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P61523 (ASSY_GEOSL) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 72. 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:GSU0153
OrganismGeobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA) [Reference proteome] [HAMAP]
Taxonomic identifier243231 [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
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 – 406406Argininosuccinate synthase HAMAP-Rule MF_00005
PRO_0000148595

Regions

Nucleotide binding14 – 229ATP By similarity

Sites

Binding site411ATP; via amide nitrogen and carbonyl oxygen By similarity
Binding site921Citrulline By similarity
Binding site971Citrulline By similarity
Binding site1221ATP; via amide nitrogen By similarity
Binding site1241Aspartate By similarity
Binding site1281Aspartate By similarity
Binding site1281Citrulline By similarity
Binding site1291Aspartate By similarity
Binding site1321Citrulline By similarity
Binding site1811Citrulline By similarity
Binding site1901Citrulline By similarity
Binding site2661Citrulline By similarity
Binding site2781Citrulline By similarity

Sequences

Sequence LengthMass (Da)Tools
P61523 [UniParc].

Last modified May 24, 2004. Version 1.
Checksum: 16AD280BD3ADA902

FASTA40645,657
        10         20         30         40         50         60 
MAKAHKDVKK IVLAYSGGLD TSIILKWLKN EYGCEVIAFS ADLGQGDELA PIRDKAIATG 

        70         80         90        100        110        120 
ADKVYIDDLK EEFVKDFVFP MFRANAIYEG HYLLGTSIAR PLIAKRQMEI AKIEGADAVS 

       130        140        150        160        170        180 
HGATGKGNDQ VRFELAYYHF DPAITVVAPW REWKLNSRQA LVNYARKNGI PIPVTKKRPW 

       190        200        210        220        230        240 
SSDRNLLHIS FEGGILEDTW AEPPENMYVL TKAPEKAPNK PQFVEIEFKN GNAVAVDGEK 

       250        260        270        280        290        300 
MSPAQLLAHL NYIGGEHGIG RVDLLENRSV GMKSRGVYET PGGTILREAH SAVEQITMDR 

       310        320        330        340        350        360 
EVMRIRDSLI PEYARQVYAG YWFSPEREML QTLIDDSQKC VNGVARVKLY KGHCRTVGRK 

       370        380        390        400 
SETNSLFNLD FATFEKDQVF NQADATGFIK INSLRLRIRS LMQGKK 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017180 Genomic DNA. Translation: AAR33488.1.
RefSeqNP_951215.1. NC_002939.5.

3D structure databases

ProteinModelPortalP61523.
SMRP61523. Positions 10-403.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243231.GSU0153.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAR33488; AAR33488; GSU0153.
GeneID2687910.
KEGGgsu:GSU0153.
PATRIC22023054. VBIGeoSul17553_0154.

Phylogenomic databases

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

Enzyme and pathway databases

BioCycGSUL243231:GH27-159-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_GEOSL
AccessionPrimary (citable) accession number: P61523
Entry history
Integrated into UniProtKB/Swiss-Prot: May 24, 2004
Last sequence update: May 24, 2004
Last modified: February 19, 2014
This is version 72 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