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A4SIM5 (ASSY_AERS4) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 45. 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
Ordered Locus Names:ASA_0581
OrganismAeromonas salmonicida (strain A449) [Complete proteome] [HAMAP]
Taxonomic identifier382245 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Aeromonadales › Aeromonadaceae › Aeromonas ›

Protein attributes

Sequence length416 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
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 – 416416Argininosuccinate synthase HAMAP-Rule MF_00005
PRO_0000321298

Regions

Nucleotide binding15 – 239ATP By similarity

Sites

Binding site421ATP; via amide nitrogen and carbonyl oxygen By similarity
Binding site941Citrulline By similarity
Binding site991Citrulline By similarity
Binding site1241ATP; via amide nitrogen By similarity
Binding site1261Aspartate By similarity
Binding site1301Aspartate By similarity
Binding site1301Citrulline By similarity
Binding site1311Aspartate By similarity
Binding site1341Citrulline By similarity
Binding site1831Citrulline By similarity
Binding site1921Citrulline By similarity
Binding site2681Citrulline By similarity
Binding site2801Citrulline By similarity

Sequences

Sequence LengthMass (Da)Tools
A4SIM5 [UniParc].

Last modified May 15, 2007. Version 1.
Checksum: 00594AB24BD9F952

FASTA41645,832
        10         20         30         40         50         60 
MERSKMSGIN KIVLAYSGGL DTSAIIPWLK EHYDAEIIAF VADVGQERDD LEGIEQKAIA 

        70         80         90        100        110        120 
SGAVKCIVKD LREEFVKEYV YPTLKTGAVY EGTYLLGTSM ARPIIAKAMV EAALAEGADA 

       130        140        150        160        170        180 
ISHGCTGKGN DQVRFEGAVA ALAPQLKVIA PWRLWDMRSR EDLLAYLEAR DIPCKATLKK 

       190        200        210        220        230        240 
IYSRDANAWH ISTEGGELES TWNEPSEAVW QWTVSAEQAP NEPEYVKLTV AKGEVVAVDD 

       250        260        270        280        290        300 
QPLSPHQILT TLNERAGKHG VGRIDITENR MVGMKSRGCY ETPGGTVMVA ALRAVEELVL 

       310        320        330        340        350        360 
DRPTRAWREK LGAEFSHLVY DGRWFTPLCK AIVASANAIA EDLDGEVILK MYKGQVTAVQ 

       370        380        390        400        410 
KKSPNSLYSE DFATFGADEV YDQSHAEGFI RLYTLASRIR AMKEQHQAIG GDHTHG

« Hide

References

[1]"The genome of Aeromonas salmonicida subsp. salmonicida A449: insights into the evolution of a fish pathogen."
Reith M.E., Singh R.K., Curtis B., Boyd J.M., Bouevitch A., Kimball J., Munholland J., Murphy C., Sarty D., Williams J., Nash J.H., Johnson S.C., Brown L.L.
BMC Genomics 9:427-427(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: A449.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000644 Genomic DNA. Translation: ABO88747.1.
RefSeqYP_001140495.1. NC_009348.1.

3D structure databases

ProteinModelPortalA4SIM5.
SMRA4SIM5. Positions 11-405.
ModBaseSearch...

Protein-protein interaction databases

STRING382245.ASA_0581.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABO88747; ABO88747; ASA_0581.
GeneID4995922.
KEGGasa:ASA_0581.
PATRIC20787486. VBIAerSal2987_0586.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0137.
HOGENOMHOG000230093.
KOK01940.
OMANDQFRFE.
ProtClustDBPRK00509.

Enzyme and pathway databases

BioCycASAL382245:GJJN-577-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]
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_AERS4
AccessionPrimary (citable) accession number: A4SIM5
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: May 15, 2007
Last modified: May 1, 2013
This is version 45 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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