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Q1MEZ8 (ASSY1_RHIL3) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 52. 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 1

EC=6.3.4.5
Alternative name(s):
Citrulline--aspartate ligase 1
Gene names
Name:argG1
Ordered Locus Names:RL2987
OrganismRhizobium leguminosarum bv. viciae (strain 3841) [Complete proteome] [HAMAP]
Taxonomic identifier216596 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeRhizobium/Agrobacterium groupRhizobium

Protein attributes

Sequence length403 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 – 403403Argininosuccinate synthase 1 HAMAP-Rule MF_00005
PRO_0000263961

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
Q1MEZ8 [UniParc].

Last modified May 30, 2006. Version 1.
Checksum: 4A143B783BBD0634

FASTA40344,319
        10         20         30         40         50         60 
MTKIEKIVLS YSGGLDTSII LKWLQETYGC EVVTFTADLG QGEELEPARA KAEMSGVKDI 

        70         80         90        100        110        120 
RIVDLREEFV SDFVFPMLRA NALYEGQYLL GSSIARPLIA KHLVGIAREV GADAVAHGAT 

       130        140        150        160        170        180 
GKGNDQIRFE LAVNALDPSI KVIAPWRQWN IRSRLQLSEY AEKHRIPVPS DKRGEAPFSI 

       190        200        210        220        230        240 
DANLLHTSTE GKSLENPAEV APDHVYQRTV DPVDAPDTPE IITVGFERGD PVSVNGKAMT 

       250        260        270        280        290        300 
PAALLTELNG LGGRHGVGRL DLVENRFIGM KSRGIYETPG GTILLAAHRG IESITLDRAA 

       310        320        330        340        350        360 
AHLKDEIMPR YAELIYNGFW FAPEREMLQA LIDHSQAFVS GEVTLRLYKG SASVISRASP 

       370        380        390        400 
CSLYSADLVT FEESTIAFDH HDAEGFIRLN GLRLRSWAAR NGR 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM236080 Genomic DNA. Translation: CAK08476.1.
RefSeqYP_768571.1. NC_008380.1.

3D structure databases

ProteinModelPortalQ1MEZ8.
SMRQ1MEZ8. Positions 6-395.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING216596.RL2987.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAK08476; CAK08476; RL2987.
GeneID4400740.
KEGGrle:RL2987.
PATRIC23142673. VBIRhiLeg32091_4258.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0137.
HOGENOMHOG000230093.
KOK01940.
OMAPCSLYSA.
OrthoDBEOG6K9QCV.
ProtClustDBPRK00509.

Enzyme and pathway databases

BioCycRLEG216596:GKE5-3035-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 nameASSY1_RHIL3
AccessionPrimary (citable) accession number: Q1MEZ8
Entry history
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: May 30, 2006
Last modified: February 19, 2014
This is version 52 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