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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)DescriptionActionsGraphical viewLength
Binding sitei104SubstrateBy similarity1

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
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)DescriptionActionsGraphical viewLength
Mutagenesisi10D → A: Loss of activity. 1 Publication1
Mutagenesisi10D → N: Reduces Kcal by 80%. Increases KM for aspartic acid 3-fold. 1 Publication1
Mutagenesisi15R → A: No effect on Kcat. Increases KM for aspartic acid 2.5-fold. 1 Publication1
Mutagenesisi26H → N: No effect on Kcat. Increases KM for aspartic acid 3-fold. 1 Publication1
Mutagenesisi29R → A: No effect on Kcat. Increases KM for aspartic acid 40-fold. 1 Publication1
Mutagenesisi55K → R: Loss of activity. 1 Publication1
Mutagenesisi124H → L: Reduces activity by 30%. 1 Publication1
Mutagenesisi143S → G: Reduces Kcat by 90%. Increases KM for aspartic acid 4-fold. 1 Publication1
Mutagenesisi143S → T: Reduces Kcat by 98.5%. Increases KM for aspartic acid 2-fold. 1 Publication1
Mutagenesisi327K → R: Reduces activity by 99.7%. Increases KM for aspartic acid 5-fold. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001613381 – 478Aspartate ammonia-lyaseAdd BLAST478

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 interactors.
DIPiDIP-36166N.
IntActiP0AC38. 12 interactors.
MINTiMINT-1258501.
STRINGi511145.b4139.

Structurei

Secondary structure

1478
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 9Combined sources6
Beta strandi14 – 20Combined sources7
Helixi25 – 33Combined sources9
Helixi47 – 64Combined sources18
Helixi70 – 83Combined sources14
Turni85 – 87Combined sources3
Helixi104 – 120Combined sources17
Turni121 – 123Combined sources3
Helixi134 – 138Combined sources5
Helixi144 – 180Combined sources37
Helixi181 – 183Combined sources3
Beta strandi185 – 187Combined sources3
Helixi190 – 192Combined sources3
Beta strandi197 – 199Combined sources3
Helixi200 – 224Combined sources25
Beta strandi234 – 237Combined sources4
Turni242 – 244Combined sources3
Helixi245 – 257Combined sources13
Beta strandi267 – 270Combined sources4
Helixi275 – 302Combined sources28
Turni305 – 307Combined sources3
Helixi331 – 355Combined sources25
Helixi365 – 389Combined sources25
Helixi391 – 393Combined sources3
Helixi398 – 405Combined sources8
Helixi412 – 414Combined sources3
Helixi416 – 419Combined sources4
Helixi421 – 432Combined sources12
Helixi438 – 445Combined sources8
Helixi451 – 454Combined sources4

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP0AC38.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni143 – 145Substrate bindingBy similarity3

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4108IJ0. Bacteria.
COG1027. LUCA.
HOGENOMiHOG000061737.
InParanoidiP0AC38.
KOiK01744.
OMAiEICENYV.
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 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti32E → V in CAA27701 (PubMed:3541901).Curated1

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1JSWX-ray2.70A/B/C/D1-478[»]
ProteinModelPortaliP0AC38.
SMRiP0AC38.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262692. 12 interactors.
DIPiDIP-36166N.
IntActiP0AC38. 12 interactors.
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.
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...

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: November 2, 2016
This is version 96 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.