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Q8GDU2 (ASSY_HELMO) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 57. 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
OrganismHeliobacillus mobilis
Taxonomic identifier28064 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesHeliobacteriaceaeHeliobacillus

Protein attributes

Sequence length408 AA.
Sequence statusFragment.
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
Gene Ontology (GO)
   Biological_processarginine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

argininosuccinate synthase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – ›408›408Argininosuccinate synthase HAMAP-Rule MF_00005
PRO_0000148598

Regions

Nucleotide binding14 – 229ATP By similarity

Sites

Binding site411ATP; via amide nitrogen and carbonyl oxygen By similarity
Binding site921Citrulline By similarity
Binding site971Citrulline By similarity
Binding site1221ATP; via amide nitrogen By similarity
Binding site1241Aspartate By similarity
Binding site1281Aspartate By similarity
Binding site1281Citrulline By similarity
Binding site1291Aspartate By similarity
Binding site1321Citrulline By similarity
Binding site1811Citrulline By similarity
Binding site1901Citrulline By similarity
Binding site2661Citrulline By similarity
Binding site2781Citrulline By similarity

Experimental info

Non-terminal residue4081

Sequences

Sequence LengthMass (Da)Tools
Q8GDU2 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 9B4DEC08F0640542

FASTA40845,642
        10         20         30         40         50         60 
MKGALGMSKK VVLAYSGGLD TSIIIPWLKE NYGYEVIAMA ADLGQGEELE PLNEKAINTG 

        70         80         90        100        110        120 
ATKIYIEDVK EEFVTEFIWP TLKAGAVYEG KYLLGTSFAR PLIAKRLVEI ARKEGAEAIA 

       130        140        150        160        170        180 
HGATGKGNDQ VRFELTVKAL APDLKIVAPW REWDIRSRED AIDYAQARNI PVPVKKDRPY 

       190        200        210        220        230        240 
SMDRNLWHLS HEGADLESPW NEPQNDLFMI CTPPEQAPDK PEYVEIEFEK GIPVKLNGEA 

       250        260        270        280        290        300 
LGPVEMIEKL NAIAAAHGVG ICDMVENRLV GMKSRGVYET PAGTVLYAAH RELEYLCLDR 

       310        320        330        340        350        360 
ATMHYKEMVA LRYAELVYDG VWYHPLRKAI DAFVDVTQET VTGLVRMKLF KGSVTPAGAK 

       370        380        390        400 
SPYSLYNEEF STFGRDEVYN QKDAEGFINL FGLPMKVRAL MEQKSGLK 

« Hide

References

[1]"Whole-genome analysis of photosynthetic prokaryotes."
Raymond J., Zhaxybayeva O., Gogarten J.P., Gerdes S.Y., Blankenship R.E.
Science 298:1616-1620(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY142882 Genomic DNA. Translation: AAN87486.1.

3D structure databases

ProteinModelPortalQ8GDU2.
SMRQ8GDU2. Positions 10-403.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

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_HELMO
AccessionPrimary (citable) accession number: Q8GDU2
Entry history
Integrated into UniProtKB/Swiss-Prot: April 23, 2003
Last sequence update: March 1, 2003
Last modified: February 19, 2014
This is version 57 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