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Protein

Argininosuccinate synthase

Gene

argG

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

Functioni

Catalytic activityi

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

Pathwayi: L-arginine biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes L-arginine from L-ornithine and carbamoyl phosphate.
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. Ornithine carbamoyltransferase subunit I (argI), Ornithine carbamoyltransferase subunit F (argF)
  2. Argininosuccinate synthase (argG)
  3. Argininosuccinate lyase (argH)
This subpathway is part of the pathway L-arginine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-arginine from L-ornithine and carbamoyl phosphate, the pathway L-arginine biosynthesis and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei43ATP; via amide nitrogen and carbonyl oxygen1 Publication1
Binding sitei99Citrulline2 Publications1
Binding sitei129ATP; via amide nitrogen1 Publication1
Binding sitei131Aspartate1 Publication1
Binding sitei131ATP1 Publication1
Binding sitei135Aspartate1 Publication1
Binding sitei135Citrulline2 Publications1
Binding sitei136Aspartate1 Publication1
Binding sitei136ATP1 Publication1
Binding sitei139Citrulline2 Publications1
Binding sitei192Citrulline2 Publications1
Binding sitei194ATP1 Publication1
Binding sitei201Citrulline2 Publications1
Binding sitei203Citrulline2 Publications1
Binding sitei280Citrulline2 Publications1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi17 – 25ATP1 Publication9

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionLigase
Biological processAmino-acid biosynthesis, Arginine biosynthesis
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:ARGSUCCINSYN-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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10068 argG

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Chemistry databases

DrugBankiDB04077 Glycerol
DB00536 Guanidine

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved2 Publications
ChainiPRO_00001486952 – 447Argininosuccinate synthaseAdd BLAST446

Proteomic databases

EPDiP0A6E4
PaxDbiP0A6E4
PRIDEiP0A6E4

2D gel databases

SWISS-2DPAGEiP0A6E4

Interactioni

Subunit structurei

Homotetramer.2 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • protein homodimerization activity Source: InterPro

Protein-protein interaction databases

BioGridi4263121, 37 interactors
DIPiDIP-35842N
IntActiP0A6E4, 14 interactors
STRINGi316385.ECDH10B_3346

Structurei

Secondary structure

1447
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 7Combined sources4
Beta strandi12 – 17Combined sources6
Helixi22 – 33Combined sources12
Beta strandi37 – 44Combined sources8
Helixi55 – 63Combined sources9
Beta strandi66 – 72Combined sources7
Helixi74 – 87Combined sources14
Helixi102 – 120Combined sources19
Beta strandi125 – 127Combined sources3
Helixi136 – 147Combined sources12
Beta strandi152 – 154Combined sources3
Helixi156 – 158Combined sources3
Helixi160 – 165Combined sources6
Beta strandi166 – 168Combined sources3
Helixi169 – 178Combined sources10
Beta strandi190 – 196Combined sources7
Beta strandi199 – 204Combined sources6
Helixi205 – 208Combined sources4
Helixi214 – 216Combined sources3
Beta strandi220 – 222Combined sources3
Beta strandi235 – 242Combined sources8
Beta strandi245 – 249Combined sources5
Helixi257 – 269Combined sources13
Turni270 – 274Combined sources5
Beta strandi276 – 281Combined sources6
Beta strandi287 – 293Combined sources7
Helixi295 – 311Combined sources17
Helixi314 – 332Combined sources19
Helixi339 – 351Combined sources13
Helixi353 – 355Combined sources3
Beta strandi358 – 364Combined sources7
Beta strandi370 – 376Combined sources7
Turni384 – 386Combined sources3
Helixi398 – 406Combined sources9
Helixi409 – 424Combined sources16
Beta strandi427 – 429Combined sources3
Beta strandi433 – 436Combined sources4

3D structure databases

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

eggNOGiENOG4105CDH Bacteria
COG0137 LUCA
HOGENOMiHOG000230094
InParanoidiP0A6E4
KOiK01940
OMAiGVGRIDM
PhylomeDBiP0A6E4

Family and domain databases

CDDicd01999 Argininosuccinate_Synthase, 1 hit
Gene3Di1.10.287.400, 1 hit
3.40.50.620, 2 hits
3.90.1260.10, 2 hits
HAMAPiMF_00581 Arg_succ_synth_type2, 1 hit
InterProiView protein in InterPro
IPR023437 Arg_succ_synth_type2_subfam
IPR001518 Arginosuc_synth
IPR018223 Arginosuc_synth_CS
IPR023434 Arginosuc_synth_type_1_subfam
IPR024074 AS_cat/multimer_dom_body
IPR024073 AS_multimer_C_tail
IPR014729 Rossmann-like_a/b/a_fold
PANTHERiPTHR11587 PTHR11587, 1 hit
PfamiView protein in Pfam
PF00764 Arginosuc_synth, 1 hit
TIGRFAMsiTIGR00032 argG, 1 hit
PROSITEiView protein in PROSITE
PS00564 ARGININOSUCCIN_SYN_1, 1 hit
PS00565 ARGININOSUCCIN_SYN_2, 1 hit

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)DescriptionActionsGraphical viewLength
Sequence conflicti220I → N in AAA23482 (PubMed:2123815).Curated1
Sequence conflicti328G → D in AAA23482 (PubMed:2123815).Curated1

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
WP_000207680.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAC76205; AAC76205; b3172
BAE77217; BAE77217; BAE77217
GeneIDi947590
KEGGiecj:JW3140
eco:b3172
PATRICifig|1411691.4.peg.3559

Similar proteinsi

Entry informationi

Entry nameiASSY_ECOLI
AccessioniPrimary (citable) accession number: P0A6E4
Secondary accession number(s): P22767, Q2M939
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: January 23, 2007
Last modified: March 28, 2018
This is version 119 of the entry and version 2 of the sequence. See 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
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Main funding by: National Institutes of Health