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Q2NEC4 (ASSY_METST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 50. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:Msp_1459
OrganismMethanosphaera stadtmanae (strain DSM 3091) [Complete proteome] [HAMAP]
Taxonomic identifier339860 [NCBI]
Taxonomic lineageArchaea › Euryarchaeota › Methanobacteria › Methanobacteriales › Methanobacteriaceae › Methanosphaera ›

Protein attributes

Sequence length392 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.

Subcellular location

Cytoplasm By similarity.

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
Gene Ontology (GO)
   Biological_processarginine biosynthetic process

Inferred from electronic annotation. Source: HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: HAMAP

argininosuccinate synthase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 392392Argininosuccinate synthase HAMAP-Rule MF_00005
PRO_0000263996

Regions

Nucleotide binding7 – 159ATP By similarity

Sites

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 site1701Citrulline By similarity
Binding site1791Citrulline By similarity
Binding site2551Citrulline By similarity
Binding site2671Citrulline By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2NEC4 [UniParc].

Last modified February 7, 2006. Version 1.
Checksum: 0BD488B9B778AD70

FASTA39244,224
        10         20         30         40         50         60 
MEKVVLAFSG GLDTSVCVKL LQEKYNMEVI TACVDVGQPE DEIKKPEAAA QKIGSDKHYT 

        70         80         90        100        110        120 
IDAKDEFAKE YAFRCIKTNS LYEGYPLSTA YARPLIAKKI VEIAKKENAS TIAHGCTGKG 

       130        140        150        160        170        180 
NDQFRFEATI RSESDLDIVA PVRDYNLTRT EEQDYAREHG IPLPSEKIYS IDENLWGRSI 

       190        200        210        220        230        240 
EGGLLENPAT AAPEEIYEWT KSTVDAPETP QIVKIEFVNG EPVKINDEEL EPVALIRKAN 

       250        260        270        280        290        300 
EIAGNNGIGR IDMVEDRIIG LKSRENYETP GAILLITAHA ALEKLIFSRE EIKFAENLSQ 

       310        320        330        340        350        360 
KYAELVYNGL WNEPLREDLD VVNDHMQQRV TGTVEVRLHK GSMKVITKES PYALYNEENV 

       370        380        390 
SFEDKGIDQR EMIGMVKYYD LQGAEYSKVK RE

« Hide

References

[1]"The genome sequence of Methanosphaera stadtmanae reveals why this human intestinal archaeon is restricted to methanol and H2 for methane formation and ATP synthesis."
Fricke W.F., Seedorf H., Henne A., Kruer M., Liesegang H., Hedderich R., Gottschalk G., Thauer R.K.
J. Bacteriol. 188:642-658(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 3091.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000102 Genomic DNA. Translation: ABC57829.1.
RefSeqYP_448472.1. NC_007681.1.

3D structure databases

HSSPHSSP built from PDB template 1VL2 based on UniProtKB Q9X2A1.
ProteinModelPortalQ2NEC4.
ModBaseSearch...

Protein-protein interaction databases

STRING339860.Msp_1459.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABC57829; ABC57829; Msp_1459.
GeneID3856091.
KEGGmst:Msp_1459.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0137.
HOGENOMHOG000230093.
KOK01940.
OMANDQFRFE.
ProtClustDBPRK13820.

Enzyme and pathway databases

BioCycMSTA339860:GJEZ-1460-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]
PANTHERPTHR11587. PTHR11587. 1 hit.
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_METST
AccessionPrimary (citable) accession number: Q2NEC4
Entry history
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: February 7, 2006
Last modified: May 1, 2013
This is version 50 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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