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C1FU68 (ASSY_CLOBJ) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 37. 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:CLM_3035
OrganismClostridium botulinum (strain Kyoto / Type A2) [Complete proteome] [HAMAP]
Taxonomic identifier536232 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length397 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 – 397397Argininosuccinate synthase HAMAP-Rule MF_00005
PRO_1000191889

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
C1FU68 [UniParc].

Last modified May 26, 2009. Version 1.
Checksum: 7D3A75EB7FBDC968

FASTA39744,742
        10         20         30         40         50         60 
MKEKVVLAYS GGLDTSIIIP WLKENYDLDV IAVCVNVGQG DDMDYVKTKA IKSGASKIYV 

        70         80         90        100        110        120 
EDVKEEFVVD YLYKAIKSEA LYEQDYMLGT SFARPLMAKK LVEIAHKEQA KYICHGCTGK 

       130        140        150        160        170        180 
GNDQVRFEVG VKAQDPIIKI IAPWRIWDIK SREDAIDYAK KVGVEVPVTK KKIYSVDKNL 

       190        200        210        220        230        240 
WHVSHEGGDL EDLKNEHKED MYFMVTPPEK AKNEPTYLEI YFEKGAPVKI NGEVLNPVDI 

       250        260        270        280        290        300 
IDKLNTIGGE NGIGIADIIE NRLVGMKSRG IYETPAGTLL YAAHKKLESV TLDKYTYQYK 

       310        320        330        340        350        360 
KIVSAQYGEL VYNGLWFTSL REAIDAFVDK TQENVTGTVQ LKLYKGNIKP CSVDTEYALY 

       370        380        390 
DEGISSFGES ELYSHKDAEG FINLFGLPSK IKALKNF 

« Hide

References

[1]"Genome sequence of Clostridium botulinum A2 Kyoto."
Shrivastava S., Brinkac L.M., Brown J.L., Bruce D., Detter C.C., Johnson E.A., Munk C.A., Smith L.A., Smith T.J., Sutton G., Brettin T.S.
Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Kyoto / Type A2.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001581 Genomic DNA. Translation: ACO86433.1.
RefSeqYP_002805173.1. NC_012563.1.

3D structure databases

ProteinModelPortalC1FU68.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING536232.CLM_3035.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACO86433; ACO86433; CLM_3035.
GeneID7764589.
KEGGcby:CLM_3035.
PATRIC19382513. VBICloBot91161_2882.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0137.
HOGENOMHOG000230093.
KOK01940.
OMAPECEYIR.
OrthoDBEOG6K9QCV.

Enzyme and pathway databases

BioCycCBOT536232:GCO3-2946-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_CLOBJ
AccessionPrimary (citable) accession number: C1FU68
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: May 26, 2009
Last modified: May 14, 2014
This is version 37 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