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Q8DRI5 (ASSY_STRR6) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 73. 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:spr0102
OrganismStreptococcus pneumoniae (strain ATCC BAA-255 / R6) [Reference proteome] [HAMAP]
Taxonomic identifier171101 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

Protein attributes

Sequence length398 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.

Sequence caution

The sequence AAK98906.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Arginine biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   Technical termComplete proteome
Reference 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 – 398398Argininosuccinate synthase HAMAP-Rule MF_00005
PRO_0000148648

Regions

Nucleotide binding9 – 179ATP 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 site1731Citrulline By similarity
Binding site2581Citrulline By similarity
Binding site2701Citrulline By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8DRI5 [UniParc].

Last modified September 19, 2003. Version 2.
Checksum: 09A7990DF0E5E776

FASTA39844,065
        10         20         30         40         50         60 
MSKEKVILAY SGGLDTSVAI TWLKKDYDVV AVCMDVGEGK DLDFIHDKAL KVGAVESYVI 

        70         80         90        100        110        120 
DVKDEFATDY VLVAHQSHAY YEQKYPLVSA LSRPLISKKL VEIAHQIGAT TIAHGCTGKG 

       130        140        150        160        170        180 
NDQVRFEVSI AALDLNLKVI APVREWKWSR EEEIYYAKEN GVPVPADLDN PYSVDQNLWG 

       190        200        210        220        230        240 
RANECGILEN PWNQAPEEAF GITTSPEQAP DMPEYIEIEF SEGVPVSLNG EVLKLADLIQ 

       250        260        270        280        290        300 
KLNEIAGKHG VGRIDHVENR LVGIKSREIY ECPGAVTLLT AHKEIEDLTL VREVAHFKPI 

       310        320        330        340        350        360 
IENELSNLIY NALWFSSATQ ALIAYIKETQ KVVNGTAKVK LYKGSAQVVA RKSPSSLYDE 

       370        380        390 
NLATYTSADT FDQDAAVGFI KLWGLPTKVH SEVQKSAK 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE007317 Genomic DNA. Translation: AAK98906.1. Different initiation.
PIRF97884.
RefSeqNP_357696.1. NC_003098.1.

3D structure databases

ProteinModelPortalQ8DRI5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING171101.spr0102.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAK98906; AAK98906; spr0102.
GeneID932865.
KEGGspr:spr0102.
PATRIC19700005. VBIStrPne107296_0121.

Phylogenomic databases

eggNOGCOG0137.
HOGENOMHOG000230093.
KOK01940.
OrthoDBEOG6K9QCV.
ProtClustDBPRK00509.

Enzyme and pathway databases

BioCycSPNE171101:GJC8-109-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_STRR6
AccessionPrimary (citable) accession number: Q8DRI5
Entry history
Integrated into UniProtKB/Swiss-Prot: April 23, 2003
Last sequence update: September 19, 2003
Last modified: February 19, 2014
This is version 73 of the entry and version 2 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