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Protein

Aspartate ammonia-lyase

Gene

aspA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

L-aspartate = fumarate + NH3.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei104 – 1041SubstrateBy similarity

GO - Molecular functioni

  • aspartate ammonia-lyase activity Source: EcoCyc

GO - Biological processi

  • aspartate metabolic process Source: EcoCyc
  • cellular amino acid biosynthetic process Source: EcoCyc
  • protein tetramerization Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Enzyme and pathway databases

BioCyciEcoCyc:ASPARTASE-MONOMER.
ECOL316407:JW4099-MONOMER.
MetaCyc:ASPARTASE-MONOMER.
BRENDAi4.3.1.1. 2026.
SABIO-RKP0AC38.

Names & Taxonomyi

Protein namesi
Recommended name:
Aspartate ammonia-lyase (EC:4.3.1.1)
Short name:
Aspartase
Gene namesi
Name:aspA
Ordered Locus Names:b4139, JW4099
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10095. aspA.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: UniProtKB
  • membrane Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi10 – 101D → A: Loss of activity. 1 Publication
Mutagenesisi10 – 101D → N: Reduces Kcal by 80%. Increases KM for aspartic acid 3-fold. 1 Publication
Mutagenesisi15 – 151R → A: No effect on Kcat. Increases KM for aspartic acid 2.5-fold. 1 Publication
Mutagenesisi26 – 261H → N: No effect on Kcat. Increases KM for aspartic acid 3-fold. 1 Publication
Mutagenesisi29 – 291R → A: No effect on Kcat. Increases KM for aspartic acid 40-fold. 1 Publication
Mutagenesisi55 – 551K → R: Loss of activity. 1 Publication
Mutagenesisi124 – 1241H → L: Reduces activity by 30%. 1 Publication
Mutagenesisi143 – 1431S → G: Reduces Kcat by 90%. Increases KM for aspartic acid 4-fold. 1 Publication
Mutagenesisi143 – 1431S → T: Reduces Kcat by 98.5%. Increases KM for aspartic acid 2-fold. 1 Publication
Mutagenesisi327 – 3271K → R: Reduces activity by 99.7%. Increases KM for aspartic acid 5-fold. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 478478Aspartate ammonia-lyasePRO_0000161338Add
BLAST

Proteomic databases

EPDiP0AC38.
PaxDbiP0AC38.
PRIDEiP0AC38.

Interactioni

Subunit structurei

Homotetramer.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
dnaKP0A6Y82EBI-544200,EBI-542092

Protein-protein interaction databases

BioGridi4262692. 12 interactions.
DIPiDIP-36166N.
IntActiP0AC38. 12 interactions.
MINTiMINT-1258501.
STRINGi511145.b4139.

Structurei

Secondary structure

1
478
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 96Combined sources
Beta strandi14 – 207Combined sources
Helixi25 – 339Combined sources
Helixi47 – 6418Combined sources
Helixi70 – 8314Combined sources
Turni85 – 873Combined sources
Helixi104 – 12017Combined sources
Turni121 – 1233Combined sources
Helixi134 – 1385Combined sources
Helixi144 – 18037Combined sources
Helixi181 – 1833Combined sources
Beta strandi185 – 1873Combined sources
Helixi190 – 1923Combined sources
Beta strandi197 – 1993Combined sources
Helixi200 – 22425Combined sources
Beta strandi234 – 2374Combined sources
Turni242 – 2443Combined sources
Helixi245 – 25713Combined sources
Beta strandi267 – 2704Combined sources
Helixi275 – 30228Combined sources
Turni305 – 3073Combined sources
Helixi331 – 35525Combined sources
Helixi365 – 38925Combined sources
Helixi391 – 3933Combined sources
Helixi398 – 4058Combined sources
Helixi412 – 4143Combined sources
Helixi416 – 4194Combined sources
Helixi421 – 43212Combined sources
Helixi438 – 4458Combined sources
Helixi451 – 4544Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JSWX-ray2.70A/B/C/D1-478[»]
ProteinModelPortaliP0AC38.
SMRiP0AC38. Positions 1-460.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AC38.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni143 – 1453Substrate bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4108IJ0. Bacteria.
COG1027. LUCA.
HOGENOMiHOG000061737.
InParanoidiP0AC38.
KOiK01744.
OMAiEICENYV.
OrthoDBiEOG6V1M4M.
PhylomeDBiP0AC38.

