P11447 (ARLY_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Argininosuccinate lyase
Short name=ASAL
EC=4.3.2.1

Alternative name(s):
Arginosuccinase

Gene names

Name:	argH
Ordered Locus Names:	b3960, JW3932

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	457 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	2-(N(omega)-L-arginino)succinate = fumarate + L-arginine. HAMAP-Rule MF_00006
Pathway	Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3. HAMAP-Rule MF_00006
Subcellular location	Cytoplasm Probable HAMAP-Rule MF_00006.
Sequence similarities	Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Arginine biosynthesis
Cellular component	Cytoplasm
Molecular function	Lyase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	arginine biosynthetic process via ornithine Inferred from electronic annotation. Source: InterPro
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	argininosuccinate lyase activity Inferred from direct assay PubMed 6762207. Source: EcoCyc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 457

457

Argininosuccinate lyase HAMAP-Rule MF_00006

PRO_0000137768

Experimental info

Sequence conflict

28

1

R → G in AAB59147. Ref.5

Sequence conflict

40

1

W → R in AAB59147. Ref.5

Secondary structure

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457

Helix Strand Turn

Details...

Helix

14 – 20

7

Helix

23 – 26

4

Helix

27 – 29

3

Helix

30 – 46

17

Helix

52 – 71

20

Helix

73 – 78

6

Helix

84 – 96

13

Helix

97 – 102

6

Turn

103 – 106

4

Helix

109 – 144

36

Turn

145 – 148

4

Beta strand

150 – 155

6

Beta strand

158 – 164

7

Helix

165 – 190

26

Turn

198 – 201

4

Helix

209 – 216

8

Beta strand

219 – 221

3

Helix

225 – 230

6

Helix

233 – 259

27

Turn

262 – 264

3

Helix

271 – 273

3

Helix

287 – 294

8

Helix

296 – 310

15

Helix

319 – 323

5

Helix

324 – 346

23

Helix

353 – 360

8

Turn

363 – 366

4

Helix

367 – 376

10

Helix

381 – 398

18

Helix

402 – 404

3

Helix

407 – 410

4

Turn

411 – 413

3

Helix

421 – 424

4

Helix

427 – 432

6

Helix

442 – 456

15

Sequences

	Sequence		Length	Mass (Da)
	P11447 [UniParc]. Last modified October 1, 1993. Version 3. Checksum: 0109EF31675B9717	FASTA	457	50,318
	10 20 30 40 50 60 MALWGGRFTQ AADQRFKQFN DSLRFDYRLA EQDIVGSVAW SKALVTVGVL TAEEQAQLEE 70 80 90 100 110 120 ALNVLLEDVR ARPQQILESD AEDIHSWVEG KLIDKVGQLG KKLHTGRSRN DQVATDLKLW 130 140 150 160 170 180 CKDTVSELLT ANRQLQSALV ETAQNNQDAV MPGYTHLQRA QPVTFAHWCL AYVEMLARDE 190 200 210 220 230 240 SRLQDALKRL DVSPLGCGAL AGTAYEIDRE QLAGWLGFAS ATRNSLDSVS DRDHVLELLS 250 260 270 280 290 300 AAAIGMVHLS RFAEDLIFFN TGEAGFVELS DRVTSGSSLM PQKKNPDALE LIRGKCGRVQ 310 320 330 340 350 360 GALTGMMMTL KGLPLAYNKD MQEDKEGLFD ALDTWLDCLH MAALVLDGIQ VKRPRCQEAA 370 380 390 400 410 420 QQGYANATEL ADYLVAKGVP FREAHHIVGE AVVEAIRQGK PLEDLPLSEL QKFSQVIDED 430 440 450 VYPILSLQSC LDKRAAKGGV SPQQVAQAIA FAQARLG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes." Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L. Nucleic Acids Res. 21:5408-5417(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[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]	"Nucleotide sequence of Escherichia coli argB and argC genes: comparison of N-acetylglutamate kinase and N-acetylglutamate-gamma-semialdehyde dehydrogenase with homologous and analogous enzymes." Parsot C., Boyen A., Cohen G.N., Glansdorff N. Gene 68:275-283(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-51.
[5]	"IS3 can function as a mobile promoter in E. coli." Charlier D.R.M., Piette J., Glansdorff N. Nucleic Acids Res. 10:5935-5948(1982) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-44. Strain: K12.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U00006 Genomic DNA. Translation: AAC43066.1.
U00096 Genomic DNA. Translation: AAC76942.1.
AP009048 Genomic DNA. Translation: BAE77351.1.
M21446 Genomic DNA. Translation: AAA23479.1.
J01590 Genomic DNA. Translation: AAB59147.1.

PIR

C65203.

RefSeq

NP_418395.1. NC_000913.2.
YP_491492.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1TJ7	X-ray	2.44	A/B	1-457	[»]

ProteinModelPortal

P11447.

SMR

P11447. Positions 3-457.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-9142N.

STRING

511145.b3960.

Proteomic databases

PaxDb

P11447.

PRIDE

P11447.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC76942; AAC76942; b3960.
BAE77351; BAE77351; BAE77351.

GeneID

12934472.
948463.

KEGG

ecj:Y75_p3228.
eco:b3960.

PATRIC

32123441. VBIEscCol129921_4081.

Organism-specific databases

EchoBASE

EB1205.

EcoGene

EG11223. argH.

Phylogenomic databases

eggNOG

COG0165.

HOGENOM

HOG000242744.

KO

K01755.

OMA

KEGIFDA.

ProtClustDB

PRK04833.

Enzyme and pathway databases

BioCyc

EcoCyc:ARGSUCCINLYA-MONOMER.
ECOL316407:JW3932-MONOMER.
MetaCyc:ARGSUCCINLYA-MONOMER.

UniPathway

UPA00068; UER00114.

Gene expression databases

Genevestigator

P11447.

Family and domain databases

Gene3D

1.10.275.10. 1 hit.

HAMAP

MF_00006. Arg_succ_lyase.

InterPro

IPR009049. Argininosuccinate_lyase.
IPR003031. D_crystallin.
IPR024083. Fumarase/histidase_N.
IPR000362. Fumarate_lyase.
IPR020557. Fumarate_lyase_CS.
IPR022761. Fumarate_lyase_N.
IPR008948. L-Aspartase-like.
[Graphical view]

PANTHER

PTHR11444:SF3. PTHR11444:SF3. 1 hit.

Pfam

PF00206. Lyase_1. 1 hit.
[Graphical view]

PRINTS

PR00145. ARGSUCLYASE.
PR00149. FUMRATELYASE.

SUPFAM

SSF48557. L-Aspartase-like. 1 hit.

TIGRFAMs

TIGR00838. argH. 1 hit.

PROSITE

PS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P11447.

Entry information

Entry name

ARLY_ECOLI

Accession

Primary (citable) accession number: P11447
Secondary accession number(s): Q2M8Q5, Q47060

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1989
Last sequence update:	October 1, 1993
Last modified:	May 1, 2013
This is version 127 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program