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P59412 (ASSY_BUCBP) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 76. 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:bbp_048
OrganismBuchnera aphidicola subsp. Baizongia pistaciae (strain Bp) [Complete proteome] [HAMAP]
Taxonomic identifier224915 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera

Protein attributes

Sequence length409 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 – 409409Argininosuccinate synthase HAMAP-Rule MF_00005
PRO_0000148578

Regions

Nucleotide binding12 – 209ATP By similarity

Sites

Binding site391ATP; via amide nitrogen and carbonyl oxygen By similarity
Binding site911Citrulline By similarity
Binding site1211ATP; via amide nitrogen By similarity
Binding site1231Aspartate By similarity
Binding site1271Aspartate By similarity
Binding site1271Citrulline By similarity
Binding site1281Aspartate By similarity
Binding site1311Citrulline By similarity
Binding site1801Citrulline By similarity
Binding site1891Citrulline By similarity
Binding site2651Citrulline By similarity
Binding site2771Citrulline By similarity

Sequences

Sequence LengthMass (Da)Tools
P59412 [UniParc].

Last modified March 28, 2003. Version 1.
Checksum: 1257088969D05697

FASTA40946,032
        10         20         30         40         50         60 
MRNKNIKKVV LAYSGGLDTS AIIPWIKENY SSEVIAFVAN VGQNQADLKD IEYKALKSGA 

        70         80         90        100        110        120 
SQCIIKDLRE EFIRDYVYPV LKSGALYEEN YLLGTALARP IIAKSQVDLA LKLKADGVCH 

       130        140        150        160        170        180 
GATGKGNDQV RFETAYVGLA PELKIIAPWR EWSFKSRGEL LSYLKEKNVK TTASIEKIYS 

       190        200        210        220        230        240 
KDENAWHVST EGGVLEDLWN KPNQDCWTWT NDPKDAPNVP EIISIKIKNG SVIAVNNEFL 

       250        260        270        280        290        300 
SPFKCLEKLN LVGIKHGIGR IDVVENRLVG MKSRACYETP GGTILVNALR SLEQLVLDRD 

       310        320        330        340        350        360 
SYKWRQQIAL EMSYVIYNGN WFSPFRKSLQ AAATELATEI DGEVILELYK GTVTAIRKFS 

       370        380        390        400 
PNSLYSKEFA TFDQDEVYRQ SDADGFIKLY SLPSKIRAIN KCMNKALMK 

« Hide

References

[1]"Reductive genome evolution in Buchnera aphidicola."
van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F., Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J., Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.
Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Bp.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016826 Genomic DNA. Translation: AAO26787.1.
RefSeqNP_777682.1. NC_004545.1.

3D structure databases

ProteinModelPortalP59412.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224915.bbp048.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAO26787; AAO26787; bbp_048.
GeneID1058536.
KEGGbab:bbp048.
PATRIC21244869. VBIBucAph80364_0045.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0137.
KOK01940.
OMAIYNGYWW.
OrthoDBEOG6K9QCV.

Enzyme and pathway databases

BioCycBAPH224915:GJ9D-48-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_BUCBP
AccessionPrimary (citable) accession number: P59412
Entry history
Integrated into UniProtKB/Swiss-Prot: March 28, 2003
Last sequence update: March 28, 2003
Last modified: February 19, 2014
This is version 76 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