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Q6LVG8 (ASSY_PHOPR) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 65. 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:PBPRA0268
OrganismPhotobacterium profundum (Photobacterium sp. (strain SS9)) [Complete proteome] [HAMAP]
Taxonomic identifier74109 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaePhotobacterium

Protein attributes

Sequence length404 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 – 404404Argininosuccinate synthase HAMAP-Rule MF_00005
PRO_0000148622

Regions

Nucleotide binding10 – 189ATP By similarity

Sites

Binding site371ATP; via amide nitrogen and carbonyl oxygen By similarity
Binding site891Citrulline By similarity
Binding site941Citrulline 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
Q6LVG8 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: B950506F128C5983

FASTA40444,263
        10         20         30         40         50         60 
MSKVTKVVLA YSGGLDTSAI IPWLKENYDC EVVAFVADVG QGAAELEGIE EKAIASGASS 

        70         80         90        100        110        120 
CYIADLKEEM VADYIYPSLK TGAIYEGKYL LGTSMARPII AKAQVECALA VGADAVCHGC 

       130        140        150        160        170        180 
TGKGNDQVRF EGAYAALAPQ LTVIAPWREW DLRSREALLD YLAERDIPCT ASLEKIYSRD 

       190        200        210        220        230        240 
ANAWHISTEG GVLENTWNQS NELCWVWTKD PENAPEKAET VSILVEKGEV VAVDGEAMSP 

       250        260        270        280        290        300 
FNALTYLNEK GAEHGVGRID IVENRLVGIK SRGCYETPGG TIMNEALRAV EQLVLDKESY 

       310        320        330        340        350        360 
EFRETVGLKA SHLIYDGRWF TPLCKSILAA ADELAQDVSG EVVVKLYKGQ ATVIQKRSMN 

       370        380        390        400 
SLYSEEFATF GEDDVYDHSH AGGFIRLYSL ASRIRALNTQ KKQK 

« Hide

References

[1]"Life at depth: Photobacterium profundum genome sequence and expression analysis."
Vezzi A., Campanaro S., D'Angelo M., Simonato F., Vitulo N., Lauro F.M., Cestaro A., Malacrida G., Simionati B., Cannata N., Romualdi C., Bartlett D.H., Valle G.
Science 307:1459-1461(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SS9.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR378663 Genomic DNA. Translation: CAG18707.1.
RefSeqYP_128509.1. NC_006370.1.

3D structure databases

ProteinModelPortalQ6LVG8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING298386.PBPRA0268.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAG18707; CAG18707; PBPRA0268.
GeneID3122122.
KEGGppr:PBPRA0268.
PATRIC22931188. VBIPhoPro109272_0341.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

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]
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_PHOPR
AccessionPrimary (citable) accession number: Q6LVG8
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: July 5, 2004
Last modified: February 19, 2014
This is version 65 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