P0AC38 (ASPA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Aspartate ammonia-lyase
Short name=Aspartase
EC=4.3.1.1

Gene names

Name:	aspA
Ordered Locus Names:	b4139, JW4099

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

General annotation (Comments)

Catalytic activity	L-aspartate = fumarate + NH3.
Subunit structure	Homotetramer. Ref.8
Sequence similarities	Belongs to the class-II fumarase/aspartase family. Aspartase subfamily.
Sequence caution	The sequence AAA97038.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Molecular function	Lyase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	aspartate metabolic process Inferred from direct assay PubMed 5000448. Source: EcoCyc cellular amino acid biosynthetic process Inferred from direct assay PubMed 5000448. Source: EcoCyc tricarboxylic acid cycle Inferred from electronic annotation. Source: InterPro
Cellular_component	cytosol Inferred from direct assay PubMed 16858726. Source: UniProtKB membrane Inferred from direct assay PubMed 16858726. Source: UniProtKB
Molecular_function	aspartate ammonia-lyase activity Inferred from direct assay PubMed 5000448. Source: EcoCyc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
dnaK	P0A6Y8	2	EBI-544200,EBI-542092

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 478

478

Aspartate ammonia-lyase

PRO_0000161338

Regions

Region

143 – 145

3

Substrate binding By similarity

Sites

Binding site

104

1

Substrate By similarity

Experimental info

Mutagenesis

10

1

D → A: Loss of activity. Ref.7

Mutagenesis

10

1

D → N: Reduces Kcal by 80%. Increases KM for aspartic acid 3-fold. Ref.7

Mutagenesis

15

1

R → A: No effect on Kcat. Increases KM for aspartic acid 2.5-fold. Ref.7

Mutagenesis

26

1

H → N: No effect on Kcat. Increases KM for aspartic acid 3-fold. Ref.7

Mutagenesis

29

1

R → A: No effect on Kcat. Increases KM for aspartic acid 40-fold. Ref.7

Mutagenesis

55

1

K → R: Loss of activity. Ref.6

Mutagenesis

124

1

H → L: Reduces activity by 30%. Ref.6

Mutagenesis

143

1

S → G: Reduces Kcat by 90%. Increases KM for aspartic acid 4-fold. Ref.7

Mutagenesis

143

1

S → T: Reduces Kcat by 98.5%. Increases KM for aspartic acid 2-fold. Ref.7

Mutagenesis

327

1

K → R: Reduces activity by 99.7%. Increases KM for aspartic acid 5-fold. Ref.6

Sequence conflict

32

1

E → V in CAA27701. Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

478

Helix Strand Turn

Details...

