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

Q9X2A1 (ASSY_THEMA) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 94. 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:TM_1780
OrganismThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099) [Reference proteome] [HAMAP]
Taxonomic identifier243274 [NCBI]
Taxonomic lineageBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga

Protein attributes

Sequence length409 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

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 – 409409Argininosuccinate synthase HAMAP-Rule MF_00005
PRO_0000148656

Regions

Nucleotide binding8 – 169ATP By similarity

Sites

Binding site341ATP; via amide nitrogen and carbonyl oxygen By similarity
Binding site851Citrulline By similarity
Binding site1151ATP; via amide nitrogen By similarity
Binding site1171Aspartate By similarity
Binding site1211Aspartate By similarity
Binding site1211Citrulline By similarity
Binding site1221Aspartate By similarity
Binding site1251Citrulline By similarity
Binding site1781Citrulline By similarity
Binding site1871Citrulline By similarity
Binding site2681Citrulline By similarity
Binding site2801Citrulline By similarity

Secondary structure

.................................................................. 409
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9X2A1 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: ECCDC8575E962482

FASTA40946,054
        10         20         30         40         50         60 
MKEKVVLAYS GGLDTSVILK WLCEKGFDVI AYVANVGQKD DFVAIKEKAL KTGASKVYVE 

        70         80         90        100        110        120 
DLRREFVTDY IFTALLGNAM YEGRYLLGTA IARPLIAKRQ VEIAEKEGAQ YVAHGATGKG 

       130        140        150        160        170        180 
NDQVRFELTY AALNPNLKVI SPWKDPEFLA KFKGRTDLIN YAMEKGIPIK VSKKRPYSED 

       190        200        210        220        230        240 
ENLMHISHEA GKLEDPAHIP DEDVFTWTVS PKDAPDEETL LEIHFENGIP VKVVNLKDGT 

       250        260        270        280        290        300 
EKTDPLELFE YLNEVGAKNG VGRLDMVENR FIGIKSRGVY ETPGATILWI AHRDLEGITM 

       310        320        330        340        350        360 
DKEVMHLRDM LAPKFAELIY NGFWFSPEME FLLAAFRKAQ ENVTGKVTVS IYKGNVMPVA 

       370        380        390        400 
RYSPYSLYNP ELSSMDVEGG FDATDSKGFI NIHALRLKVH QLVKKGYQR 

« Hide

References

« Hide 'large scale' references
[1]"Evidence for lateral gene transfer between Archaea and Bacteria from genome sequence of Thermotoga maritima."
Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M., Cotton M.D., Pratt M.S. expand/collapse author list , Phillips C.A., Richardson D.L., Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.
Nature 399:323-329(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
[2]"Crystal structure of argininosuccinate synthase (TM1780) from Thermotoga maritima at 1.65 A resolution."
Joint center for structural genomics (JCSG)
Submitted (MAR-2006) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS), SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000512 Genomic DNA. Translation: AAD36844.1.
PIRH72210.
RefSeqNP_229577.1. NC_000853.1.
YP_007978138.1. NC_021214.1.
YP_008991121.1. NC_023151.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1VL2X-ray1.65A/B/C/D1-409[»]
ProteinModelPortalQ9X2A1.
SMRQ9X2A1. Positions 2-409.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243274.TM1780.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAD36844; AAD36844; TM_1780.
GeneID15495547.
18092910.
897844.
KEGGtma:TM1780.
tmm:Tmari_1789.
PATRIC23938542. VBITheMar51294_1799.

Phylogenomic databases

eggNOGCOG0137.
KOK01940.
OMAIYNGYWW.
OrthoDBEOG6K9QCV.
ProtClustDBPRK00509.

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...

Other

EvolutionaryTraceQ9X2A1.

Entry information

Entry nameASSY_THEMA
AccessionPrimary (citable) accession number: Q9X2A1
Entry history
Integrated into UniProtKB/Swiss-Prot: October 19, 2002
Last sequence update: November 1, 1999
Last modified: March 19, 2014
This is version 94 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