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B9KPT5 (ASSY_RHOSK) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 38. 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:RSKD131_2610
OrganismRhodobacter sphaeroides (strain KD131 / KCTC 12085) [Complete proteome] [HAMAP]
Taxonomic identifier557760 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRhodobacter

Protein attributes

Sequence length408 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 – 408408Argininosuccinate synthase HAMAP-Rule MF_00005
PRO_1000116290

Regions

Nucleotide binding10 – 189ATP By similarity

Sites

Binding site371ATP; via amide nitrogen and carbonyl oxygen By similarity
Binding site901Citrulline By similarity
Binding site951Citrulline By similarity
Binding site1201ATP; via amide nitrogen By similarity
Binding site1221Aspartate By similarity
Binding site1261Aspartate By similarity
Binding site1261Citrulline By similarity
Binding site1271Aspartate By similarity
Binding site1301Citrulline By similarity
Binding site1811Citrulline By similarity
Binding site1901Citrulline By similarity
Binding site2661Citrulline By similarity
Binding site2781Citrulline By similarity

Sequences

Sequence LengthMass (Da)Tools
B9KPT5 [UniParc].

Last modified March 24, 2009. Version 1.
Checksum: AE24E105324E0927

FASTA40845,244
        10         20         30         40         50         60 
MSAPKKVVLA YSGGLDTSII LKWLQTEYGC EVVTFTADLG QGEELEPARE KAVMLGIKPE 

        70         80         90        100        110        120 
NIFIEDVREE FVRDFVFPMF RANALYEGLY LLGTSIARPL IAKRLVEIAA QTGADAVAHG 

       130        140        150        160        170        180 
ATGKGNDQVR FELTAYALDP AIKVIAPWRE WDLTSRTKLL EFAEQNQIPI AKNKRGEAPF 

       190        200        210        220        230        240 
SVDANLLHTS SEGRVLENPG EEAPDYVYQR TVDPEKAPDA PEFVEIAFEK GDAVAINGEA 

       250        260        270        280        290        300 
MSPATILTKL NELGGKHGVG RLDLVENRFV GMKSRGIYET PGGTILLEAH RGIEQITLDS 

       310        320        330        340        350        360 
GAGHLKDSIM PRYAELIYNG FWYSPEREML QALIDKSQEH VTGTVRVKLY KGFARTVARW 

       370        380        390        400 
SEHSLYSEKH VTFEEDAGAY DQKDAAGFIR LNALRLKLIA TRNARVKG 

« Hide

References

[1]"Complete genome sequence of Rhodobacter sphaeroides KD131."
Lim S.-K., Kim S.J., Cha S.H., Oh Y.-K., Rhee H.-J., Kim M.-S., Lee J.K.
J. Bacteriol. 191:1118-1119(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: KD131 / KCTC 12085.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001150 Genomic DNA. Translation: ACM02470.1.
RefSeqYP_002526971.1. NC_011963.1.

3D structure databases

ProteinModelPortalB9KPT5.
SMRB9KPT5. Positions 6-400.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING557760.RSKD131_2610.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACM02470; ACM02470; RSKD131_2610.
GeneID7360026.
KEGGrsk:RSKD131_2610.
PATRIC23184352. VBIRhoSph125910_4016.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0137.
HOGENOMHOG000230093.
KOK01940.
OMAAPPEEAY.
OrthoDBEOG6K9QCV.

Enzyme and pathway databases

BioCycRSPH557760:GH1P-2643-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_RHOSK
AccessionPrimary (citable) accession number: B9KPT5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 24, 2009
Last modified: May 14, 2014
This is version 38 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