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Q5LXZ8 (ASSY_STRT1) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 59. 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:str1813
OrganismStreptococcus thermophilus (strain CNRZ 1066) [Complete proteome] [HAMAP]
Taxonomic identifier299768 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Lactobacillales › Streptococcaceae › Streptococcus ›

Protein attributes

Sequence length399 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.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the argininosuccinate synthase family. Type 1 subfamily.

Sequence caution

The sequence AAV63329.1 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
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 – 399399Argininosuccinate synthase HAMAP-Rule MF_00005
PRO_0000148649

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
Q5LXZ8 [UniParc].

Last modified March 15, 2005. Version 2.
Checksum: D62EF4242B086416

FASTA39944,055
        10         20         30         40         50         60 
MSKEKVILAY SGGLDTSVAI TWLKKDYDVI AVCMDVGEGK DLEFIHDKAL TVGAVESYVL 

        70         80         90        100        110        120 
DVKDEFAEDY VLPALQAHAY YEQKYPLVSA LSRPIIAKKL VEIAHKTGAT TIAHGCTGKG 

       130        140        150        160        170        180 
NDQVRFEVAI AALDPSLKVV APVREWKWSR EEEIEYAKAN GVPVPADLDN PYSVDQNLWG 

       190        200        210        220        230        240 
RANECGVLEN PWNQAPEEAF GITNSPESAP DEAEYVDVTF KEGKPVALNG KEMKLADLIQ 

       250        260        270        280        290        300 
EMNVIAGKHG VGRIDHVENR LVGIKSREIY ECPGAIALLT AHKEIEDLTL VREVSHFKPI 

       310        320        330        340        350        360 
LENELSNLIY NALWFSPATE AIIAYIKETQ KVVNGIAKVK LYKGHAQVVA RQSANSLYDE 

       370        380        390 
NLATYTSADS FDQDAAIGFI KLWGLPTQVN SQVNHPFDK

« Hide

References

[1]"Complete sequence and comparative genome analysis of the dairy bacterium Streptococcus thermophilus."
Bolotin A., Quinquis B., Renault P., Sorokin A., Ehrlich S.D., Kulakauskas S., Lapidus A., Goltsman E., Mazur M., Pusch G.D., Fonstein M., Overbeek R., Kyprides N., Purnelle B., Prozzi D., Ngui K., Masuy D., Hancy F. expand/collapse author list , Burteau S., Boutry M., Delcour J., Goffeau A., Hols P.
Nat. Biotechnol. 22:1554-1558(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CNRZ 1066.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000024 Genomic DNA. Translation: AAV63329.1. Different initiation.
RefSeqYP_142144.2. NC_006449.1.

3D structure databases

ProteinModelPortalQ5LXZ8.
ModBaseSearch...

Protein-protein interaction databases

STRING299768.str1813.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAV63329; AAV63329; str1813.
GeneID3167039.
KEGGstc:str1813.
PATRIC19796705. VBIStrThe135799_1796.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0137.
HOGENOMHOG000230093.
KOK01940.
ProtClustDBPRK00509.

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]
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_STRT1
AccessionPrimary (citable) accession number: Q5LXZ8
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: March 15, 2005
Last modified: May 1, 2013
This is version 59 of the entry and version 2 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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