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A0Q1Z2 (ASSY_CLONN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 47. 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:NT01CX_0135
OrganismClostridium novyi (strain NT) [Complete proteome] [HAMAP]
Taxonomic identifier386415 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length402 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 – 402402Argininosuccinate synthase HAMAP-Rule MF_00005
PRO_1000000393

Regions

Nucleotide binding8 – 169ATP By similarity

Sites

Binding site861Citrulline By similarity
Binding site911Citrulline By similarity
Binding site1161ATP; via amide nitrogen By similarity
Binding site1181Aspartate By similarity
Binding site1221Aspartate By similarity
Binding site1221Citrulline By similarity
Binding site1231Aspartate By similarity
Binding site1261Citrulline By similarity
Binding site1751Citrulline By similarity
Binding site1841Citrulline By similarity
Binding site2601Citrulline By similarity
Binding site2721Citrulline By similarity

Sequences

Sequence LengthMass (Da)Tools
A0Q1Z2 [UniParc].

Last modified January 9, 2007. Version 1.
Checksum: 7882A75E040103AB

FASTA40245,413
        10         20         30         40         50         60 
MKEKVVLAYS GGLDTSITIH WLKENYNLDV IACCVNVGQD EDFDEIKKKA IKSGATKIYV 

        70         80         90        100        110        120 
EDVKDEFVSE YIYKGVKANA VYEGKYLLGT SFARPLIAKK LVEVAHKEGA KYICHGCTGK 

       130        140        150        160        170        180 
GNDQVRFEVG IMSLDPSIKV IAPWRIWNIK SREDAVDYAN ANGIEVPVTK EKIYSRDQNL 

       190        200        210        220        230        240 
WHISHEGGDL ENIRNEHKTD MYCMTVPPEK AKDEVSYIKI TFEKGEAKKL DDVEMSPVEI 

       250        260        270        280        290        300 
LEKLNKIGGE NGIGVIDLLE NRLVGMKSRG VYETPGGTIL YAAHKELEYL TMQKETFHFK 

       310        320        330        340        350        360 
QMVSQKYGEL VYNGLWFSTL KESLDAFIDK TQEVVNGTVR LKLYKGNIMV AGMESPNALY 

       370        380        390        400 
EESISSFGAS DFYDHKDAEG FINLFGLPYK INAMIQLKNQ EN 

« Hide

References

[1]"The genome and transcriptomes of the anti-tumor agent Clostridium novyi-NT."
Bettegowda C., Huang X., Lin J., Cheong I., Kohli M., Szabo S.A., Zhang X., Diaz L.A. Jr., Velculescu V.E., Parmigiani G., Kinzler K.W., Vogelstein B., Zhou S.
Nat. Biotechnol. 24:1573-1580(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000382 Genomic DNA. Translation: ABK61403.1.
RefSeqYP_878644.1. NC_008593.1.

3D structure databases

ProteinModelPortalA0Q1Z2.
SMRA0Q1Z2. Positions 4-396.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING386415.NT01CX_0135.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABK61403; ABK61403; NT01CX_0135.
GeneID4540890.
KEGGcno:NT01CX_0135.
PATRIC19480812. VBICloNov112828_1676.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0137.
HOGENOMHOG000230093.
KOK01940.
OMAIYNGYWW.
OrthoDBEOG6K9QCV.
ProtClustDBPRK00509.

Enzyme and pathway databases

BioCycCNOV386415:GH98-1703-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_CLONN
AccessionPrimary (citable) accession number: A0Q1Z2
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 9, 2007
Last modified: February 19, 2014
This is version 47 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