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P0A6E4 (ASSY_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·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:b3172, JW3140
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length447 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

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.

Subcellular location

Cytoplasm Probable HAMAP-Rule MF_00581.

Domain

The monomer is composed of two major structural domains: a nucleotide-binding domain and a catalytic/multimerization domain. Binding of ATP results in a large rigid body conformational change of the nucleotide binding domain. HAMAP-Rule MF_00581

Sequence similarities

Belongs to the argininosuccinate synthase family. Type 2 subfamily.

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

dacBP242282EBI-1120296,EBI-1131834

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1 Ref.4
Chain2 – 447446Argininosuccinate synthase HAMAP-Rule MF_00581
PRO_0000148695

Regions

Nucleotide binding17 – 259ATP HAMAP-Rule MF_00581

Sites

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

Experimental info

Sequence conflict2201I → N in AAA23482. Ref.1
Sequence conflict3281G → D in AAA23482. Ref.1

Secondary structure

....................................................................... 447
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A6E4 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: D5E7E51BD06E1813

FASTA44749,898
        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 MLEANRIGGR 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 SAASGVPQVE NLENKGQ 

« Hide

References

« Hide 'large scale' references
[1]"Sequences of the genes encoding argininosuccinate synthetase in Escherichia coli and Saccharomyces cerevisiae: comparison with methanogenic archaebacteria and mammals."
van Vliet F., Crabeel M., Boyen A., Tricot C., Stalon V., Falmagne P., Nakamura Y., Baumberg S., Glansdorff N.
Gene 95:99-104(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-11.
Strain: K12.
[2]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[3]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
Link A.J., Robison K., Church G.M.
Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-13.
Strain: K12 / EMG2.
[5]"Expression, purification, crystallization and preliminary X-ray analysis of Escherichia coli argininosuccinate synthetase."
Lemke C., Yeung M., Howell P.L.
Acta Crystallogr. D 55:2028-2030(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION, CRYSTALLIZATION.
[6]"The 1.6 A crystal structure of E. coli argininosuccinate synthetase suggests a conformational change during catalysis."
Lemke C.T., Howell P.L.
Structure 9:1153-1164(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) UNCOMPLEXED AND IN COMPLEX WITH ASPARTATE AND CITRULLINE.
[7]"Substrate induced conformational changes in argininosuccinate synthetase."
Lemke C.T., Howell P.L.
J. Biol. Chem. 277:13074-13081(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH ATP AND CITRULLINE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M35236 Genomic DNA. Translation: AAA23482.1.
U18997 Genomic DNA. Translation: AAA57974.1.
U00096 Genomic DNA. Translation: AAC76205.1.
AP009048 Genomic DNA. Translation: BAE77217.1.
PIRAJECRS. G65107.
RefSeqNP_417640.1. NC_000913.3.
YP_491358.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1K92X-ray1.60A2-447[»]
1K97X-ray2.00A2-447[»]
1KP2X-ray2.00A2-447[»]
1KP3X-ray2.00A2-447[»]
ProteinModelPortalP0A6E4.
SMRP0A6E4. Positions 2-445.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-35842N.
IntActP0A6E4. 13 interactions.
STRING511145.b3172.

Chemistry

DrugBankDB00536. Guanidine.

2D gel databases

SWISS-2DPAGEP0A6E4.

Proteomic databases

PaxDbP0A6E4.
PRIDEP0A6E4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC76205; AAC76205; b3172.
BAE77217; BAE77217; BAE77217.
GeneID12934127.
947590.
KEGGecj:Y75_p3093.
eco:b3172.
PATRIC32121762. VBIEscCol129921_3266.

Organism-specific databases

EchoBASEEB0066.
EcoGeneEG10068. argG.

Phylogenomic databases

eggNOGCOG0137.
HOGENOMHOG000230094.
KOK01940.
OMARQEMSEF.
OrthoDBEOG6K9QCV.
PhylomeDBP0A6E4.

Enzyme and pathway databases

BioCycEcoCyc:ARGSUCCINSYN-MONOMER.
ECOL316407:JW3140-MONOMER.
UniPathwayUPA00068; UER00113.

Gene expression databases

GenevestigatorP0A6E4.

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...

Other

EvolutionaryTraceP0A6E4.
PROP0A6E4.

Entry information

Entry nameASSY_ECOLI
AccessionPrimary (citable) accession number: P0A6E4
Secondary accession number(s): P22767, Q2M939
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: January 23, 2007
Last modified: June 11, 2014
This is version 92 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene