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Reviewed, UniProtKB/Swiss-Prot B6EMN8 (ASSY_ALISL)

Last modified February 9, 2010. Version 14. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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
Ordered Locus Names: VSAL_I2758
OrganismAliivibrio salmonicida (strain LFI1238) (Vibrio salmonicida (strain LFI1238)) [Complete proteome] [HAMAP]
Taxonomic identifier316275 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Vibrionales › Vibrionaceae › Aliivibrio

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Protein attributes

Sequence length403 AA.
Sequence statusComplete.
Protein existenceInferred from homology.

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General annotation (Comments)

Catalytic activity

ATP + L-citrulline + L-aspartate = AMP + diphosphate + N(omega)-(L-arginino)succinate. HAMAP MF_00005

Pathway

Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 2/3. HAMAP MF_00005

Subunit structure

Homotetramer By similarity. HAMAP MF_00005

Subcellular location

Cytoplasm Probable HAMAP MF_00005.

Sequence similarities

Belongs to the argininosuccinate synthase family. Type 1 subfamily.

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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: 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...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 403403Argininosuccinate synthase HAMAP MF_00005
PRO_1000089021

Regions

Nucleotide binding13 – 219ATP By similarity

Sites

Binding site401ATP; via amide nitrogen and carbonyl oxygen By similarity
Binding site921Citrulline By similarity
Binding site971Citrulline By similarity
Binding site1221ATP; via amide nitrogen By similarity
Binding site1241Aspartate By similarity
Binding site1281Aspartate By similarity
Binding site1281Citrulline By similarity
Binding site1291Aspartate By similarity
Binding site1321Citrulline By similarity
Binding site1811Citrulline By similarity
Binding site1901Citrulline By similarity
Binding site2661Citrulline By similarity
Binding site2781Citrulline By similarity

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Sequences

Sequence LengthMass (Da)Tools
B6EMN8-1 [UniParc].

Last modified November 25, 2008. Version 1.
Checksum: 4BFC2888DC934D2F

FASTA40344,340
        10         20         30         40         50         60 
MNKKVNVNKV VVAYSGGLDT SVIIPWLKEN YDCEVIAFVA DVGQGAEELE GIEAKAIASG 

        70         80         90        100        110        120 
ASECYVADLK EEMVSEYIFP TLKTGALYEG KYLLGTSMAR PIIAKAQVEV ARNVGADALC 

       130        140        150        160        170        180 
HGCTGKGNDQ IRFEGAFAAL APDLHVIAPW REWDLVSREE CLDYLAERNI PCTASLTKIY 

       190        200        210        220        230        240 
SRDANAWHIS TEGGVLEDTW NEPNEDCWAW TVDPEQAPNE SETVSIKVEK GAVVAVDGKA 

       250        260        270        280        290        300 
MTPYEVVVYL NEKGIKHGVG RIDIVENRLV GMKSRGCYET PGGTIINEAL RAVEQLVLDK 

       310        320        330        340        350        360 
ASFEFREELG IKASHLVYDG RWFTPLCKSI LAATEELAQD VNGDVVIKLY KGQATVTQKR 

       370        380        390        400 
SDNSLYSEEF ATFGADEVYD QSHAEGFIRL YSLSSRIRAL NSK

« Hide

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References

[1]"The complete genome sequence of the fish pathogen Aliivibrio salmonicida strain LFI1238."
Hjerde E., Lorentzen M.S., Holden M.T.G., Seeger K., Paulsen S., Bason N., Churcher C., Harris D., Norbertczak H., Quail M.A., Sanders S., Thurston S., Parkhill J., Willassen N.-P., Thomson N.R.
Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		FM178379 Genomic DNA. Translation: CAQ80442.1.
RefSeqYP_002264094.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID6988249.
GenomeReviewsGene locus VSAL_I2758 in contig FM178379_GR.
KEGGvsa:VSAL_I2758.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG335267.
OMAIAPVREW.

Family and domain databases

HAMAPMF_00005. Arg_succ_synth_type1.
[Tree]
InterProIPR001518. Arginosuc_synth.
IPR018223. Arginosuc_synth_CS.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
Gene3DG3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
PANTHERPTHR11587. Arginosuc_synth. 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...

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Entry information

Entry nameASSY_ALISL
AccessionPrimary (citable) accession number: B6EMN8
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: November 25, 2008
Last modified: February 9, 2010
This is version 14 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents