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A4YI75 (ASSY_METS5) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 46. 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:Msed_1987
OrganismMetallosphaera sedula (strain ATCC 51363 / DSM 5348) [Complete proteome] [HAMAP]
Taxonomic identifier399549 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeMetallosphaera

Protein attributes

Sequence length391 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
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 – 391391Argininosuccinate synthase HAMAP-Rule MF_00005
PRO_1000070914

Regions

Nucleotide binding6 – 149ATP By similarity

Sites

Binding site841Citrulline By similarity
Binding site1141ATP; via amide nitrogen By similarity
Binding site1161Aspartate By similarity
Binding site1201Aspartate By similarity
Binding site1201Citrulline By similarity
Binding site1211Aspartate By similarity
Binding site1241Citrulline By similarity
Binding site1711Citrulline By similarity
Binding site1801Citrulline By similarity
Binding site2531Citrulline By similarity
Binding site2651Citrulline By similarity

Sequences

Sequence LengthMass (Da)Tools
A4YI75 [UniParc].

Last modified May 29, 2007. Version 1.
Checksum: CB7585851315C5FF

FASTA39144,199
        10         20         30         40         50         60 
MKIVLAYSGG LDTTVAIKWL SETFHAEVIS VSVDVGQKDD FKKIEERAYK AGSAKHYLVD 

        70         80         90        100        110        120 
AKREFAENFA LKDIKMNGLY EEVYPLATAL ARPLIAEKVA EVAKKEGTEY VAHGSTSKGN 

       130        140        150        160        170        180 
DQVRFDLALK TALDNVKIIA PARIWKMTRE DEIAYARERG IPIKTESSKY SIDENLWGRS 

       190        200        210        220        230        240 
IEGDIISDPA SEVPEDAFEW TAVRKQDKLK LSVEFEKGVP VRVNGEKLDP VKLISLLNEE 

       250        260        270        280        290        300 
VGSRGFGRVE HLENRVVGFK SREVYEAPAA LALIAAHKDL EKTVLTPLEL RFKRHLDSLW 

       310        320        330        340        350        360 
SDLVYQGLWY EPLRNTLELA GDEINKWVSG EVKLEVDLKS LRVVGRTSPY SPYSEKISSY 

       370        380        390 
NKGWYPSDEE ARGFIEIWGM HSLLTRKARY G 

« Hide

References

[1]"The genome sequence of the metal-mobilizing, extremely thermoacidophilic archaeon Metallosphaera sedula provides insights into bioleaching-associated metabolism."
Auernik K.S., Maezato Y., Blum P.H., Kelly R.M.
Appl. Environ. Microbiol. 74:682-692(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 51363 / DSM 5348.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000682 Genomic DNA. Translation: ABP96127.1.
RefSeqYP_001192051.1. NC_009440.1.

3D structure databases

ProteinModelPortalA4YI75.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING399549.Msed_1987.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABP96127; ABP96127; Msed_1987.
GeneID5103374.
KEGGmse:Msed_1987.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0137.
HOGENOMHOG000230093.
KOK01940.
OMAIYNGYWW.
ProtClustDBPRK00509.

Enzyme and pathway databases

BioCycMSED399549:GH1O-2018-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_METS5
AccessionPrimary (citable) accession number: A4YI75
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: May 29, 2007
Last modified: February 19, 2014
This is version 46 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