UniProtKB - P37595 (IAAA_ECOLI)
Protein
Isoaspartyl peptidase
Gene
iaaA
Organism
Escherichia coli (strain K12)
Status
Functioni
Degrades proteins damaged by L-isoaspartyl residue formation (also known as beta-Asp residues). Degrades L-isoaspartyl-containing di- and maybe also tripeptides. Also has L-asparaginase activity, although this may not be its principal function.1 Publication
May be involved in glutathione, and possibly other peptide, transport, although these results could also be due to polar effects of disruption.1 Publication
Catalytic activityi
- Cleavage of a beta-linked Asp residue from the N-terminus of a polypeptide. EC:3.4.19.5
Kineticsi
No activity for GlcNAc-Asn, Gly-L-Asn, L-Asp, L-Asn-alpha-amide, L-Gln, aspartylglucosamides alpha- or gamma-aspartyl dipeptides.
- KM=0.138 mM for beta-L-Asp-L-Leu1 Publication
- KM=3.9 mM for L-Asn1 Publication
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 179 | Nucleophile1 Publication | 1 |
GO - Molecular functioni
- asparaginase activity Source: EcoCyc
- beta-aspartyl-peptidase activity Source: EcoCyc
- hydrolase activity Source: EcoliWiki
GO - Biological processi
- protein autoprocessing Source: EcoCyc
Keywordsi
Molecular function | Hydrolase, Protease |
Enzyme and pathway databases
BioCyci | EcoCyc:EG12407-MONOMER MetaCyc:EG12407-MONOMER |
BRENDAi | 3.4.19.5, 2026 3.5.1.1, 2026 |
SABIO-RKi | P37595 |
Protein family/group databases
MEROPSi | T02.002 |
Names & Taxonomyi
Protein namesi | Recommended name: Isoaspartyl peptidase (EC:3.4.19.5)Alternative name(s): Beta-aspartyl-peptidase EcAIII Isoaspartyl dipeptidase Cleaved into the following 2 chains: |
Gene namesi | Name:iaaA Synonyms:spt, ybiK Ordered Locus Names:b0828, JW0812 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
Pathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 179 | T → A: Catalytically inactive. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | Removed | |||
ChainiPRO_0000002349 | 2 – 178 | Isoaspartyl peptidase subunit alphaAdd BLAST | 177 | |
ChainiPRO_0000329014 | 179 – 321 | Isoaspartyl peptidase subunit betaAdd BLAST | 143 |
Post-translational modificationi
Autocleaved. Generates the alpha and beta subunits. The N-terminal residue of the beta subunit is thought to be responsible for the nucleophile hydrolase activity.
Both subunits undergo further processing at their C-termini. The overexpressed alpha subunit seems to consist of residues 2-161, with an oxidized Met residue and a tightly coordinated Na+, whereas the overexpressed beta subunit is processed to residue 315 and has 3 oxidized Met residues. Processing of the alpha subunit is inhibited by Zn2+.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 178 – 179 | Cleavage; by autolysis1 Publication | 2 |
Keywords - PTMi
Autocatalytic cleavageProteomic databases
jPOSTi | P37595 |
PaxDbi | P37595 |
PRIDEi | P37595 |
Expressioni
Inductioni
Repressed by cysteine, an effect that is attributed to CysB.
Interactioni
Subunit structurei
Heterotetramer of two alpha and two beta chains arranged as a dimer of alpha/beta heterodimers.
