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Q2RG67 (ASSY_MOOTA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 58. 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:Moth_2285
OrganismMoorella thermoacetica (strain ATCC 39073) [Reference proteome] [HAMAP]
Taxonomic identifier264732 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaThermoanaerobacteralesThermoanaerobacteraceaeMoorella groupMoorella

Protein attributes

Sequence length408 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.

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 – 408408Argininosuccinate synthase HAMAP-Rule MF_00005
PRO_0000263940

Regions

Nucleotide binding14 – 229ATP By similarity

Sites

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

Sequences

Sequence LengthMass (Da)Tools
Q2RG67 [UniParc].

Last modified January 24, 2006. Version 1.
Checksum: E9BDFD1EFB8681D6

FASTA40844,870
        10         20         30         40         50         60 
MKGVFTVAEK VVLAYSGGLD TSIIIPWLKE TYGYEVIAVA VDVGQGEELE PLEEKAIKSG 

        70         80         90        100        110        120 
ASKIYILDKK KEFVEEYIWP TLKAGAVYEG KYLLGTSFAR PLIAKCLVEV AAQEGATAVA 

       130        140        150        160        170        180 
HGATGKGNDQ VRFELGVKAL NPQLKVIAPW RIWNIRSREE AMDYAAARGI PVPVTKDRPY 

       190        200        210        220        230        240 
SMDRNLWHLS HEGGDLEDPW NAPGDDLYLI ITPPEQAPDK PTYVTIDFEK GIPVAVDGEK 

       250        260        270        280        290        300 
LDAVALVEKL NDLAAANGVG IVDIVENRLV GMKSRGVYET PGGTILYTAH RELEYLTLDR 

       310        320        330        340        350        360 
MTMHFKEMVA AKYAELVYDG NWFSPLKKAL DAFVDSTQET VTGTVRLKLY KGSCTPAGVK 

       370        380        390        400 
SPYSIYNEDL VTFGAGGDYD HKDATGFINL FGLPLKVRAL MEQKTGLR 

« Hide

References

[1]"The complete genome sequence of Moorella thermoacetica (f. Clostridium thermoaceticum)."
Pierce E., Xie G., Barabote R.D., Saunders E., Han C.S., Detter J.C., Richardson P., Brettin T.S., Das A., Ljungdahl L.G., Ragsdale S.W.
Environ. Microbiol. 10:2550-2573(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 39073.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000232 Genomic DNA. Translation: ABC20572.1.
RefSeqYP_431115.1. NC_007644.1.

3D structure databases

ProteinModelPortalQ2RG67.
SMRQ2RG67. Positions 10-403.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING264732.Moth_2285.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABC20572; ABC20572; Moth_2285.
GeneID3831317.
KEGGmta:Moth_2285.
PATRIC22642042. VBIMooThe6753_2489.

Phylogenomic databases

eggNOGCOG0137.
HOGENOMHOG000230093.
KOK01940.
OMAAPPEEAY.
OrthoDBEOG6K9QCV.

Enzyme and pathway databases

BioCycMTHE264732:GH0A-2366-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_MOOTA
AccessionPrimary (citable) accession number: Q2RG67
Entry history
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: January 24, 2006
Last modified: May 14, 2014
This is version 58 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