SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P39377

- IADA_ECOLI

UniProt

P39377 - IADA_ECOLI

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Isoaspartyl dipeptidase
Gene
iadA, yjiF, b4328, JW4291
Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalyzes the hydrolytic cleavage of a subset of L-isoaspartyl (L-beta-aspartyl) dipeptides. Used to degrade proteins damaged by L-isoaspartyl residues formation. The best substrate for the enzyme reported thus far is iso-Asp-Leu.4 Publications

Cofactori

Binds 2 zinc ions per subunit. Has highest activity with zinc ions, but is also active with cobalt ions.3 Publications

Enzyme regulationi

P-hydroxymercuribenzoate causes a slight inhibition (8 to 17 %). Iodoacetamide, o-iodosobenzoate and ammonium persulfate do not inhibit the enzyme activity.1 Publication

Kineticsi

  1. KM=0.81 mM for beta-aspartylleucine (at pH 8.0)1 Publication

pH dependencei

Optimum pH is 7.5. Active over a wide pH range.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi68 – 681Zinc 1; via tele nitrogen; catalytic
Metal bindingi70 – 701Zinc 1; via tele nitrogen; catalytic
Binding sitei106 – 1061Substrate
Binding sitei137 – 1371Substrate
Metal bindingi162 – 1621Zinc 1; via carbamate group; catalytic
Metal bindingi162 – 1621Zinc 2; via carbamate group; catalytic
Binding sitei169 – 1691Substrate
Metal bindingi201 – 2011Zinc 2; via pros nitrogen; catalytic
Metal bindingi230 – 2301Zinc 2; via tele nitrogen; catalytic
Binding sitei233 – 2331Substrate
Active sitei285 – 2851Proton acceptor1 Publication
Metal bindingi285 – 2851Zinc 1; catalytic
Binding sitei289 – 2891Substrate; via amide nitrogen and carbonyl oxygen

GO - Molecular functioni

  1. beta-aspartyl-peptidase activity Source: UniProtKB
  2. hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds Source: InterPro
  3. metallopeptidase activity Source: UniProtKB-KW
  4. zinc ion binding Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Cobalt, Metal-binding, Zinc

Enzyme and pathway databases

BioCyciEcoCyc:G7925-MONOMER.
ECOL316407:JW4291-MONOMER.
MetaCyc:G7925-MONOMER.
SABIO-RKP39377.

Protein family/group databases

MEROPSiM38.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Isoaspartyl dipeptidase (EC:3.4.19.-)
Gene namesi
Name:iadA
Synonyms:yjiF
Ordered Locus Names:b4328, JW4291
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG12567. iadA.

Subcellular locationi

Cytoplasm 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

No observable phenotype. Does not result in reduced stationary phase or heat shock survival. Approximately 31% of the enzyme activity present.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi77 – 771E → D or Q: Reduces activity 100000-fold. 2 Publications
Mutagenesisi137 – 1371Y → A or F: Reduces activity 1000-fold. 2 Publications
Mutagenesisi169 – 1691R → K: Reduces activity 1000-fold. 1 Publication
Mutagenesisi169 – 1691R → M: Loss of activity. 1 Publication
Mutagenesisi233 – 2331R → K: Reduces activity 1000-fold. 1 Publication
Mutagenesisi233 – 2331R → M: Loss of activity. 1 Publication
Mutagenesisi285 – 2851D → A: Reduces activity 100000-fold. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 390390Isoaspartyl dipeptidase
PRO_0000079178Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei162 – 1621N6-carboxylysine

Post-translational modificationi

Carbamylation allows a single lysine to coordinate two zinc ions (1 Publication, 1 Publication, 1 Publication, 1 Publication).

Proteomic databases

PaxDbiP39377.
PRIDEiP39377.

Expressioni

Gene expression databases

GenevestigatoriP39377.

