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Q8ZLT0 (ASSY_SALTY) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 94. 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:STM3290
OrganismSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) [Reference proteome] [HAMAP]
Taxonomic identifier99287 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

Protein attributes

Sequence length447 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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 2 subfamily.

Sequence caution

The sequence AAL22161.1 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

Initiator methionine11Removed By similarity
Chain2 – 447446Argininosuccinate synthase HAMAP-Rule MF_00005
PRO_0000148706

Regions

Nucleotide binding17 – 259ATP By similarity

Sites

Binding site431ATP; via amide nitrogen and carbonyl oxygen By similarity
Binding site991Citrulline By similarity
Binding site1291ATP; via amide nitrogen By similarity
Binding site1311Aspartate By similarity
Binding site1311ATP By similarity
Binding site1351Aspartate By similarity
Binding site1351Citrulline By similarity
Binding site1361Aspartate By similarity
Binding site1361ATP By similarity
Binding site1391Citrulline By similarity
Binding site1921Citrulline By similarity
Binding site1941ATP By similarity
Binding site2011Citrulline By similarity
Binding site2031Citrulline By similarity
Binding site2801Citrulline By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8ZLT0 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 7E829BC54E5E9D71

FASTA44749,754
        10         20         30         40         50         60 
MTTILKHLPA GQRIGIAFSG GLDTSAALLW MRQKGAVPYA YTANLGQPDE DDYDAIPRRA 

        70         80         90        100        110        120 
MEYGAENARL IDCRKQLVAE GIAAIQCGAF HNTTGGLTYF NTTPLGRAVT GTMLVAAMKE 

       130        140        150        160        170        180 
DGVNIWGDGS TYKGNDIERF YRYGLLTNAE LQIYKPWLDT DFIDELGGRH EMSEFMIACG 

       190        200        210        220        230        240 
FDYKMSVEKA YSTDSNMLGA THEAKDLEFL NSSVKIVNPI MGVKFWDESV KIPAEVVTVR 

       250        260        270        280        290        300 
FEQGHPVALN GKTFSDDVEM MLEANRIGGR HGLGMSDQIE NRIIEAKSRG IYEAPGMALL 

       310        320        330        340        350        360 
HIAYERLLTG IHNEDTIEQY HSHGRQLGKL LYQGRWFDSQ ALMLRDGLQR WVASQITGEV 

       370        380        390        400        410        420 
TLELRRGNDY SILNTVSDNL TYKAERLTME KGESVFSPDD RIGQLTMRNL DITDTREKLF 

       430        440 
GYAKAGLLTA SSATGLPQVE NLENKGK 

« Hide

References

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE006468 Genomic DNA. Translation: AAL22161.1. Different initiation.
RefSeqNP_462202.2. NC_003197.1.

3D structure databases

ProteinModelPortalQ8ZLT0.
SMRQ8ZLT0. Positions 2-445.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PaxDbQ8ZLT0.
PRIDEQ8ZLT0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL22161; AAL22161; STM3290.
GeneID1254813.
KEGGstm:STM3290.S.
PATRIC32385367. VBISalEnt20916_3488.

Phylogenomic databases

eggNOGCOG0137.
KOK01940.
OMARQEMSEF.
OrthoDBEOG6K9QCV.
PhylomeDBQ8ZLT0.

Enzyme and pathway databases

BioCycSENT99287:GCTI-3311-MONOMER.
UniPathwayUPA00068; UER00113.

Family and domain databases

Gene3D1.10.287.400. 1 hit.
3.40.50.620. 1 hit.
3.90.1260.10. 1 hit.
HAMAPMF_00581. Arg_succ_synth_type2.
InterProIPR023437. Arg_succ_synth_type2_subfam.
IPR001518. Arginosuc_synth.
IPR018223. Arginosuc_synth_CS.
IPR024074. AS_cat/multimer_dom_body.
IPR024073. AS_multimer_C_tail.
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_SALTY
AccessionPrimary (citable) accession number: Q8ZLT0
Entry history
Integrated into UniProtKB/Swiss-Prot: October 19, 2002
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 94 of the entry and version 3 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