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P59602 (ASSY_CLOTE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:CTC_00561
OrganismClostridium tetani (strain Massachusetts / E88) [Complete proteome] [HAMAP]
Taxonomic identifier212717 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium ›

Protein attributes

Sequence length398 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.

Subcellular location

Cytoplasm By similarity.

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: 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...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 398398Argininosuccinate synthase HAMAP-Rule MF_00005
PRO_0000148587

Regions

Nucleotide binding9 – 179ATP By similarity

Sites

Binding site871Citrulline By similarity
Binding site921Citrulline 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
P59602 [UniParc].

Last modified April 23, 2003. Version 1.
Checksum: 4F153EB0073694AD

FASTA39844,419
        10         20         30         40         50         60 
MTKEKVVLAY SGGLDTSIII PWLKENYDLD VIAVCIDVGQ DDDMEEVKKK AIKTGAVKVY 

        70         80         90        100        110        120 
VEDAKEEFVK DYVFKALKAN ALYEEKYMLG TSLARPLMAK KLVEIAHKEG AKYICHGCTG 

       130        140        150        160        170        180 
KGNDQVRFEV GIASFDPSIK IIAPWRIWDI KSREDAIDYA KEKGVEVPVT KKKIYSVDKN 

       190        200        210        220        230        240 
ILHTSHEGGE LEDPKNAHNK EMYSMVTPPE KAKDEPTYVD IYFNKGVPEK INGKEISPVE 

       250        260        270        280        290        300 
LLNTLNKIGG ENGVGVVDIV ENRLVGMKSR GVYETPGGTI LYEAHKDLES LTLDKLTLHC 

       310        320        330        340        350        360 
KQELAQKYGE IAYDGLWFTT LRESLDAFVD VTQENVTGTV KLKLYKGNIM NAGIDTKNAL 

       370        380        390 
YDEGISSFGA SELYSHKDAE GFIKLFSLPS KIKALKNK

« Hide

References

[1]"The genome sequence of Clostridium tetani, the causative agent of tetanus disease."
Brueggemann H., Baeumer S., Fricke W.F., Wiezer A., Liesegang H., Decker I., Herzberg C., Martinez-Arias R., Merkl R., Henne A., Gottschalk G.
Proc. Natl. Acad. Sci. U.S.A. 100:1316-1321(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Massachusetts / E88.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE015927 Genomic DNA. Translation: AAO35180.1.
RefSeqNP_781243.1. NC_004557.1.

3D structure databases

ProteinModelPortalP59602.
SMRP59602. Positions 5-398.
ModBaseSearch...

Protein-protein interaction databases

STRING212717.CTC00561.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAO35180; AAO35180; CTC_00561.
GeneID1058773.
KEGGctc:CTC00561.
PATRIC19508952. VBICloTet101274_0526.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0137.
KOK01940.
OMAIYNGYWW.
ProtClustDBPRK00509.

Enzyme and pathway databases

BioCycCTET212717:GJAM-506-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]
PANTHERPTHR11587. PTHR11587. 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...

Entry information

Entry nameASSY_CLOTE
AccessionPrimary (citable) accession number: P59602
Entry history
Integrated into UniProtKB/Swiss-Prot: April 23, 2003
Last sequence update: April 23, 2003
Last modified: May 1, 2013
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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