SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P0A6E4

- ASSY_ECOLI

UniProt

P0A6E4 - ASSY_ECOLI

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Argininosuccinate synthase
Gene
argG, b3172, JW3140
Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Pathwayi

Sites

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

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi17 – 259ATPUniRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-HAMAP
  2. argininosuccinate synthase activity Source: UniProtKB-HAMAP
  3. protein binding Source: IntAct

GO - Biological processi

  1. arginine biosynthetic process Source: UniProtKB-HAMAP
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 Inferred UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
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 synthaseUniRule annotation
PRO_0000148695Add
BLAST

Proteomic databases

PaxDbiP0A6E4.
PRIDEiP0A6E4.

2D gel databases

SWISS-2DPAGEP0A6E4.

Expressioni

Gene expression databases

GenevestigatoriP0A6E4.

Interactioni

Subunit structurei

Homotetramer.

Binary interactionsi

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

Protein-protein interaction databases

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

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

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.UniRule annotation

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0137.
HOGENOMiHOG000230094.
KOiK01940.
OMAiRQEMSEF.
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

MTTILKHLPV GQRIGIAFSG GLDTSAALLW MRQKGAVPYA YTANLGQPDE    50
EDYDAIPRRA MEYGAENARL IDCRKQLVAE GIAAIQCGAF HNTTGGLTYF 100
NTTPLGRAVT GTMLVAAMKE DGVNIWGDGS TYKGNDIERF YRYGLLTNAE 150
LQIYKPWLDT DFIDELGGRH EMSEFMIACG FDYKMSVEKA YSTDSNMLGA 200
THEAKDLEYL NSSVKIVNPI MGVKFWDESV KIPAEEVTVR FEQGHPVALN 250
GKTFSDDVEM MLEANRIGGR HGLGMSDQIE NRIIEAKSRG IYEAPGMALL 300
HIAYERLLTG IHNEDTIEQY HAHGRQLGRL LYQGRWFDSQ ALMLRDSLQR 350
WVASQITGEV TLELRRGNDY SILNTVSENL TYKPERLTME KGDSVFSPDD 400
RIGQLTMRNL DITDTREKLF GYAKTGLLSS SAASGVPQVE NLENKGQ 447
Length:447
Mass (Da):49,898
Last modified:January 23, 2007 - v2
Checksum:iD5E7E51BD06E1813
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti220 – 2201I → N in AAA23482. 1 Publication
Sequence conflicti328 – 3281G → D in AAA23482. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
PIRi G65107. AJECRS.
RefSeqi NP_417640.1. NC_000913.3.
YP_491358.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1K92 X-ray 1.60 A 2-447 [» ]
1K97 X-ray 2.00 A 2-447 [» ]
1KP2 X-ray 2.00 A 2-447 [» ]
1KP3 X-ray 2.00 A 2-447 [» ]
ProteinModelPortali P0A6E4.
SMRi P0A6E4. Positions 2-445.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-35842N.
IntActi P0A6E4. 13 interactions.
STRINGi 511145.b3172.

Chemistry

DrugBanki DB00536. Guanidine.

2D gel databases

SWISS-2DPAGE P0A6E4.

Proteomic databases

PaxDbi P0A6E4.
PRIDEi P0A6E4.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC76205 ; AAC76205 ; b3172 .
BAE77217 ; BAE77217 ; BAE77217 .
GeneIDi 12934127.
947590.
KEGGi ecj:Y75_p3093.
eco:b3172.
PATRICi 32121762. VBIEscCol129921_3266.

Organism-specific databases

EchoBASEi EB0066.
EcoGenei EG10068. argG.

Phylogenomic databases

eggNOGi COG0137.
HOGENOMi HOG000230094.
KOi K01940.
OMAi RQEMSEF.
OrthoDBi EOG6K9QCV.
PhylomeDBi P0A6E4.

Enzyme and pathway databases

UniPathwayi UPA00068 ; UER00113 .
BioCyci EcoCyc:ARGSUCCINSYN-MONOMER.
ECOL316407:JW3140-MONOMER.

Miscellaneous databases

EvolutionaryTracei P0A6E4.
PROi P0A6E4.

Gene expression databases

Genevestigatori P0A6E4.

Family and domain databases

Gene3Di 1.10.287.400. 1 hit.
3.40.50.620. 1 hit.
3.90.1260.10. 1 hit.
HAMAPi MF_00581. Arg_succ_synth_type2.
InterProi IPR023437. 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 ]
Pfami PF00764. Arginosuc_synth. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR00032. argG. 1 hit.
PROSITEi PS00564. ARGININOSUCCIN_SYN_1. 1 hit.
PS00565. ARGININOSUCCIN_SYN_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: June 11, 2014
This is version 92 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