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P13257 (ASSY_METBA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 83. 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
OrganismMethanosarcina barkeri
Taxonomic identifier2208 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanomicrobiaMethanosarcinalesMethanosarcinaceaeMethanosarcina

Protein attributes

Sequence length396 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.

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
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 – 396396Argininosuccinate synthase HAMAP-Rule MF_00005
PRO_0000148675

Regions

Nucleotide binding8 – 169ATP By similarity

Sites

Binding site861Citrulline By similarity
Binding site911Citrulline By similarity
Binding site1161ATP; via amide nitrogen By similarity
Binding site1181Aspartate By similarity
Binding site1221Aspartate By similarity
Binding site1221Citrulline By similarity
Binding site1231Aspartate By similarity
Binding site1261Citrulline By similarity
Binding site1721Citrulline By similarity
Binding site1811Citrulline By similarity
Binding site2571Citrulline By similarity
Binding site2691Citrulline By similarity

Sequences

Sequence LengthMass (Da)Tools
P13257 [UniParc].

Last modified January 1, 1990. Version 1.
Checksum: BF9DA4207D1ACC6B

FASTA39644,441
        10         20         30         40         50         60 
MAKKVALAYS GGLDTSVCIP ILKEKYGYDE VVTISVDVGQ PEEEIKRADA KAEKISNKHY 

        70         80         90        100        110        120 
TIDAKEEFVK DYVFPLIKAN GSYEGYVMGT SIARPLIAKK VVEAARKEGA VALAHGCTGK 

       130        140        150        160        170        180 
GNDQLRFEAV FRQTDMDVIA PMREMNLTRE WEIDYAKEHG IPVEVTKSKP WSVDENIWSR 

       190        200        210        220        230        240 
SIEGGRLEDP SFVPPEEIFE WTTSPEKAPE QPRVVDIGFE AGVPVSLDGE KMSGYAFVKK 

       250        260        270        280        290        300 
MNEIAGENGV GRTDMIEDRV LGLKARENYE HPAATVLRQP NSRPLRNSSL TRSELKFKKI 

       310        320        330        340        350        360 
VDDQWSELAY YGLVDEPLYA DLNAFIDKSQ ERVTGIVKVR LYKGALTILA RSSPNALYSE 

       370        380        390 
DLVSFDSQTI DQKGSEGFAK YHGFQARMYR KVMDKQ 

« Hide

References

[1]"Conservation of structure in the human gene encoding argininosuccinate synthetase and the argG genes of the archaebacteria Methanosarcina barkeri MS and Methanococcus vannielii."
Morris C.J., Reeve J.N.
J. Bacteriol. 170:3125-3130(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 43569 / MS / DSM 800 / JCM 10043 / NBRC 100474.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M21314 Genomic DNA. Translation: AAA72677.1.
PIRAJMZRB. B28180.

3D structure databases

ProteinModelPortalP13257.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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...

Entry information

Entry nameASSY_METBA
AccessionPrimary (citable) accession number: P13257
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
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

PATHWAY comments

Index of metabolic and biosynthesis pathways