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Reviewed, UniProtKB/Swiss-Prot Q058D6 (ASSY_BUCCC)

Last modified June 16, 2009. Version 16. 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: BCc_032
OrganismBuchnera aphidicola subsp. Cinara cedri [Complete proteome] [HAMAP]
Taxonomic identifier372461 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera

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Protein attributes

Sequence length399 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

Subcellular location

Cytoplasm Probable.

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 – 399399Argininosuccinate synthase HAMAP 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

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Sequences

Sequence LengthMass (Da)Tools
Q058D6-1 [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

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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: 17038625] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

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Cross-references

Sequence databases

CP000263 Genomic DNA. Translation: ABJ90513.1.
RefSeqYP_802606.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID4440707.
GenomeReviewsGene locus BCc_032 in contig CP000263_GR.
KEGGbcc:BCc_032.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAQ058D6. YVFPMFR.

Family and domain databases

HAMAPMF_00005.
[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_BUCCC
AccessionPrimary (citable) accession number: Q058D6
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: November 14, 2006
Last modified: June 16, 2009
This is version 16 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