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Q97A55 (ASSY_THEVO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 78. 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:TV0955
ORF Names:TVG0979194
OrganismThermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1) [Complete proteome] [HAMAP]
Taxonomic identifier273116 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaThermoplasmataThermoplasmatalesThermoplasmataceaeThermoplasma

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 BAB60097.1 differs from that shown. Reason: Erroneous termination at position 62. Translated as Lys.

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 – 397397Argininosuccinate synthase HAMAP-Rule MF_00005
PRO_0000148689

Regions

Nucleotide binding7 – 159ATP By similarity

Sites

Binding site831Citrulline By similarity
Binding site1131ATP; via amide nitrogen By similarity
Binding site1151Aspartate By similarity
Binding site1191Aspartate By similarity
Binding site1191Citrulline By similarity
Binding site1201Aspartate By similarity
Binding site1231Citrulline By similarity
Binding site1691Citrulline By similarity
Binding site1781Citrulline By similarity
Binding site2531Citrulline By similarity
Binding site2651Citrulline By similarity

Sequences

Sequence LengthMass (Da)Tools
Q97A55 [UniParc].

Last modified February 20, 2007. Version 3.
Checksum: 2A0DBCDF55AD880F

FASTA39744,342
        10         20         30         40         50         60 
MKELLLLYSG GLDTSVMIKW MNENLGYDVS TLTLDIGNND LKSIREKAEA IGAVETFVED 

        70         80         90        100        110        120 
VKQEFSYEYI SKSILANGSY EGYPLSTALA RPLMAKKAVE LAEKHGFEAI AHGSTGRGND 

       130        140        150        160        170        180 
QVRFELGIKA LNPSLEMLAP VRDWNMLRSE EIEYAKKNNI IVPSDGKYSV DENLWGRSIE 

       190        200        210        220        230        240 
GSEIENMSLP VPEDAYEWLV PPWEAGPGEV IKLEFSNGLP VAINDSDFEL QNLIANLNII 

       250        260        270        280        290        300 
GGRNSIGLID HVEDRITGIK SREVYECPAA EIITYAHGYL ESLILNKHEI SIKSFLDSKF 

       310        320        330        340        350        360 
SQFVYNGLWY DPAMKPLIAG EEILNSEING SISLKLYKGK IYFNGSKGAN FSYNSNVANY 

       370        380        390 
STYEFDQKSS KGFIDIFKND TVYSILARQK AKEEALS 

« Hide

References

[1]"Archaeal adaptation to higher temperatures revealed by genomic sequence of Thermoplasma volcanium."
Kawashima T., Amano N., Koike H., Makino S., Higuchi S., Kawashima-Ohya Y., Watanabe K., Yamazaki M., Kanehori K., Kawamoto T., Nunoshiba T., Yamamoto Y., Aramaki H., Makino K., Suzuki M.
Proc. Natl. Acad. Sci. U.S.A. 97:14257-14262(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000011 Genomic DNA. Translation: BAB60097.1. Sequence problems.
RefSeqNP_111446.1. NC_002689.2.

3D structure databases

ProteinModelPortalQ97A55.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING273116.TVN0927.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB60097; BAB60097; BAB60097.
GeneID1442033.
KEGGtvo:TVN0927.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0137.
KOK01940.
OMAAPPEEAY.

Enzyme and pathway databases

BioCycTVOL273116:GC31-954-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_THEVO
AccessionPrimary (citable) accession number: Q97A55
Entry history
Integrated into UniProtKB/Swiss-Prot: April 23, 2003
Last sequence update: February 20, 2007
Last modified: May 14, 2014
This is version 78 of the entry and version 3 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