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B1W3B3 (ASSY_STRGG) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 39. 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:SGR_5966
OrganismStreptomyces griseus subsp. griseus (strain JCM 4626 / NBRC 13350) [Complete proteome] [HAMAP]
Taxonomic identifier455632 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Streptomycineae › Streptomycetaceae › Streptomyces ›

Protein attributes

Sequence length397 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: 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 – 397397Argininosuccinate synthase HAMAP-Rule MF_00005
PRO_1000089054

Regions

Nucleotide binding8 – 169ATP By similarity

Sites

Binding site871Citrulline By similarity
Binding site1171ATP; via amide nitrogen By similarity
Binding site1191Aspartate By similarity
Binding site1231Aspartate By similarity
Binding site1231Citrulline By similarity
Binding site1241Aspartate By similarity
Binding site1271Citrulline By similarity
Binding site1751Citrulline By similarity
Binding site2591Citrulline By similarity
Binding site2711Citrulline By similarity

Sequences

Sequence LengthMass (Da)Tools
B1W3B3 [UniParc].

Last modified May 20, 2008. Version 1.
Checksum: C92947FFD4FC9965

FASTA39743,321
        10         20         30         40         50         60 
MTERVVLAYS GGLDTSVAIG WIAEETGAEV IAVAVDVGQG GEDLDVIRKR ALACGAVEAE 

        70         80         90        100        110        120 
VADARDEFAE EYCLPAIKAN ALYMDRYPLV SALSRPTIVK HLVAAARKHG AGTVAHGCTG 

       130        140        150        160        170        180 
KGNDQVRFEA GISALGPDLK CIAPVRDYAM TRDRAIAFCE EKNLPIATTR KSPYSIDQNV 

       190        200        210        220        230        240 
FGRAVETGFL EDIWNAPIED IYEYTADPAV PREADEVVIS FKEGVPVAVD GRPVTVLQAI 

       250        260        270        280        290        300 
QQLNERAGAQ GVGRIDMVED RLVGIKSREV YEAPGAIALI TAHQELENVT VERELARYKR 

       310        320        330        340        350        360 
QVEQRWGEMV YDGLWFSPLK RALDGFINEA NQHVTGDIRM TLHAGRAVVT GRKSEESLYD 

       370        380        390 
FNLATYDSGD TFDQSKAQGF IEIFGLSAKI AARRDLA

« Hide

References

[1]"Genome sequence of the streptomycin-producing microorganism Streptomyces griseus IFO 13350."
Ohnishi Y., Ishikawa J., Hara H., Suzuki H., Ikenoya M., Ikeda H., Yamashita A., Hattori M., Horinouchi S.
J. Bacteriol. 190:4050-4060(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JCM 4626 / NBRC 13350.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AP009493 Genomic DNA. Translation: BAG22795.1.
RefSeqYP_001827478.1. NC_010572.1.

3D structure databases

ProteinModelPortalB1W3B3.
ModBaseSearch...

Protein-protein interaction databases

STRING455632.SGR_5966.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAG22795; BAG22795; SGR_5966.
GeneID6209495.
KEGGsgr:SGR_5966.
PATRIC23758757. VBIStrGri32265_6117.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0137.
HOGENOMHOG000230093.
KOK01940.
OMANDQFRFE.
ProtClustDBPRK00509.

Enzyme and pathway databases

BioCycSGRI455632:GD3A-6042-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_STRGG
AccessionPrimary (citable) accession number: B1W3B3
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: May 20, 2008
Last modified: May 29, 2013
This is version 39 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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