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Q4J8F1 (ASSY_SULAC) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 55. 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:Saci_1617
OrganismSulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770) [Complete proteome] [HAMAP]
Taxonomic identifier330779 [NCBI]
Taxonomic lineageArchaea › Crenarchaeota › Thermoprotei › Sulfolobales › Sulfolobaceae › Sulfolobus ›

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: 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 – 391391Argininosuccinate synthase HAMAP-Rule MF_00005
PRO_0000148685

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
Q4J8F1 [UniParc].

Last modified August 2, 2005. Version 1.
Checksum: C3862A7EEFA65843

FASTA39144,342
        10         20         30         40         50         60 
MKIVLAYSGG LDTTVAIRWL RETFNADVTT VTVDVGQKDD FYQIEKRAYI AGAIKHYTID 

        70         80         90        100        110        120 
AKKDFAERYI SYAIKMNGLY EDIYPLSTAL ARPLIVEKVV EIAKKIGAEA IAHGSTSKGN 

       130        140        150        160        170        180 
DQVRFDLAVK ALYPEAKIIA PARIWNMTRD KEIEYAKSKG IPIKTESSKY SIDENLWGRS 

       190        200        210        220        230        240 
IEGDIISDPS KEVPEDAFEW TKKTKDDKLK ISLTFDKGLP VEVNGEKMDL LKVIQVLNEL 

       250        260        270        280        290        300 
VGSRGFGRVE HLENRVVGFK SREVYEVPAA LVLINSHKDL EKSTYTPLEF RFKRSLDGQW 

       310        320        330        340        350        360 
SDLVYQGLWF EPLRETIQIA GDNLNKWISG EVFIEVENGN MKILGRKGKF SPFSEEIASY 

       370        380        390 
NKGWYPSDEM ARGFIEIFGM HSLVARKSRG I

« Hide

References

[1]"The genome of Sulfolobus acidocaldarius, a model organism of the Crenarchaeota."
Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E., Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.
J. Bacteriol. 187:4992-4999(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000077 Genomic DNA. Translation: AAY80929.1.
RefSeqYP_256222.1. NC_007181.1.

3D structure databases

ProteinModelPortalQ4J8F1.
ModBaseSearch...

Protein-protein interaction databases

STRING330779.Saci_1617.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAY80929; AAY80929; Saci_1617.
GeneID3474173.
KEGGsai:Saci_1617.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0137.
HOGENOMHOG000230093.
KOK01940.
OMANDQFRFE.
ProtClustDBPRK00509.

Enzyme and pathway databases

BioCycSACI330779:GH9J-1588-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_SULAC
AccessionPrimary (citable) accession number: Q4J8F1
Entry history
Integrated into UniProtKB/Swiss-Prot: September 27, 2005
Last sequence update: August 2, 2005
Last modified: May 29, 2013
This is version 55 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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