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Q1R6G5 (ASSY_ECOUT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 50. 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:UTI89_C3604
OrganismEscherichia coli (strain UTI89 / UPEC) [Complete proteome] [HAMAP]
Taxonomic identifier364106 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length447 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_00581

Pathway

Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 2/3. HAMAP-Rule MF_00581

Subunit structure

Homotetramer By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the argininosuccinate synthase family. Type 2 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 – 447447Argininosuccinate synthase HAMAP-Rule MF_00581
PRO_1000025423

Regions

Nucleotide binding17 – 259ATP By similarity

Sites

Binding site431ATP 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
Q1R6G5 [UniParc].

Last modified May 16, 2006. Version 1.
Checksum: D5E655AAD0DFB8A3

FASTA44749,910
        10         20         30         40         50         60 
MTTILKHLPV GQRIGIAFSG GLDTSAALLW MRQKGAVPYA YTANLGQPDE EDYDAIPRRA 

        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 THEAKDLEYL NSSVKIVNPI MGVKFWDESV KIPAEEVTVR 

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

       310        320        330        340        350        360 
HIAYERLLTG IHNEDTIEQY HAHGRQLGRL LYQGRWFDSQ ALMLRDSLQR WVASQITGEV 

       370        380        390        400        410        420 
TLELRRGNDY SILNTVSENL TYKPERLTME KGDSVFSPDD RIGQLTMRNL DITDTREKLF 

       430        440 
GYAKTGLLSS SATSGVPQVE NLENKGQ

« Hide

References

[1]"Identification of genes subject to positive selection in uropathogenic strains of Escherichia coli: a comparative genomics approach."
Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A., Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., Fulton R.S., Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., Hultgren S.J., Gordon J.I.
Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: UTI89 / UPEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000243 Genomic DNA. Translation: ABE09049.1.
RefSeqYP_542580.1. NC_007946.1.

3D structure databases

ProteinModelPortalQ1R6G5.
SMRQ1R6G5. Positions 2-445.
ModBaseSearch...

Protein-protein interaction databases

STRING364106.UTI89_C3604.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABE09049; ABE09049; UTI89_C3604.
GeneID3994751.
KEGGeci:UTI89_C3604.
PATRIC18456700. VBIEscCol42261_3565.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0137.
HOGENOMHOG000230094.
KOK01940.
OMAGGRKEMS.
ProtClustDBPRK05370.

Enzyme and pathway databases

BioCycECOL364106:GHPQ-3623-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]
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_ECOUT
AccessionPrimary (citable) accession number: Q1R6G5
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: May 16, 2006
Last modified: May 1, 2013
This is version 50 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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