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Reviewed, UniProtKB/Swiss-Prot A8EUB2 (ASSY_ARCB4)

Last modified November 3, 2009. Version 14. 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: Abu_1279
OrganismArcobacter butzleri (strain RM4018) [Complete proteome] [HAMAP]
Taxonomic identifier367737 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Campylobacteraceae › Arcobacter

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Protein attributes

Sequence length413 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 – 413413Argininosuccinate synthase HAMAP MF_00005
PRO_0000321300

Regions

Nucleotide binding12 – 209ATP By similarity

Sites

Binding site391ATP; via amide nitrogen and carbonyl oxygen By similarity
Binding site921Citrulline By similarity
Binding site971Citrulline By similarity
Binding site1221ATP; via amide nitrogen By similarity
Binding site1241Aspartate By similarity
Binding site1281Aspartate By similarity
Binding site1281Citrulline By similarity
Binding site1291Aspartate By similarity
Binding site1321Citrulline By similarity
Binding site1891Citrulline By similarity
Binding site1981Citrulline By similarity
Binding site2741Citrulline By similarity
Binding site2861Citrulline By similarity

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Sequences

Sequence LengthMass (Da)Tools
A8EUB2-1 [UniParc].

Last modified November 13, 2007. Version 1.
Checksum: E035334064CC2470

FASTA41346,373
        10         20         30         40         50         60 
MSKKDIKKVV LAYSGGLDTS IILKWLQDEY NAEVITFTAD LGQGEEVEPA RQKAIACGIK 

        70         80         90        100        110        120 
PENVFILDIK EEFVKDYVFP MFRANAIYEG EYLLGTSIAR PLIAKKLVEI ANQKGAEAVS 

       130        140        150        160        170        180 
HGATGKGNDQ VRFELGALAL NPDLKVIAPW REWTLNSRES LLEYAKKNGI EISQKHVDEN 

       190        200        210        220        230        240 
GNPKISPYSM DANLLHISYE GLHLENPANE PEESMWLWTN SPEQAPDEAE YITIGYKNGD 

       250        260        270        280        290        300 
PISINGKELS PATLLKTLND YGNKHGIGRV DIVENRYVGM KARGCYETPG GTIMLKAHRA 

       310        320        330        340        350        360 
IESLTLDREA AHLKDELMPR YAKLIYQGYW FSPEREMLQA AIDATQKNVE GTVRLKLYKG 

       370        380        390        400        410 
NVTVVGRESS KSLYDDAYST FEKDEVYNQK DAEGFIRLNA LRFIIAGKKN NKK

« Hide

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References

[1]"The complete genome sequence and analysis of the Epsilonproteobacterium Arcobacter butzleri."
Miller W.G., Parker C.T., Rubenfield M., Mendz G.L., Woesten M.M.S.M., Ussery D.W., Stolz J.F., Binnewies T.T., Hallin P.F., Wang G., Malek J.A., Rogosin A., Stanker L.H., Mandrell R.E.
PLoS ONE 2:E1358-E1358(2007) [PubMed: 18159241] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

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Cross-references

Sequence databases

CP000361 Genomic DNA. Translation: ABV67536.1.
RefSeqYP_001490205.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA8EUB2.

Genome annotation databases

GeneID5625040.
GenomeReviewsGene locus Abu_1279 in contig CP000361_GR.
KEGGabu:Abu_1279.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAYVFPMFR.

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_ARCB4
AccessionPrimary (citable) accession number: A8EUB2
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: November 13, 2007
Last modified: November 3, 2009
This is version 14 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