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Q5WZ50 (ASSY_LEGPL) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 64. 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:lpl0532
OrganismLegionella pneumophila (strain Lens) [Complete proteome] [HAMAP]
Taxonomic identifier297245 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaLegionellalesLegionellaceaeLegionella

Protein attributes

Sequence length405 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 – 405405Argininosuccinate synthase HAMAP-Rule MF_00005
PRO_0000148605

Regions

Nucleotide binding11 – 199ATP By similarity

Sites

Binding site901Citrulline By similarity
Binding site1191ATP; via amide nitrogen By similarity
Binding site1211Aspartate By similarity
Binding site1251Aspartate By similarity
Binding site1251Citrulline By similarity
Binding site1261Aspartate By similarity
Binding site1291Citrulline By similarity
Binding site1781Citrulline By similarity
Binding site1871Citrulline By similarity
Binding site2631Citrulline By similarity
Binding site2751Citrulline By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5WZ50 [UniParc].

Last modified November 23, 2004. Version 1.
Checksum: 391153A92A122497

FASTA40545,052
        10         20         30         40         50         60 
MKKNIKKIAL AYSGGLDTSI MIPWLKEHYE HAEVIAVICD LGQQEDLDAI KNKALKSGAS 

        70         80         90        100        110        120 
KAYVVDVKNE FAIQYLWPLV KSGALYEDQY ILGTISRPLI AQKLVEIALT EQVNAVAHGA 

       130        140        150        160        170        180 
TGKGNDQVRF EYSLKALAPQ LEIIAPWRAW DIKSRQEAIV YAKAHGIEVP VTPKAPYSRD 

       190        200        210        220        230        240 
HNIWYISHEG GVLEDPSQEM PDDVLLMTSP VSQAPDEEEM IILDFKKGVP VALNEQKLSP 

       250        260        270        280        290        300 
VALLNSLNQK AGQHGIGVAD IVENRLVGMK IRGIYEAPAA AVLYKAHKLL ESLCLTRSTL 

       310        320        330        340        350        360 
HLKQSLQQTY ANLVYEGRWF SQTKQALDAF IDVTQQHVTG RVKLKLFKGN IIPAGMHSPY 

       370        380        390        400 
SLHHPALATF EEDNVYNQKD AEGFINLFSL SAKIYSQVHQ GGNYD 

« Hide

References

[1]"Evidence in the Legionella pneumophila genome for exploitation of host cell functions and high genome plasticity."
Cazalet C., Rusniok C., Brueggemann H., Zidane N., Magnier A., Ma L., Tichit M., Jarraud S., Bouchier C., Vandenesch F., Kunst F., Etienne J., Glaser P., Buchrieser C.
Nat. Genet. 36:1165-1173(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Lens.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR628337 Genomic DNA. Translation: CAH14762.1.
RefSeqYP_125898.1. NC_006369.1.

3D structure databases

ProteinModelPortalQ5WZ50.
SMRQ5WZ50. Positions 7-400.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING297245.lpl0532.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAH14762; CAH14762; lpl0532.
GeneID3113326.
KEGGlpf:lpl0532.
PATRIC22314573. VBILegPne33733_0628.

Organism-specific databases

LegioListlpl0532.
CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycLPNE297245:GJD4-565-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_LEGPL
AccessionPrimary (citable) accession number: Q5WZ50
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: November 23, 2004
Last modified: February 19, 2014
This is version 64 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