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B1I814 (ASSY_STRPI) 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:SPH_0215
OrganismStreptococcus pneumoniae (strain Hungary19A-6) [Complete proteome] [HAMAP]
Taxonomic identifier487214 [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.

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 – 398398Argininosuccinate synthase HAMAP-Rule MF_00005
PRO_1000089055

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
B1I814 [UniParc].

Last modified April 29, 2008. Version 1.
Checksum: BC55990A6F10788B

FASTA39844,081
        10         20         30         40         50         60 
MSKEKVILAY SGGLDTSVAI TWLKKDYDVV SVCMDVGEGK 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

References

[1]"Complete sequence of Streptococcus pneumoniae strain Hungary 19A-6."
Hotopp J.D., Censini S., Masignani V., Covacci A., Tettelin H.
Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Hungary19A-6.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000936 Genomic DNA. Translation: ACA36199.1.
RefSeqYP_001693635.1. NC_010380.1.

3D structure databases

ProteinModelPortalB1I814.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING487214.SPH_0215.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACA36199; ACA36199; SPH_0215.
GeneID6029570.
KEGGspv:SPH_0215.
PATRIC19690506. VBIStrPne34925_0206.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0137.
HOGENOMHOG000230093.
KOK01940.
OMAIYNGYWW.
OrthoDBEOG6K9QCV.
ProtClustDBPRK00509.

Enzyme and pathway databases

BioCycSPNE487214:GHY0-212-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_STRPI
AccessionPrimary (citable) accession number: B1I814
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: April 29, 2008
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