Beta strand

4 – 9

6

Beta strand

14 – 20

7

Helix

25 – 33

9

Helix

47 – 64

18

Helix

70 – 83

14

Turn

85 – 87

3

Helix

104 – 120

17

Turn

121 – 123

3

Helix

134 – 138

5

Helix

144 – 180

37

Helix

181 – 183

3

Beta strand

185 – 187

3

Helix

190 – 192

3

Beta strand

197 – 199

3

Helix

200 – 224

25

Beta strand

234 – 237

4

Turn

242 – 244

3

Helix

245 – 257

13

Beta strand

267 – 270

4

Helix

275 – 302

28

Turn

305 – 307

3

Helix

331 – 355

25

Helix

365 – 389

25

Helix

391 – 393

3

Helix

398 – 405

8

Helix

412 – 414

3

Helix

416 – 419

4

Helix

421 – 432

12

Helix

438 – 445

8

Helix

451 – 454

4

Sequences

	Sequence		Length	Mass (Da)
	P0AC38 [UniParc]. Last modified August 13, 1987. Version 1. Checksum: B6E8432DBF385DEA	FASTA	478	52,356
	10 20 30 40 50 60 MSNNIRIEED LLGTREVPAD AYYGVHTLRA IENFYISNNK ISDIPEFVRG MVMVKKAAAM 70 80 90 100 110 120 ANKELQTIPK SVANAIIAAC DEVLNNGKCM DQFPVDVYQG GAGTSVNMNT NEVLANIGLE 130 140 150 160 170 180 LMGHQKGEYQ YLNPNDHVNK CQSTNDAYPT GFRIAVYSSL IKLVDAINQL REGFERKAVE 190 200 210 220 230 240 FQDILKMGRT QLQDAVPMTL GQEFRAFSIL LKEEVKNIQR TAELLLEVNL GATAIGTGLN 250 260 270 280 290 300 TPKEYSPLAV KKLAEVTGFP CVPAEDLIEA TSDCGAYVMV HGALKRLAVK MSKICNDLRL 310 320 330 340 350 360 LSSGPRAGLN EINLPELQAG SSIMPAKVNP VVPEVVNQVC FKVIGNDTTV TMAAEAGQLQ 370 380 390 400 410 420 LNVMEPVIGQ AMFESVHILT NACYNLLEKC INGITANKEV CEGYVYNSIG IVTYLNPFIG 430 440 450 460 470 HHNGDIVGKI CAETGKSVRE VVLERGLLTE AELDDIFSVQ NLMHPAYKAK RYTDESEQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and nucleotide sequence of the aspartase gene of Escherichia coli W." Takagi J.S., Ida N., Tokushige M., Sakamoto H., Shimura Y. Nucleic Acids Res. 13:2063-2074(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: W / ATCC 11105 / DSM 1900.
[2]	"Structural and functional relationships between fumarase and aspartase. Nucleotide sequences of the fumarase (fumC) and aspartase (aspA) genes of Escherichia coli K12." Woods S.A., Miles J.S., Roberts R.E., Guest J.R. Biochem. J. 237:547-557(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[3]	"Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes." Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R. Nucleic Acids Res. 23:2105-2119(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"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.
[5]	"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.
[6]	"Mutagenic investigation of conserved functional amino acids in Escherichia coli L-aspartase." Saribas A.S., Schindler J.F., Viola R.E. J. Biol. Chem. 269:6313-6319(1994) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF LYS-55; HIS-124 AND LYS-327.
[7]	"Evaluation of functionally important amino acids in L-aspartate ammonia-lyase from Escherichia coli." Jayasekera M.M., Shi W., Farber G.K., Viola R.E. Biochemistry 36:9145-9150(1997) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF ASP-10; ARG-15; HIS-26; ARG-29 AND SER-143.
[8]	"The structure of L-aspartate ammonia-lyase from Escherichia coli." Shi W., Dunbar J., Jayasekera M.M.K., Viola R.E., Farber G.K. Biochemistry 36:9136-9144(1997) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), SUBUNIT.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X02307 Genomic DNA. Translation: CAA26173.1.
X04066 Genomic DNA. Translation: CAA27701.1.
U14003 Genomic DNA. Translation: AAA97038.1. Different initiation.
U00096 Genomic DNA. Translation: AAC77099.2.
AP009048 Genomic DNA. Translation: BAE78141.1.

PIR

UFECDW. A01159.

RefSeq

NP_418562.4. NC_000913.2.
YP_492282.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1JSW	X-ray	2.70	A/B/C/D	1-478	[»]

ProteinModelPortal

P0AC38.

SMR

P0AC38. Positions 1-460.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-36166N.

IntAct

P0AC38. 12 interactions.

MINT

MINT-1258501.

STRING

511145.b4139.

Proteomic databases

PaxDb

P0AC38.

PRIDE

P0AC38.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC77099; AAC77099; b4139.
BAE78141; BAE78141; BAE78141.

GeneID

12933698.
948658.

KEGG

ecj:Y75_p4026.
eco:b4139.

PATRIC

32123845. VBIEscCol129921_4270.

Organism-specific databases

EchoBASE

EB0093.

EcoGene

EG10095. aspA.

Phylogenomic databases

eggNOG

COG1027.

HOGENOM

HOG000061737.

KO

K01744.

OMA

VGKICAQ.

ProtClustDB

PRK12273.

Enzyme and pathway databases

BioCyc

EcoCyc:ASPARTASE-MONOMER.
ECOL316407:JW4099-MONOMER.
MetaCyc:ASPARTASE-MONOMER.

BRENDA

4.3.1.1. 2026.

SABIO-RK

P0AC38.

Gene expression databases

Genevestigator

P0AC38.

Family and domain databases

Gene3D

1.10.275.10. 1 hit.

InterPro

IPR004708. ApsA.
IPR003031. D_crystallin.
IPR024083. Fumarase/histidase_N.
IPR018951. Fumarase_C_C.
IPR000362. Fumarate_lyase.
IPR020557. Fumarate_lyase_CS.
IPR022761. Fumarate_lyase_N.
IPR008948. L-Aspartase-like.
[Graphical view]

Pfam

PF10415. FumaraseC_C. 1 hit.
PF00206. Lyase_1. 1 hit.
[Graphical view]

PRINTS

PR00145. ARGSUCLYASE.
PR00149. FUMRATELYASE.

SUPFAM

SSF48557. L-Aspartase-like. 1 hit.

TIGRFAMs

TIGR00839. aspA. 1 hit.

PROSITE

PS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P0AC38.

Entry information

Entry name

ASPA_ECOLI

Accession

Primary (citable) accession number: P0AC38
Secondary accession number(s): P04422, P78140, Q2M6G5

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 13, 1987
Last sequence update:	August 13, 1987
Last modified:	May 1, 2013
This is version 73 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program