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

C6E6Y6 (ASSY_GEOSM) 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:GM21_3745
OrganismGeobacter sp. (strain M21) [Complete proteome] [HAMAP]
Taxonomic identifier443144 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaDesulfuromonadalesGeobacteraceaeGeobacter

Protein attributes

Sequence length406 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 – 406406Argininosuccinate synthase HAMAP-Rule MF_00005
PRO_1000201683

Regions

Nucleotide binding12 – 209ATP By similarity

Sites

Binding site391ATP; via amide nitrogen and carbonyl oxygen By similarity
Binding site901Citrulline By similarity
Binding site951Citrulline By similarity
Binding site1201ATP; via amide nitrogen By similarity
Binding site1221Aspartate By similarity
Binding site1261Aspartate By similarity
Binding site1261Citrulline By similarity
Binding site1271Aspartate By similarity
Binding site1301Citrulline By similarity
Binding site1791Citrulline By similarity
Binding site1881Citrulline By similarity
Binding site2641Citrulline By similarity
Binding site2761Citrulline By similarity

Sequences

Sequence LengthMass (Da)Tools
C6E6Y6 [UniParc].

Last modified September 1, 2009. Version 1.
Checksum: 7E2591A89A4EAC47

FASTA40646,165
        10         20         30         40         50         60 
MAKKEVKKIV LAYSGGLDTS IILKWLKNEY GCEVVTFSAD LGQGDELEPV REKAFKTGAD 

        70         80         90        100        110        120 
KVYIDDLREE FVRDFVFPMF RANAIYEGSY LLGTSIARPL IAKRQMEIAQ IEGCDAVSHG 

       130        140        150        160        170        180 
ATGKGNDQVR FELAYYHFNP GITVVAPWRE WKLNSRQALI NYAKRNDIPI PITKKRPWSS 

       190        200        210        220        230        240 
DRNLLHISFE GGILEDTWLE PPENMFVLTK PPEKAPNKPQ YVEIEFEKGN AVAVDGVRMS 

       250        260        270        280        290        300 
PAELLAHLNT IGGEHGIGRV DLLENRSVGM KSRGVYETPG GTILREAHMA VEQITMDREV 

       310        320        330        340        350        360 
MHLRDSLIPR YAEMIYNGYW FSPEREMMQC MIDESQKTVN GVARLKLYKG HCRTVGRKSE 

       370        380        390        400 
SDSLFNLDFA TFEKDQVYNQ ADAEGFIKLN SLRLRIRSLM LANKNK 

« Hide

References

[1]"Complete sequence of Geobacter sp. M21."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G., Lovley D.
Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: M21.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001661 Genomic DNA. Translation: ACT19764.1.
RefSeqYP_003023522.1. NC_012918.1.

3D structure databases

ProteinModelPortalC6E6Y6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING443144.GM21_3745.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACT19764; ACT19764; GM21_3745.
GeneID8139119.
KEGGgem:GM21_3745.
PATRIC22021936. VBIGeoSp56140_3658.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycGSP443144:GHKM-3821-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_GEOSM
AccessionPrimary (citable) accession number: C6E6Y6
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: September 1, 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