Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P59846 (ASSY_THET8) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 83. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:TTHA0284
OrganismThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) [Reference proteome] [HAMAP]
Taxonomic identifier300852 [NCBI]
Taxonomic lineageBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus

Protein attributes

Sequence length400 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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. Ref.2 Ref.3

Subcellular location

Cytoplasm Probable 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 term3D-structure
Complete 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 – 400400Argininosuccinate synthase HAMAP-Rule MF_00005
PRO_0000148658

Regions

Nucleotide binding6 – 149ATP HAMAP-Rule MF_00005

Sites

Binding site331ATP; via amide nitrogen and carbonyl oxygen
Binding site841Citrulline
Binding site891Citrulline
Binding site1141ATP; via amide nitrogen
Binding site1161Aspartate
Binding site1201Aspartate
Binding site1201Citrulline
Binding site1211Aspartate
Binding site1241Citrulline
Binding site1731Citrulline
Binding site1821Citrulline
Binding site2581Citrulline
Binding site2701Citrulline

Secondary structure

................................................................. 400
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P59846 [UniParc].

Last modified September 19, 2003. Version 1.
Checksum: A4DAC90A7C5185C6

FASTA40044,816
        10         20         30         40         50         60 
MKIVLAYSGG LDTSIILKWL KETYRAEVIA FTADIGQGEE VEEAREKALR TGASKAIALD 

        70         80         90        100        110        120 
LKEEFVRDFV FPMMRAGAVY EGYYLLGTSI ARPLIAKHLV RIAEEEGAEA IAHGATGKGN 

       130        140        150        160        170        180 
DQVRFELTAY ALKPDIKVIA PWREWSFQGR KEMIAYAEAH GIPVPVTQEK PYSMDANLLH 

       190        200        210        220        230        240 
ISYEGGVLED PWAEPPKGMF RMTQDPEEAP DAPEYVEVEF FEGDPVAVNG ERLSPAALLQ 

       250        260        270        280        290        300 
RLNEIGGRHG VGRVDIVENR FVGMKSRGVY ETPGGTILYH ARRAVESLTL DREVLHQRDM 

       310        320        330        340        350        360 
LSPKYAELVY YGFWYAPERE ALQAYFDHVA RSVTGVARLK LYKGNVYVVG RKAPKSLYRQ 

       370        380        390        400 
DLVSFDEAGG YDQKDAEGFI KIQALRLRVR ALVEREGHGA 

« Hide

References

« Hide 'large scale' references
[1]"Complete genome sequence of Thermus thermophilus HB8."
Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T., Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HB8 / ATCC 27634 / DSM 579.
[2]"Crystal structure of argininosuccinate synthetase from Thermus thermophilus HB8. Structural basis for the catalytic action."
Goto M., Nakajima Y., Hirotsu K.
J. Biol. Chem. 277:15890-15896(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH ATP AND SUBSTRATE ANALOGS, SUBUNIT.
[3]"Structures of argininosuccinate synthetase in enzyme-ATP substrates and enzyme-AMP product forms: stereochemistry of the catalytic reaction."
Goto M., Omi R., Miyahara I., Sugahara M., Hirotsu K.
J. Biol. Chem. 278:22964-22971(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH ATP AND SUBSTRATES, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP008226 Genomic DNA. Translation: BAD70107.1.
RefSeqYP_143550.1. NC_006461.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1J1ZX-ray2.10A/B/C/D1-400[»]
1J20X-ray2.00A/B/C/D1-400[»]
1J21X-ray2.20A/B/C/D1-400[»]
1KH1X-ray2.30A/B/C/D1-400[»]
1KH2X-ray2.30A/B/C/D1-400[»]
1KH3X-ray2.15A/B/C/D1-400[»]
1KORX-ray1.95A/B/C/D1-400[»]
ProteinModelPortalP59846.
SMRP59846. Positions 1-395.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING300852.TTHA0284.

Chemistry

DrugBankDB00131. Adenosine monophosphate.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAD70107; BAD70107; BAD70107.
GeneID3168176.
KEGGttj:TTHA0284.
PATRIC23955523. VBITheThe93045_0284.

Phylogenomic databases

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

Enzyme and pathway databases

BioCycTTHE300852:GH8R-298-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...

Other

EvolutionaryTraceP59846.

Entry information

Entry nameASSY_THET8
AccessionPrimary (citable) accession number: P59846
Secondary accession number(s): Q5SLK9
Entry history
Integrated into UniProtKB/Swiss-Prot: September 19, 2003
Last sequence update: September 19, 2003
Last modified: February 19, 2014
This is version 83 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways