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Q2K3B7 (ASSY_RHIEC) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 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:RHE_CH03924
OrganismRhizobium etli (strain CFN 42 / ATCC 51251) [Complete proteome] [HAMAP]
Taxonomic identifier347834 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Rhizobiaceae › Rhizobium/Agrobacterium group › Rhizobium ›

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: 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 – 407407Argininosuccinate synthase HAMAP-Rule MF_00005
PRO_0000263960

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
Q2K3B7 [UniParc].

Last modified March 7, 2006. Version 1.
Checksum: 9EFA7ACA0D053034

FASTA40745,213
        10         20         30         40         50         60 
MASYKDVKKV VLAYSGGLDT SIILKWLQTE LGAEVVTFTA DLGQGEELEP ARKKAEMLGI 

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

       130        140        150        160        170        180 
GATGKGNDQV RFELSAYALN PDIKIIAPWR DWAFKSRTEL LAFAEQHQIP VAKDKKGEAP 

       190        200        210        220        230        240 
FSVDANLLHS SSEGKVLEDP AQEAPEYVHM RTISPEAAPD KATVIKVGFR KGDAVSINGV 

       250        260        270        280        290        300 
EMSPATLLAT LNTYGRDNGI GRLDLVENRF VGMKSRGVYE TPGGTILLSA HRAIESITLD 

       310        320        330        340        350        360 
RGAAHLKDEI MPRYAELIYY GFWFSPEREM LQALIDKSQE YVEGEVTLKL YKGNVMVIGR 

       370        380        390        400 
ESEKSLYSDK LVTFEDDQGA YDQKDAAGFI KLNALRLRTL GKRNLAK

« Hide

References

[1]"The partitioned Rhizobium etli genome: genetic and metabolic redundancy in seven interacting replicons."
Gonzalez V., Santamaria R.I., Bustos P., Hernandez-Gonzalez I., Medrano-Soto A., Moreno-Hagelsieb G., Janga S.C., Ramirez M.A., Jimenez-Jacinto V., Collado-Vides J., Davila G.
Proc. Natl. Acad. Sci. U.S.A. 103:3834-3839(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CFN 42 / ATCC 51251.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000133 Genomic DNA. Translation: ABC92669.1.
RefSeqYP_471396.1. NC_007761.1.

3D structure databases

ProteinModelPortalQ2K3B7.
SMRQ2K3B7. Positions 9-398.
ModBaseSearch...

Protein-protein interaction databases

STRING347834.RHE_CH03924.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABC92669; ABC92669; RHE_CH03924.
GeneID3894174.
KEGGret:RHE_CH03924.
PATRIC23089588. VBIRhiEtl108884_4428.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0137.
HOGENOMHOG000230093.
KOK01940.
OMAIYNGYWW.
ProtClustDBPRK00509.

Enzyme and pathway databases

BioCycRETL347834:GJJ0-3942-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]
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_RHIEC
AccessionPrimary (citable) accession number: Q2K3B7
Entry history
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: March 7, 2006
Last modified: May 29, 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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