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Protein

Argininosuccinate synthase

Gene

argG

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

ATP + L-citrulline + L-aspartate = AMP + diphosphate + N(omega)-(L-arginino)succinate.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei43 – 431ATP; via amide nitrogen and carbonyl oxygen1 Publication
Binding sitei99 – 991Citrulline2 Publications
Binding sitei129 – 1291ATP; via amide nitrogen1 Publication
Binding sitei131 – 1311Aspartate1 Publication
Binding sitei131 – 1311ATP1 Publication
Binding sitei135 – 1351Aspartate1 Publication
Binding sitei135 – 1351Citrulline2 Publications
Binding sitei136 – 1361Aspartate1 Publication
Binding sitei136 – 1361ATP1 Publication
Binding sitei139 – 1391Citrulline2 Publications
Binding sitei192 – 1921Citrulline2 Publications
Binding sitei194 – 1941ATP1 Publication
Binding sitei201 – 2011Citrulline2 Publications
Binding sitei203 – 2031Citrulline2 Publications
Binding sitei280 – 2801Citrulline2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi17 – 259ATP1 Publication

GO - Molecular functioni

  1. argininosuccinate synthase activity Source: GO_Central
  2. ATP binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. arginine biosynthetic process Source: GO_Central
  2. argininosuccinate metabolic process Source: GO_Central
  3. urea cycle Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Amino-acid biosynthesis, Arginine biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:ARGSUCCINSYN-MONOMER.
ECOL316407:JW3140-MONOMER.
UniPathwayiUPA00068; UER00113.

Names & Taxonomyi

Protein namesi
Recommended name:
Argininosuccinate synthase (EC:6.3.4.5)
Alternative name(s):
Citrulline--aspartate ligase
Gene namesi
Name:argG
Ordered Locus Names:b3172, JW3140
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10068. argG.

Subcellular locationi

Cytoplasm Curated

GO - Cellular componenti

  1. cytoplasm Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 447446Argininosuccinate synthasePRO_0000148695Add
BLAST

Proteomic databases

PaxDbiP0A6E4.
PRIDEiP0A6E4.

2D gel databases

SWISS-2DPAGEP0A6E4.

Expressioni

Gene expression databases

GenevestigatoriP0A6E4.

Interactioni

Subunit structurei

Homotetramer.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
dacBP242282EBI-1120296,EBI-1131834

Protein-protein interaction databases

DIPiDIP-35842N.
IntActiP0A6E4. 13 interactions.
STRINGi511145.b3172.

Structurei

Secondary structure

1
447
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 74Combined sources
Beta strandi12 – 176Combined sources
Helixi22 – 3312Combined sources
Beta strandi37 – 448Combined sources
Helixi55 – 639Combined sources
Beta strandi66 – 727Combined sources
Helixi74 – 8714Combined sources
Helixi102 – 12019Combined sources
Beta strandi125 – 1273Combined sources
Helixi136 – 14712Combined sources
Beta strandi152 – 1543Combined sources
Helixi156 – 1583Combined sources
Helixi160 – 1656Combined sources
Beta strandi166 – 1683Combined sources
Helixi169 – 17810Combined sources
Beta strandi190 – 1967Combined sources
Beta strandi199 – 2046Combined sources
Helixi205 – 2084Combined sources
Helixi214 – 2163Combined sources
Beta strandi220 – 2223Combined sources
Beta strandi235 – 2428Combined sources
Beta strandi245 – 2495Combined sources
Helixi257 – 26913Combined sources
Turni270 – 2745Combined sources
Beta strandi276 – 2816Combined sources
Beta strandi287 – 2937Combined sources
Helixi295 – 31117Combined sources
Helixi314 – 33219Combined sources
Helixi339 – 35113Combined sources
Helixi353 – 3553Combined sources
Beta strandi358 – 3647Combined sources
Beta strandi370 – 3767Combined sources
Turni384 – 3863Combined sources
Helixi398 – 4069Combined sources
Helixi409 – 42416Combined sources
Beta strandi427 – 4293Combined sources
Beta strandi433 – 4364Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1K92X-ray1.60A2-447[»]
1K97X-ray2.00A2-447[»]
1KP2X-ray2.00A2-447[»]
1KP3X-ray2.00A2-447[»]
ProteinModelPortaliP0A6E4.
SMRiP0A6E4. Positions 2-445.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A6E4.

Family & Domainsi

Domaini

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.

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0137.
HOGENOMiHOG000230094.
InParanoidiP0A6E4.
KOiK01940.
OMAiMRNLDIA.
OrthoDBiEOG6K9QCV.
PhylomeDBiP0A6E4.

