Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q8U484 (ASSY_PYRFU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 74. 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
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:PF0207
OrganismPyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1) [Reference proteome] [HAMAP]
Taxonomic identifier186497 [NCBI]
Taxonomic lineageArchaea › Euryarchaeota › Thermococci › Thermococcales › Thermococcaceae › Pyrococcus ›

Protein attributes

Sequence length410 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
   Technical termComplete proteome
Reference proteome
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 – 410410Argininosuccinate synthase HAMAP-Rule MF_00005
PRO_0000148684

Regions

Nucleotide binding6 – 149ATP 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 site1691Citrulline By similarity
Binding site1781Citrulline By similarity
Binding site2541Citrulline By similarity
Binding site2661Citrulline By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8U484 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: BEF1CD6792295047

FASTA41045,973
        10         20         30         40         50         60 
MRIVLAYSGG LDTSVILKLM QEKLGAEVIT VTVDVGQKDD FEKIEEKAYK FGAVKHYYID 

        70         80         90        100        110        120 
AKEEFAENYV CKAIKANALY ENAYPLSTAL ARPLIVEKLV EVAKKEGAGI IAHGCTGKGN 

       130        140        150        160        170        180 
DQVRFNLGIK ALMPEAEILQ PVAEWNLTRD WEMEYAKKHG IPVSDKIYSI DENIWGRSIE 

       190        200        210        220        230        240 
GGVLEDPSIE PPEEVFEWTV SIEKAPDKPE YVTIGFENGV PVSLNGEKMK LLELILKLNE 

       250        260        270        280        290        300 
IAGKHGVGRI DHIEDRSVGI KSREVYEAPA AVTLIKAHQD LEKLTLTKWV IEFKSIVDSK 

       310        320        330        340        350        360 
WSWLVYNGLW YEPLRLALEG FIDEAEKAVN GEVTVKLWKG NAIVVGRKSD NALYDVKMAT 

       370        380        390        400        410 
YEKFSTFDQK LAKGFIELFG MQSVLAYNML HGVHSTSNIS EIKEAIKTLE

« Hide

References

[1]"Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences."
Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M., DiRuggiero J., Robb F.T.
Genetics 152:1299-1305(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE009950 Genomic DNA. Translation: AAL80331.1.
RefSeqNP_577936.1. NC_003413.1.

3D structure databases

ProteinModelPortalQ8U484.
ModBaseSearch...

Protein-protein interaction databases

STRING186497.PF0207.

Proteomic databases

PRIDEQ8U484.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL80331; AAL80331; PF0207.
GeneID1468039.
KEGGpfu:PF0207.

Phylogenomic databases

eggNOGCOG0137.
HOGENOMHOG000230093.
KOK01940.
OMANDQFRFE.

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_PYRFU
AccessionPrimary (citable) accession number: Q8U484
Entry history
Integrated into UniProtKB/Swiss-Prot: October 19, 2002
Last sequence update: June 1, 2002
Last modified: May 1, 2013
This is version 74 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents