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Q1QVN0 (ASSY_CHRSD) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 49. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:Csal_2127
OrganismChromohalobacter salexigens (strain DSM 3043 / ATCC BAA-138 / NCIMB 13768) [Complete proteome] [HAMAP]
Taxonomic identifier290398 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Oceanospirillales › Halomonadaceae › Chromohalobacter ›

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.

Subcellular location

Cytoplasm By similarity.

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: HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: HAMAP

argininosuccinate synthase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 406406Argininosuccinate synthase HAMAP-Rule MF_00005
PRO_0000263912

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 site1801Citrulline By similarity
Binding site1891Citrulline By similarity
Binding site2651Citrulline By similarity
Binding site2771Citrulline By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1QVN0 [UniParc].

Last modified May 16, 2006. Version 1.
Checksum: 12B113596AE48634

FASTA40645,409
        10         20         30         40         50         60 
MSDVKKVVLA YSGGLDTSVI VKWLQETYDC EVVTFTADIG QGEEVEPARA KAQALGVKEI 

        70         80         90        100        110        120 
YIEDLREEFV RDYVYPMFRA NTIYEGEYLL GTSIARPLIA KRLVEIANET GADAISHGAT 

       130        140        150        160        170        180 
GKGNDQVRFE LGAYALKPGV KVIAPWREWD LNSREKLMNY CEEHDIPVDF STSKKKSPYS 

       190        200        210        220        230        240 
MDANLLHISY EGGILEDPWA EAEEDMWRWS VSPEAAPEQP TYVELTFDKG DIVAIDGEPL 

       250        260        270        280        290        300 
KPHEVLSRLN RMGGDNGIGR LDIVENRYVG MKSRGCYETP GGTIMLRAHR AIESLTLDRE 

       310        320        330        340        350        360 
AAHLKDELMP KYAEVIYNGY WWSPERKMLQ AAIDATQDNV NGVVRMKLYK GSATVVGRKS 

       370        380        390        400 
EQSLFDASIA TFEDDAGAYD QKDAEGFIKL NALRLRIAAG KGRQAD

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000285 Genomic DNA. Translation: ABE59478.1.
RefSeqYP_574177.1. NC_007963.1.

3D structure databases

ProteinModelPortalQ1QVN0.
SMRQ1QVN0. Positions 6-399.
ModBaseSearch...

Protein-protein interaction databases

STRING290398.Csal_2127.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABE59478; ABE59478; Csal_2127.
GeneID4026463.
KEGGcsa:Csal_2127.
PATRIC21448096. VBIChrSal113723_2146.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0137.
HOGENOMHOG000230093.
KOK01940.
OMAIYNGYWW.
ProtClustDBPRK00509.

Enzyme and pathway databases

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]
PANTHERPTHR11587. PTHR11587. 1 hit.
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_CHRSD
AccessionPrimary (citable) accession number: Q1QVN0
Entry history
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: May 16, 2006
Last modified: May 1, 2013
This is version 49 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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