Family and domain databases

Gene3Di1.10.287.400. 1 hit.
3.40.50.620. 1 hit.
3.90.1260.10. 1 hit.
HAMAPiMF_00581. Arg_succ_synth_type2.
InterProiIPR023437. 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]
PfamiPF00764. Arginosuc_synth. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00032. argG. 1 hit.
PROSITEiPS00564. ARGININOSUCCIN_SYN_1. 1 hit.
PS00565. ARGININOSUCCIN_SYN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0A6E4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTILKHLPV GQRIGIAFSG GLDTSAALLW MRQKGAVPYA YTANLGQPDE
60 70 80 90 100
EDYDAIPRRA MEYGAENARL IDCRKQLVAE GIAAIQCGAF HNTTGGLTYF
110 120 130 140 150
NTTPLGRAVT GTMLVAAMKE DGVNIWGDGS TYKGNDIERF YRYGLLTNAE
160 170 180 190 200
LQIYKPWLDT DFIDELGGRH EMSEFMIACG FDYKMSVEKA YSTDSNMLGA
210 220 230 240 250
THEAKDLEYL NSSVKIVNPI MGVKFWDESV KIPAEEVTVR FEQGHPVALN
260 270 280 290 300
GKTFSDDVEM MLEANRIGGR HGLGMSDQIE NRIIEAKSRG IYEAPGMALL
310 320 330 340 350
HIAYERLLTG IHNEDTIEQY HAHGRQLGRL LYQGRWFDSQ ALMLRDSLQR
360 370 380 390 400
WVASQITGEV TLELRRGNDY SILNTVSENL TYKPERLTME KGDSVFSPDD
410 420 430 440
RIGQLTMRNL DITDTREKLF GYAKTGLLSS SAASGVPQVE NLENKGQ
Length:447
Mass (Da):49,898
Last modified:January 23, 2007 - v2
Checksum:iD5E7E51BD06E1813
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti220 – 2201I → N in AAA23482 (PubMed:2123815).Curated
Sequence conflicti328 – 3281G → D in AAA23482 (PubMed:2123815).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M35236 Genomic DNA. Translation: AAA23482.1.
U18997 Genomic DNA. Translation: AAA57974.1.
U00096 Genomic DNA. Translation: AAC76205.1.
AP009048 Genomic DNA. Translation: BAE77217.1.
PIRiG65107. AJECRS.
RefSeqiNP_417640.1. NC_000913.3.
YP_491358.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC76205; AAC76205; b3172.
BAE77217; BAE77217; BAE77217.
GeneIDi12934127.
947590.
KEGGiecj:Y75_p3093.
eco:b3172.
PATRICi32121762. VBIEscCol129921_3266.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M35236 Genomic DNA. Translation: AAA23482.1.
U18997 Genomic DNA. Translation: AAA57974.1.
U00096 Genomic DNA. Translation: AAC76205.1.
AP009048 Genomic DNA. Translation: BAE77217.1.
PIRiG65107. AJECRS.
RefSeqiNP_417640.1. NC_000913.3.
YP_491358.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1K92X-ray1.60A2-447[»]
1K97X-ray2.00A2-447[»]
1KP2X-ray2.00A2-447[»]
1KP3X-ray2.00A2-447[»]
ProteinModelPortaliP0A6E4.
SMRiP0A6E4. Positions 2-445.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-35842N.
IntActiP0A6E4. 13 interactions.
STRINGi511145.b3172.

Chemistry

DrugBankiDB00536. Guanidine.

2D gel databases

SWISS-2DPAGEP0A6E4.

Proteomic databases

PaxDbiP0A6E4.
PRIDEiP0A6E4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76205; AAC76205; b3172.
BAE77217; BAE77217; BAE77217.
GeneIDi12934127.
947590.
KEGGiecj:Y75_p3093.
eco:b3172.
PATRICi32121762. VBIEscCol129921_3266.

Organism-specific databases

EchoBASEiEB0066.
EcoGeneiEG10068. argG.

Phylogenomic databases

eggNOGiCOG0137.
HOGENOMiHOG000230094.
InParanoidiP0A6E4.
KOiK01940.
OMAiMRNLDIA.
OrthoDBiEOG6K9QCV.
PhylomeDBiP0A6E4.

Enzyme and pathway databases

UniPathwayiUPA00068; UER00113.
BioCyciEcoCyc:ARGSUCCINSYN-MONOMER.
ECOL316407:JW3140-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0A6E4.
PROiP0A6E4.

Gene expression databases

GenevestigatoriP0A6E4.

Family and domain databases

Gene3Di1.10.287.400. 1 hit.
3.40.50.620. 1 hit.
3.90.1260.10. 1 hit.
HAMAPiMF_00581. Arg_succ_synth_type2.
InterProiIPR023437. 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]
PfamiPF00764. Arginosuc_synth. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00032. argG. 1 hit.
PROSITEiPS00564. ARGININOSUCCIN_SYN_1. 1 hit.
PS00565. ARGININOSUCCIN_SYN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiASSY_ECOLI
AccessioniPrimary (citable) accession number: P0A6E4
Secondary accession number(s): P22767, Q2M939
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: January 23, 2007
Last modified: February 4, 2015
This is version 97 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.