Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

C4LIE1 (ASSY_CORK4) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 36. 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:ckrop_0842
OrganismCorynebacterium kroppenstedtii (strain DSM 44385 / CCUG 35717) [Complete proteome] [HAMAP]
Taxonomic identifier645127 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium

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. 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 – 398398Argininosuccinate synthase HAMAP-Rule MF_00005
PRO_1000201677

Regions

Nucleotide binding8 – 169ATP By similarity

Sites

Binding site871Citrulline 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 site1751Citrulline By similarity
Binding site2591Citrulline By similarity
Binding site2711Citrulline By similarity

Sequences

Sequence LengthMass (Da)Tools
C4LIE1 [UniParc].

Last modified July 7, 2009. Version 1.
Checksum: D83DBC1E75C7E121

FASTA39843,829
        10         20         30         40         50         60 
MTNRVVLAYS GGLDTSVAIP YLSKMTDGEV VAVSIDLGQG GEDMESVRQR ALACGAVEAI 

        70         80         90        100        110        120 
VVDAKDEFAE QYCLPAIKAN GLYMKQYPLV SALSRPLIVK HLVETAKEHG GTHVAHGCTG 

       130        140        150        160        170        180 
KGNDQVRFEV GFADTAPDLK IIAPARDYAW TRDKAIAFAE EIDLPIEQSA SSPFSIDQNV 

       190        200        210        220        230        240 
WGRAVETGFL EDLWNPPTKD LYAYTEEPSL GNAPDEVVIS FEGGKPVAID GRPVSVLEAI 

       250        260        270        280        290        300 
EEMNRRGGAQ GVGRLDMVED RLVGIKSREV YEAPGAMVLI RAHEALEDIT VERELARYKR 

       310        320        330        340        350        360 
GIDARWSEEV YDGLWFAPLK RSLDAFIDST QENVTGDIRL VLHEGRITVN GRRSEKSLYD 

       370        380        390 
FNLATYDTGD TFDQTLSRGF VELHGLSSKI ACKRDREQ 

« Hide

References

[1]"Ultrafast pyrosequencing of Corynebacterium kroppenstedtii DSM44385 revealed insights into the physiology of a lipophilic corynebacterium that lacks mycolic acids."
Tauch A., Schneider J., Szczepanowski R., Tilker A., Viehoever P., Gartemann K.-H., Arnold W., Blom J., Brinkrolf K., Brune I., Goetker S., Weisshaar B., Goesmann A., Droege M., Puehler A.
J. Biotechnol. 136:22-30(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 44385 / CCUG 35717.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001620 Genomic DNA. Translation: ACR17596.1.
RefSeqYP_002906139.1. NC_012704.1.

3D structure databases

ProteinModelPortalC4LIE1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING645127.ckrop_0842.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACR17596; ACR17596; ckrop_0842.
GeneID7877047.
KEGGckp:ckrop_0842.
PATRIC21516987. VBICorKro120627_0868.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycCKRO645127:GI7D-828-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_CORK4
AccessionPrimary (citable) accession number: C4LIE1
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: July 7, 2009
Last modified: February 19, 2014
This is version 36 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