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Q97KE6 (ASSY_CLOAB) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 85. 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:CA_C0973
OrganismClostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787) [Reference proteome] [HAMAP]
Taxonomic identifier272562 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length400 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
Reference 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 – 400400Argininosuccinate synthase HAMAP-Rule MF_00005
PRO_0000148585

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
Q97KE6 [UniParc].

Last modified October 1, 2001. Version 1.
Checksum: 38F4F3139D3958C3

FASTA40045,045
        10         20         30         40         50         60 
MKEKVVLAYS GGLDTSVTIP WLKDNYDVEV IAVCVNVGQE DDMDKVKEKA VNSGAAKIYV 

        70         80         90        100        110        120 
EDVKEEFVTE YLYNAIKWNA TYEGKYLLGT SFARPLIAKK LVEVAHKEGA KYICHGCTGK 

       130        140        150        160        170        180 
GNDQVRFETA IAAMDPYIKI IAPWRLWNID SREAEIDYAL SKGVEVPVTK EKIYSEDWNL 

       190        200        210        220        230        240 
WHISHEGGDL EDPKNEHKEE MYKCVTPPEE AKDEPAYISI YFEKGVPCKI NGEELEPVKL 

       250        260        270        280        290        300 
IEKVNKVAGE NGIGVVDLVE NRLVGMKSRG VYETPGGTLL YEAHAQLERL TVDKDAYHYK 

       310        320        330        340        350        360 
QVLALKYSEL VYDGLWFTTT REALDAFVDT VEENVTGTVK LKLYKGNMKV SSVESENALY 

       370        380        390        400 
DEGISSFGAS DLYDHKDAQG FINLFSLPSK IKAMKKLEKK 

« Hide

References

[1]"Genome sequence and comparative analysis of the solvent-producing bacterium Clostridium acetobutylicum."
Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R., Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F., Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V., Smith D.R.
J. Bacteriol. 183:4823-4838(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE001437 Genomic DNA. Translation: AAK78949.1.
PIRB97020.
RefSeqNP_347609.1. NC_003030.1.

3D structure databases

ProteinModelPortalQ97KE6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272562.CA_C0973.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAK78949; AAK78949; CA_C0973.
GeneID1117156.
KEGGcac:CA_C0973.
PATRIC32036333. VBICloAce74127_1182.

Phylogenomic databases

eggNOGCOG0137.
HOGENOMHOG000230093.
KOK01940.
OMAPECEYIR.
OrthoDBEOG6K9QCV.

Enzyme and pathway databases

BioCycCACE272562:GJIH-1020-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_CLOAB
AccessionPrimary (citable) accession number: Q97KE6
Entry history
Integrated into UniProtKB/Swiss-Prot: October 19, 2002
Last sequence update: October 1, 2001
Last modified: May 14, 2014
This is version 85 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