P0A6E4 (ASSY_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Argininosuccinate synthase
EC=6.3.4.5

Alternative name(s):
Citrulline--aspartate ligase

Gene names

Name:	argG
Ordered Locus Names:	b3172, JW3140

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	447 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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

Keywords
Biological process	Amino-acid biosynthesis Arginine biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	arginine biosynthetic process Inferred from electronic annotation. Source: HAMAP
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: HAMAP argininosuccinate synthase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.1 Ref.4

Chain

2 – 447

446

Argininosuccinate synthase HAMAP-Rule MF_00581

PRO_0000148695

Regions

Nucleotide binding

17 – 25

9

ATP HAMAP-Rule MF_00581

Sites

Binding site

43

1

ATP; via amide nitrogen and carbonyl oxygen

Binding site

99

1

Citrulline

Binding site

129

1

ATP; via amide nitrogen

Binding site

131

1

Aspartate

Binding site

131

1

ATP

Binding site

135

1

Aspartate

Binding site

135

1

Citrulline

Binding site

136

1

Aspartate

Binding site

136

1

ATP

Binding site

139

1

Citrulline

Binding site

192

1

Citrulline

Binding site

194

1

ATP

Binding site

201

1

Citrulline

Binding site

203

1

Citrulline

Binding site

280

1

Citrulline

Experimental info

Sequence conflict

220

1

I → N in AAA23482. Ref.1

Sequence conflict

328

1

G → D in AAA23482. Ref.1

Secondary structure

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447

Helix Strand Turn

Details...

Beta strand

4 – 7

4

Beta strand

12 – 17

6

Helix

22 – 33

12

Beta strand

37 – 44

8

Helix

55 – 63

9

Beta strand

66 – 72

7

Helix

74 – 87

14

Helix

102 – 120

19

Beta strand

125 – 127

3

Helix

136 – 147

12

Beta strand

152 – 154

3

Helix

156 – 158

3

Helix

160 – 165

6

Beta strand

166 – 168

3

Helix

169 – 178

10

Beta strand

190 – 196

7

Beta strand

199 – 204

6

Helix

205 – 208

4

Helix

214 – 216

3

Beta strand

220 – 222

3

Beta strand

235 – 242

8

Beta strand

245 – 249

5

Helix

257 – 269

13

Turn

270 – 274

5

Beta strand

276 – 281

6

Beta strand

287 – 293

7

Helix

295 – 311

17

Helix

314 – 332

19

Helix

339 – 351

13

Helix

353 – 355

3

Beta strand

358 – 364

7

Beta strand

370 – 376

7

Turn

384 – 386

3

Helix

398 – 406

9

Helix

409 – 424

16

Beta strand

427 – 429

3

Beta strand

433 – 436

4

Sequences

	Sequence		Length	Mass (Da)
	P0A6E4 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: D5E7E51BD06E1813	FASTA	447	49,898
	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

References

	« Hide 'large scale' referencesShow '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 277:1453-1474(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.

PIR

AJECRS. G65107.

RefSeq

NP_417640.1. NC_000913.2.
YP_491358.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P0A6E4.

SMR

P0A6E4. Positions 2-445.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-35842N.

IntAct

P0A6E4. 13 interactions.

STRING

511145.b3172.

2D gel databases

SWISS-2DPAGE

P0A6E4.

Proteomic databases

PaxDb

P0A6E4.

PRIDE

P0A6E4.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC76205; AAC76205; b3172.
BAE77217; BAE77217; BAE77217.

GeneID

12934127.
947590.

KEGG

ecj:Y75_p3093.
eco:b3172.

PATRIC

32121762. VBIEscCol129921_3266.

Organism-specific databases

EchoBASE

EB0066.

EcoGene

EG10068. argG.

Phylogenomic databases

eggNOG

COG0137.

HOGENOM

HOG000230094.

KO

K01940.

OMA

GGRKEMS.

ProtClustDB

PRK05370.

Enzyme and pathway databases

BioCyc

EcoCyc:ARGSUCCINSYN-MONOMER.
ECOL316407:JW3140-MONOMER.

UniPathway

UPA00068; UER00113.

Gene expression databases

Genevestigator

P0A6E4.

Family and domain databases

Gene3D

1.10.287.400. 1 hit.
3.40.50.620. 1 hit.
3.90.1260.10. 1 hit.

HAMAP

MF_00581. Arg_succ_synth_type2.

InterPro

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]

PANTHER

PTHR11587. PTHR11587. 1 hit.

Pfam

PF00764. Arginosuc_synth. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00032. argG. 1 hit.

PROSITE

PS00564. ARGININOSUCCIN_SYN_1. 1 hit.
PS00565. ARGININOSUCCIN_SYN_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

DrugBank

DB00536. Guanidine.

EvolutionaryTrace

P0A6E4.

Entry information

Entry name

ASSY_ECOLI

Accession

Primary (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:	May 1, 2013
This is version 83 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program