References

[1]"The att locus of Rhodococcus fascians strain D188 is essential for full virulence on tobacco through the production of an autoregulatory compound."
Maes T., Vereecke D., Ritsema T., Cornelis K., Thu H.N., Van Montagu M., Holsters M., Goethals K.
Mol. Microbiol. 42:13-28(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: D188.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AJ311775 Genomic DNA. Translation: CAC43336.1.

3D structure databases

ProteinModelPortalQ93JQ8.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

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_RHOFA
AccessionPrimary (citable) accession number: Q93JQ8
Entry history
Integrated into UniProtKB/Swiss-Prot: March 25, 2003
Last sequence update: December 1, 2001
Last modified: April 3, 2013
This is version 58 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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