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Q3IYJ1 (ASSY_RHOS4) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 58. 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:RHOS4_28250
ORF Names:RSP_1212
OrganismRhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158) [Reference proteome] [HAMAP]
Taxonomic identifier272943 [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
Reference 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_0000263963

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
Q3IYJ1 [UniParc].

Last modified November 8, 2005. 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 sequence of chromosome 1 of Rhodobacter sphaeroides 2.4.1."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C., Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., Kaplan S.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000143 Genomic DNA. Translation: ABA80393.1.
RefSeqYP_354294.1. NC_007493.2.

3D structure databases

ProteinModelPortalQ3IYJ1.
SMRQ3IYJ1. Positions 6-400.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272943.RSP_1212.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABA80393; ABA80393; RSP_1212.
GeneID3720240.
KEGGrsp:RSP_1212.
PATRIC23155657. VBIRhoSph57909_3193.

Phylogenomic databases

eggNOGCOG0137.
HOGENOMHOG000230093.
KOK01940.
OMAIYNGYWW.
OrthoDBEOG6K9QCV.
ProtClustDBPRK00509.

Enzyme and pathway databases

BioCycRSPH272943:GJAS-2893-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_RHOS4
AccessionPrimary (citable) accession number: Q3IYJ1
Entry history
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: November 8, 2005
Last modified: February 19, 2014
This is version 58 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