Family and domain databases

Gene3Di1.10.275.10. 1 hit.
InterProiIPR004708. ApsA.
IPR024083. Fumarase/histidase_N.
IPR018951. Fumarase_C_C.
IPR020557. Fumarate_lyase_CS.
IPR000362. Fumarate_lyase_fam.
IPR022761. Fumarate_lyase_N.
IPR008948. L-Aspartase-like.
[Graphical view]
PANTHERiPTHR11444. PTHR11444. 1 hit.
PfamiPF10415. FumaraseC_C. 1 hit.
PF00206. Lyase_1. 1 hit.
[Graphical view]
PRINTSiPR00149. FUMRATELYASE.
SUPFAMiSSF48557. SSF48557. 1 hit.
TIGRFAMsiTIGR00839. aspA. 1 hit.
PROSITEiPS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0AC38-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSNNIRIEED LLGTREVPAD AYYGVHTLRA IENFYISNNK ISDIPEFVRG
60 70 80 90 100
MVMVKKAAAM ANKELQTIPK SVANAIIAAC DEVLNNGKCM DQFPVDVYQG
110 120 130 140 150
GAGTSVNMNT NEVLANIGLE LMGHQKGEYQ YLNPNDHVNK CQSTNDAYPT
160 170 180 190 200
GFRIAVYSSL IKLVDAINQL REGFERKAVE FQDILKMGRT QLQDAVPMTL
210 220 230 240 250
GQEFRAFSIL LKEEVKNIQR TAELLLEVNL GATAIGTGLN TPKEYSPLAV
260 270 280 290 300
KKLAEVTGFP CVPAEDLIEA TSDCGAYVMV HGALKRLAVK MSKICNDLRL
310 320 330 340 350
LSSGPRAGLN EINLPELQAG SSIMPAKVNP VVPEVVNQVC FKVIGNDTTV
360 370 380 390 400
TMAAEAGQLQ LNVMEPVIGQ AMFESVHILT NACYNLLEKC INGITANKEV
410 420 430 440 450
CEGYVYNSIG IVTYLNPFIG HHNGDIVGKI CAETGKSVRE VVLERGLLTE
460 470
AELDDIFSVQ NLMHPAYKAK RYTDESEQ
Length:478
Mass (Da):52,356
Last modified:August 13, 1987 - v1
Checksum:iB6E8432DBF385DEA
GO

Sequence cautioni

The sequence AAA97038.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti32 – 321E → V in CAA27701 (PubMed:3541901).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiA01159. UFECDW.
RefSeqiNP_418562.4. NC_000913.3.
WP_000069437.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC77099; AAC77099; b4139.
BAE78141; BAE78141; BAE78141.
GeneIDi948658.
KEGGiecj:JW4099.
eco:b4139.
PATRICi32123845. VBIEscCol129921_4270.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiA01159. UFECDW.
RefSeqiNP_418562.4. NC_000913.3.
WP_000069437.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JSWX-ray2.70A/B/C/D1-478[»]
ProteinModelPortaliP0AC38.
SMRiP0AC38. Positions 1-460.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262692. 12 interactions.
DIPiDIP-36166N.
IntActiP0AC38. 12 interactions.
MINTiMINT-1258501.
STRINGi511145.b4139.

Proteomic databases

EPDiP0AC38.
PaxDbiP0AC38.
PRIDEiP0AC38.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC77099; AAC77099; b4139.
BAE78141; BAE78141; BAE78141.
GeneIDi948658.
KEGGiecj:JW4099.
eco:b4139.
PATRICi32123845. VBIEscCol129921_4270.

Organism-specific databases

EchoBASEiEB0093.
EcoGeneiEG10095. aspA.

Phylogenomic databases

eggNOGiENOG4108IJ0. Bacteria.
COG1027. LUCA.
HOGENOMiHOG000061737.
InParanoidiP0AC38.
KOiK01744.
OMAiEICENYV.
OrthoDBiEOG6V1M4M.
PhylomeDBiP0AC38.

Enzyme and pathway databases

BioCyciEcoCyc:ASPARTASE-MONOMER.
ECOL316407:JW4099-MONOMER.
MetaCyc:ASPARTASE-MONOMER.
BRENDAi4.3.1.1. 2026.
SABIO-RKP0AC38.

Miscellaneous databases

EvolutionaryTraceiP0AC38.
PROiP0AC38.

Family and domain databases

Gene3Di1.10.275.10. 1 hit.
InterProiIPR004708. ApsA.
IPR024083. Fumarase/histidase_N.
IPR018951. Fumarase_C_C.
IPR020557. Fumarate_lyase_CS.
IPR000362. Fumarate_lyase_fam.
IPR022761. Fumarate_lyase_N.
IPR008948. L-Aspartase-like.
[Graphical view]
PANTHERiPTHR11444. PTHR11444. 1 hit.
PfamiPF10415. FumaraseC_C. 1 hit.
PF00206. Lyase_1. 1 hit.
[Graphical view]
PRINTSiPR00149. FUMRATELYASE.
SUPFAMiSSF48557. SSF48557. 1 hit.
TIGRFAMsiTIGR00839. aspA. 1 hit.
PROSITEiPS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiASPA_ECOLI
AccessioniPrimary (citable) accession number: P0AC38
Secondary accession number(s): P04422, P78140, Q2M6G5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: March 16, 2016
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.