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A9BDR3 (ASSY_PROM4) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 46. 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:P9211_18441
OrganismProchlorococcus marinus (strain MIT 9211) [Complete proteome] [HAMAP]
Taxonomic identifier93059 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus

Protein attributes

Sequence length400 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 – 400400Argininosuccinate synthase HAMAP-Rule MF_00005
PRO_1000089050

Regions

Nucleotide binding9 – 179ATP By similarity

Sites

Binding site371ATP; via amide nitrogen and carbonyl oxygen By similarity
Binding site881Citrulline By similarity
Binding site1181ATP; via amide nitrogen By similarity
Binding site1201Aspartate By similarity
Binding site1241Aspartate By similarity
Binding site1241Citrulline By similarity
Binding site1251Aspartate By similarity
Binding site1281Citrulline By similarity
Binding site1761Citrulline By similarity
Binding site1851Citrulline By similarity
Binding site2611Citrulline By similarity
Binding site2731Citrulline By similarity

Sequences

Sequence LengthMass (Da)Tools
A9BDR3 [UniParc].

Last modified January 15, 2008. Version 1.
Checksum: D7BD44E37BBDB210

FASTA40043,840
        10         20         30         40         50         60 
MEVKKVVLAY SGGVDTSSCI PYLINEYGVE EVVAFAADLG QGDELEPIRE KALSAGASEC 

        70         80         90        100        110        120 
LVDDLVKPFI EDFAFPAIRA NALYEGKYPL STALARPLIS KRLVDIAKEL EADAVAHGCT 

       130        140        150        160        170        180 
GKGNDQVRFD IAIATLAPEL KVLTPARQWG MSREEVIAYG ERYGIPAPVS KKSPYSIDLN 

       190        200        210        220        230        240 
LLGRSVEAGP LEDISLSPPE EVYQITSSIE NTPDQSQEIE IIFEGGNPIA IDGVELDPLS 

       250        260        270        280        290        300 
LIVLANQLAG KHGFGRIDMI ENRVVGIKSR EIYETPGLLL LIKAHQELES LTLPADVLRT 

       310        320        330        340        350        360 
KSTLETQWAD LVYQGLWFSP LKNALDGFID RTQDEVNGSV KVKLHKGNAT ITGRSSSQNS 

       370        380        390        400 
LYLPDFSTYG SQDKFKHDNA EGFIYIWGLP SRLWAQSKNK 

« Hide

References

[1]"Patterns and implications of gene gain and loss in the evolution of Prochlorococcus."
Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S., Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M., Richardson P., Chisholm S.W.
PLoS Genet. 3:2515-2528(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MIT 9211.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000878 Genomic DNA. Translation: ABX09775.1.
RefSeqYP_001551729.1. NC_009976.1.

3D structure databases

ProteinModelPortalA9BDR3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING93059.P9211_18441.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABX09775; ABX09775; P9211_18441.
GeneID5731811.
KEGGpmj:P9211_18441.
PATRIC22989386. VBIProMar136502_1952.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0137.
HOGENOMHOG000230093.
KOK01940.
OMAYAFPAIK.
OrthoDBEOG6K9QCV.

Enzyme and pathway databases

BioCycPMAR93059:GHJV-1890-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_PROM4
AccessionPrimary (citable) accession number: A9BDR3
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: January 15, 2008
Last modified: May 14, 2014
This is version 46 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