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Q8ZU97 (ASSY_PYRAE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 81. 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:PAE2884
OrganismPyrobaculum aerophilum (strain ATCC 51768 / IM2 / DSM 7523 / JCM 9630 / NBRC 100827) [Reference proteome] [HAMAP]
Taxonomic identifier178306 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiThermoprotealesThermoproteaceaePyrobaculum

Protein attributes

Sequence length397 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.

Sequence caution

The sequence AAL64511.1 differs from that shown. Reason: Erroneous initiation.

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 – 397397Argininosuccinate synthase HAMAP-Rule MF_00005
PRO_0000148683

Regions

Nucleotide binding9 – 179ATP By similarity

Sites

Binding site871Citrulline By similarity
Binding site1171ATP; via amide nitrogen By similarity
Binding site1191Aspartate By similarity
Binding site1231Aspartate By similarity
Binding site1231Citrulline By similarity
Binding site1241Aspartate By similarity
Binding site1271Citrulline By similarity
Binding site1741Citrulline By similarity
Binding site1831Citrulline By similarity
Binding site2591Citrulline By similarity
Binding site2711Citrulline By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8ZU97 [UniParc].

Last modified October 19, 2002. Version 2.
Checksum: A1A8D70BEE2B7A09

FASTA39744,421
        10         20         30         40         50         60 
MGASKIVLAY SGGLDTTVAV KWLSEKFGAE VYTVTVDVGQ EDDFSKIEER AYKAGAVQHF 

        70         80         90        100        110        120 
YIDAKREFAE EYIARAILMN GMYEGVYPLG TALARPLIAA KVVEVARRLG ADAVAHGSTS 

       130        140        150        160        170        180 
KGNDQVRFDV TVKALAPDLK IIAPARIWGM TRAEEIEYAK RHGLPVGEEH KKYSIDDNLW 

       190        200        210        220        230        240 
SRSIEGGPID DPLAEPPEDA FKWTVSPDKA PHDPTYLTIE FEKGLPVAVN GEKMSLASII 

       250        260        270        280        290        300 
SLLNHVGGAN GVGRIDHIEN RLVGFKSREV YEAPAAVILY HAHRDLEKMV LTPRELRFKH 

       310        320        330        340        350        360 
YVLDPQWADL VYQGLWVEPL RNALEKAAEE MERWVSGEVR VKLYKGSLWV VGRESPYGGY 

       370        380        390 
SKELADYSAG WYPSDEEARG FIEMWSLHSL TALRRRK 

« Hide

References

[1]"Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum aerophilum."
Fitz-Gibbon S.T., Ladner H., Kim U.-J., Stetter K.O., Simon M.I., Miller J.H.
Proc. Natl. Acad. Sci. U.S.A. 99:984-989(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 51768 / IM2 / DSM 7523 / JCM 9630 / NBRC 100827.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE009441 Genomic DNA. Translation: AAL64511.1. Different initiation.
RefSeqNP_560329.1. NC_003364.1.

3D structure databases

ProteinModelPortalQ8ZU97.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING178306.PAE2884.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL64511; AAL64511; PAE2884.
GeneID1463673.
KEGGpai:PAE2884.

Phylogenomic databases

eggNOGCOG0137.
HOGENOMHOG000230093.
KOK01940.
OMARFESTIR.

Enzyme and pathway databases

BioCycPAER178306:GCEO-2080-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_PYRAE
AccessionPrimary (citable) accession number: Q8ZU97
Entry history
Integrated into UniProtKB/Swiss-Prot: October 19, 2002
Last sequence update: October 19, 2002
Last modified: May 14, 2014
This is version 81 of the entry and version 2 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