4 PublicationsProtein-protein interaction databases
BioGRIDi | 4259980, 8 interactors |
IntActi | P37595, 9 interactors |
STRINGi | 511145.b0828 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P37595 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P37595 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 207 – 210 | Substrate bindingCombined sources1 Publication | 4 | |
Regioni | 230 – 233 | Substrate bindingCombined sources1 Publication | 4 |
Sequence similaritiesi
Belongs to the Ntn-hydrolase family.Curated
Phylogenomic databases
eggNOGi | COG1446, Bacteria |
HOGENOMi | CLU_021603_1_0_6 |
InParanoidi | P37595 |
PhylomeDBi | P37595 |
Family and domain databases
InterProi | View protein in InterPro IPR029055, Ntn_hydrolases_N IPR000246, Peptidase_T2 |
PANTHERi | PTHR10188, PTHR10188, 2 hits |
Pfami | View protein in Pfam PF01112, Asparaginase_2, 1 hit |
SUPFAMi | SSF56235, SSF56235, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
P37595-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MGKAVIAIHG GAGAISRAQM SLQQELRYIE ALSAIVETGQ KMLEAGESAL
60 70 80 90 100
DVVTEAVRLL EECPLFNAGI GAVFTRDETH ELDACVMDGN TLKAGAVAGV
110 120 130 140 150
SHLRNPVLAA RLVMEQSPHV MMIGEGAENF AFARGMERVS PEIFSTSLRY
160 170 180 190 200
EQLLAARKEG ATVLDHSGAP LDEKQKMGTV GAVALDLDGN LAAATSTGGM
210 220 230 240 250
TNKLPGRVGD SPLVGAGCYA NNASVAVSCT GTGEVFIRAL AAYDIAALMD
260 270 280 290 300
YGGLSLAEAC ERVVMEKLPA LGGSGGLIAI DHEGNVALPF NTEGMYRAWG
310 320
YAGDTPTTGI YREKGDTVAT Q
Mass spectrometryi
Molecular mass is 17091 Da. Determined by ESI. Subunit alpha.1 Publication
Molecular mass is 13852 Da. Determined by ESI. Subunit beta.1 Publication
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | U00096 Genomic DNA Translation: AAC73915.1 AP009048 Genomic DNA Translation: BAA35516.1 M21151 Genomic DNA No translation available. |
PIRi | D64820 |
RefSeqi | NP_415349.1, NC_000913.3 WP_000513781.1, NZ_LN832404.1 |
Genome annotation databases
EnsemblBacteriai | AAC73915; AAC73915; b0828 BAA35516; BAA35516; BAA35516 |
GeneIDi | 945456 |
KEGGi | ecj:JW0812 eco:b0828 |
PATRICi | fig|1411691.4.peg.1450 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | U00096 Genomic DNA Translation: AAC73915.1 AP009048 Genomic DNA Translation: BAA35516.1 M21151 Genomic DNA No translation available. |
PIRi | D64820 |
RefSeqi | NP_415349.1, NC_000913.3 WP_000513781.1, NZ_LN832404.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1JN9 | X-ray | 2.30 | A/C | 2-178 | [»] | |
B/D | 179-321 | [»] | ||||
1K2X | X-ray | 1.65 | A/C | 2-178 | [»] | |
B/D | 179-321 | [»] | ||||
1T3M | X-ray | 1.65 | A/C | 2-178 | [»] | |
B/D | 179-321 | [»] | ||||
2ZAK | X-ray | 2.01 | A/B | 2-321 | [»] | |
2ZAL | X-ray | 1.90 | A/C | 2-161 | [»] | |
B/D | 179-315 | [»] | ||||
3C17 | X-ray | 1.95 | A/B | 2-321 | [»] | |
SMRi | P37595 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 4259980, 8 interactors |
IntActi | P37595, 9 interactors |
STRINGi | 511145.b0828 |
Protein family/group databases
MEROPSi | T02.002 |
Proteomic databases
jPOSTi | P37595 |
PaxDbi | P37595 |
PRIDEi | P37595 |
Genome annotation databases
EnsemblBacteriai | AAC73915; AAC73915; b0828 BAA35516; BAA35516; BAA35516 |
GeneIDi | 945456 |
KEGGi | ecj:JW0812 eco:b0828 |
PATRICi | fig|1411691.4.peg.1450 |
Organism-specific databases
EchoBASEi | EB2307 |
Phylogenomic databases
eggNOGi | COG1446, Bacteria |
HOGENOMi | CLU_021603_1_0_6 |
InParanoidi | P37595 |
PhylomeDBi | P37595 |
Enzyme and pathway databases
BioCyci | EcoCyc:EG12407-MONOMER MetaCyc:EG12407-MONOMER |
BRENDAi | 3.4.19.5, 2026 3.5.1.1, 2026 |
SABIO-RKi | P37595 |
Miscellaneous databases
EvolutionaryTracei | P37595 |
PROi | PR:P37595 |
Family and domain databases
InterProi | View protein in InterPro IPR029055, Ntn_hydrolases_N IPR000246, Peptidase_T2 |
PANTHERi | PTHR10188, PTHR10188, 2 hits |
Pfami | View protein in Pfam PF01112, Asparaginase_2, 1 hit |
SUPFAMi | SSF56235, SSF56235, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | IAAA_ECOLI | |
Accessioni | P37595Primary (citable) accession number: P37595 Secondary accession number(s): P75795 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | October 1, 1994 |
Last sequence update: | November 1, 1997 | |
Last modified: | December 2, 2020 | |
This is version 151 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families