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Q058D6 (ASSY_BUCCC) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 49. 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:BCc_032
OrganismBuchnera aphidicola subsp. Cinara cedri (strain Cc) [Complete proteome] [HAMAP]
Taxonomic identifier372461 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera

Protein attributes

Sequence length399 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 – 399399Argininosuccinate synthase HAMAP-Rule MF_00005
PRO_1000057038

Regions

Nucleotide binding8 – 169ATP By similarity

Sites

Binding site351ATP; via amide nitrogen and carbonyl oxygen By similarity
Binding site871Citrulline By similarity
Binding site1171ATP; via amide nitrogen By similarity
Binding site1191Aspartate By similarity
Binding site1231Aspartate By similarity
Binding site1231Citrulline By similarity
Binding site1241Aspartate By similarity
Binding site1271Citrulline By similarity
Binding site1761Citrulline By similarity
Binding site1851Citrulline By similarity
Binding site2611Citrulline By similarity
Binding site2731Citrulline By similarity

Sequences

Sequence LengthMass (Da)Tools
Q058D6 [UniParc].

Last modified November 14, 2006. Version 1.
Checksum: 65E279640523F661

FASTA39945,285
        10         20         30         40         50         60 
MKKTIVLAYS GGLDTSAIIP WIKDNYNFDV VAFVADIGQS KKDLYKIKEK AIISGASDCY 

        70         80         90        100        110        120 
ISDLKDIFVK KYVFPMLKTG AIYEGEYLLG TAIARPLIAK AQVDYAKKIN AIGLCHGSTG 

       130        140        150        160        170        180 
KGNDQVRFEL AYSALAPSLL VIAPWREWKF QSREDLLKYL KTKNIVTNVN KKKIYSRDEN 

       190        200        210        220        230        240 
IFHVSTEGGI LEDPWNPANE DCWFWTKSPL NAPNKPKKIS LKIEKGCVVS INNKFFNEFN 

       250        260        270        280        290        300 
CLKRLNKIGA KHSIGRIDIV ENRLIGMKSR GCYETPGGTI IYKALRSLEQ LVFDRECMYW 

       310        320        330        340        350        360 
KNKIALQLSS IIYDGKWFTP IRKSLQKSSD ILSSSISGKV VVELYKGSVR ILQKKSLNSL 

       370        380        390 
YSKKYVTFGK DNVYNQIDAK GFIRLFSLSS RIRALKNKK 

« Hide

References

[1]"A small microbial genome: the end of a long symbiotic relationship?"
Perez-Brocal V., Gil R., Ramos S., Lamelas A., Postigo M., Michelena J.M., Silva F.J., Moya A., Latorre A.
Science 314:312-313(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Cc.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000263 Genomic DNA. Translation: ABJ90513.1.
RefSeqYP_802606.1. NC_008513.1.

3D structure databases

ProteinModelPortalQ058D6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING372461.BCc_032.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABJ90513; ABJ90513; BCc_032.
GeneID4440707.
KEGGbcc:BCc_032.
PATRIC21245999. VBIBucAph7855_0027.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0137.
HOGENOMHOG000230093.
KOK01940.
OMAIYNGYWW.
OrthoDBEOG6K9QCV.

Enzyme and pathway databases

BioCycBAPH372461:GHAJ-32-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_BUCCC
AccessionPrimary (citable) accession number: Q058D6
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: November 14, 2006
Last modified: February 19, 2014
This is version 49 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