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A8LPE0 (ASSY_DINSH) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 46. 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:Dshi_3472
OrganismDinoroseobacter shibae (strain DSM 16493 / NCIMB 14021 / DFL 12) [Complete proteome] [HAMAP]
Taxonomic identifier398580 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeDinoroseobacter

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_1000073819

Regions

Nucleotide binding10 – 189ATP By similarity

Sites

Binding site371ATP; via amide nitrogen and carbonyl oxygen By similarity
Binding site881Citrulline By similarity
Binding site931Citrulline By similarity
Binding site1181ATP; via amide nitrogen By similarity
Binding site1201Aspartate By similarity
Binding site1241Aspartate By similarity
Binding site1241Citrulline By similarity
Binding site1251Aspartate By similarity
Binding site1281Citrulline By similarity
Binding site1791Citrulline By similarity
Binding site1881Citrulline By similarity
Binding site2641Citrulline By similarity
Binding site2761Citrulline By similarity

Sequences

Sequence LengthMass (Da)Tools
A8LPE0 [UniParc].

Last modified December 4, 2007. Version 1.
Checksum: C0EEE8D18B28D0D4

FASTA40644,777
        10         20         30         40         50         60 
MSAPKKVVLA YSGGLDTSII LKWLQTEYDC EVVTFTADLG QGEELEPARA KAEMMGASAI 

        70         80         90        100        110        120 
YIEDLREEFV RDFVFPMFRA NAVYEGLYLL GTSIARPLIS KRLVEIAEAE GADAVAHGAT 

       130        140        150        160        170        180 
GKGNDQVRFE LAAYALNPDI KVIAPWREWD LSSRTKLIDF AEKHQIPIAK DKRGEAPFSV 

       190        200        210        220        230        240 
DANLLHTSSE GKVLEDPAED APDYVYQRTV NPEDAPNTPE YIEVGFERGD AVSINGEAMS 

       250        260        270        280        290        300 
PATVLTKLNE LGGAHGIGRL DLVEGRFVGM KSRGIYETPG GTILLEAHRG IEQITLDRGA 

       310        320        330        340        350        360 
AHLKDELMPR YAELIYNGFW FSPEREMLQA AIDASQAHVT GTVRLKLYKG SVRTVGRWSD 

       370        380        390        400 
HSLYSEAHVT FEDDAGAYDQ KDAAGFIQLN ALRLKLLAAR NKRLGK 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000830 Genomic DNA. Translation: ABV95205.1.
RefSeqYP_001534806.1. NC_009952.1.

3D structure databases

ProteinModelPortalA8LPE0.
SMRA8LPE0. Positions 6-398.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING398580.Dshi_3472.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABV95205; ABV95205; Dshi_3472.
GeneID5712530.
KEGGdsh:Dshi_3472.
PATRIC21819755. VBIDinShi9476_3606.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycDSHI398580:GKEL-3513-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_DINSH
AccessionPrimary (citable) accession number: A8LPE0
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: December 4, 2007
Last modified: March 19, 2014
This is version 46 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