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Q1MAN9 (ASSY2_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 2

EC=6.3.4.5
Alternative name(s):
Citrulline--aspartate ligase 2
Gene names
Name:argG2
Ordered Locus Names:RL4515
OrganismRhizobium leguminosarum bv. viciae (strain 3841) [Complete proteome] [HAMAP]
Taxonomic identifier216596 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeRhizobium/Agrobacterium groupRhizobium

Protein attributes

Sequence length407 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 – 407407Argininosuccinate synthase 2 HAMAP-Rule MF_00005
PRO_0000263962

Regions

Nucleotide binding13 – 219ATP By similarity

Sites

Binding site401ATP; via amide nitrogen and carbonyl oxygen By similarity
Binding site911Citrulline By similarity
Binding site961Citrulline By similarity
Binding site1211ATP; via amide nitrogen By similarity
Binding site1231Aspartate By similarity
Binding site1271Aspartate By similarity
Binding site1271Citrulline By similarity
Binding site1281Aspartate By similarity
Binding site1311Citrulline By similarity
Binding site1821Citrulline By similarity
Binding site1911Citrulline By similarity
Binding site2671Citrulline By similarity
Binding site2791Citrulline By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1MAN9 [UniParc].

Last modified May 30, 2006. Version 1.
Checksum: FD48DFBDB2D285DD

FASTA40745,177
        10         20         30         40         50         60 
MASYKDVKKV VLAYSGGLDT SIILKWLQTE LGAEVVTFTA DLGQGEELEP ARKKAEMLGI 

        70         80         90        100        110        120 
KEIYIEDVRE EFVRDFVFPM FRANAVYEGV YLLGTSIARP LISKHLIDIA KKTGADAIAH 

       130        140        150        160        170        180 
GATGKGNDQV RFELSAYALN PDIKIIAPWR DWAFKSRTDL LAFAEQHQIP VAKDKMGEAP 

       190        200        210        220        230        240 
FSVDANLLHS SSEGKVLEDP SQEAPEYVHM RTISPEAAPD KATTIKVGFE KGDAVSINGV 

       250        260        270        280        290        300 
RMSPATLLAA LNNYGRDNGI GRLDLVENRF VGMKSRGVYE TPGGTILLTA HRAIESITLD 

       310        320        330        340        350        360 
RGAAHLKDDI MPRYAELIYY GFWFSPEREM LQALIDKSQE HVEGEVTLKL YKGNVMVIGR 

       370        380        390        400 
ESDKSLYSDK LVTFEDDQGA YDQKDAAGFI KLNALRLRTL AKRNLVK 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM236080 Genomic DNA. Translation: CAK09999.1.
RefSeqYP_770080.1. NC_008380.1.

3D structure databases

ProteinModelPortalQ1MAN9.
SMRQ1MAN9. Positions 9-401.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING216596.RL4515.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAK09999; CAK09999; RL4515.
GeneID4400741.
KEGGrle:RL4515.
PATRIC23145901. VBIRhiLeg32091_5853.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0137.
HOGENOMHOG000230093.
KOK01940.
OMAGIKSKFD.
OrthoDBEOG6K9QCV.
ProtClustDBPRK00509.

Enzyme and pathway databases

BioCycRLEG216596:GKE5-4590-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 nameASSY2_RHIL3
AccessionPrimary (citable) accession number: Q1MAN9
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