Interactioni

Protein-protein interaction databases

DIPiDIP-10001N.
IntActiP39377. 4 interactions.
STRINGi511145.b4328.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 73
Beta strandi10 – 145
Beta strandi16 – 2510
Beta strandi27 – 315
Beta strandi34 – 396
Beta strandi46 – 494
Beta strandi51 – 544
Beta strandi59 – 624
Beta strandi64 – 696
Helixi80 – 823
Helixi89 – 946
Beta strandi97 – 1026
Helixi113 – 12614
Beta strandi128 – 1358
Beta strandi137 – 1404
Beta strandi144 – 1463
Helixi148 – 1547
Beta strandi158 – 16710
Helixi175 – 19218
Beta strandi197 – 2026
Turni206 – 2094
Helixi210 – 2178
Helixi223 – 2253
Beta strandi226 – 2294
Helixi231 – 2333
Helixi235 – 24612
Beta strandi251 – 2544
Beta strandi259 – 2613
Helixi263 – 27210
Helixi277 – 2793
Beta strandi280 – 2834
Beta strandi289 – 2935
Beta strandi295 – 2973
Beta strandi299 – 3046
Helixi309 – 32113
Helixi325 – 3295
Helixi330 – 3323
Helixi334 – 3396
Beta strandi356 – 3594
Beta strandi365 – 3706
Beta strandi373 – 3775
Beta strandi380 – 3834

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ONWX-ray1.65A/B1-390[»]
1ONXX-ray2.10A/B1-390[»]
1PO9X-ray2.00A/B1-390[»]
1POJX-ray3.30A/B1-390[»]
1POKX-ray2.70A/B1-390[»]
1YBQX-ray2.00A/B1-390[»]
2AQOX-ray1.95A/B1-390[»]
2AQVX-ray1.95A/B1-390[»]
ProteinModelPortaliP39377.

Miscellaneous databases

EvolutionaryTraceiP39377.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni75 – 773Substrate binding

Sequence similaritiesi

Belongs to the peptidase M38 family.

Phylogenomic databases

eggNOGiNOG04347.
HOGENOMiHOG000275891.
KOiK01305.
OMAiIADHRSS.
OrthoDBiEOG625JTQ.
PhylomeDBiP39377.

Family and domain databases

Gene3Di2.30.40.10. 1 hit.
InterProiIPR011059. Metal-dep_hydrolase_composite.
IPR010229. Pept_M38_dipep.
[Graphical view]
PIRSFiPIRSF001238. IadA. 1 hit.
SUPFAMiSSF51338. SSF51338. 2 hits.
TIGRFAMsiTIGR01975. isoAsp_dipep. 1 hit.

Sequencei

Sequence statusi: Complete.

P39377-1 [UniParc]FASTAAdd to Basket

« Hide

MIDYTAAGFT LLQGAHLYAP EDRGICDVLV ANGKIIAVAS NIPSDIVPNC    50
TVVDLSGQIL CPGFIDQHVH LIGGGGEAGP TTRTPEVALS RLTEAGVTSV 100
VGLLGTDSIS RHPESLLAKT RALNEEGISA WMLTGAYHVP SRTITGSVEK 150
DVAIIDRVIG VKCAISDHRS AAPDVYHLAN MAAESRVGGL LGGKPGVTVF 200
HMGDSKKALQ PIYDLLENCD VPISKLLPTH VNRNVPLFEQ ALEFARKGGT 250
IDITSSIDEP VAPAEGIARA VQAGIPLARV TLSSDGNGSQ PFFDDEGNLT 300
HIGVAGFETL LETVQVLVKD YDFSISDALR PLTSSVAGFL NLTGKGEILP 350
GNDADLLVMT PELRIEQVYA RGKLMVKDGK ACVKGTFETA 390
Length:390
Mass (Da):41,084
Last modified:February 1, 1995 - v1
Checksum:i9CEEC838381545B5
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U15029 Genomic DNA. Translation: AAC43299.1.
U14003 Genomic DNA. Translation: AAA97224.1.
U00096 Genomic DNA. Translation: AAC77284.1.
AP009048 Genomic DNA. Translation: BAE78321.1.
PIRiB55889.
RefSeqiNP_418748.1. NC_000913.3.
YP_492462.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC77284; AAC77284; b4328.
BAE78321; BAE78321; BAE78321.
GeneIDi12932011.
948853.
KEGGiecj:Y75_p4214.
eco:b4328.
PATRICi32124258. VBIEscCol129921_4472.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U15029 Genomic DNA. Translation: AAC43299.1 .
U14003 Genomic DNA. Translation: AAA97224.1 .
U00096 Genomic DNA. Translation: AAC77284.1 .
AP009048 Genomic DNA. Translation: BAE78321.1 .
PIRi B55889.
RefSeqi NP_418748.1. NC_000913.3.
YP_492462.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1ONW X-ray 1.65 A/B 1-390 [» ]
1ONX X-ray 2.10 A/B 1-390 [» ]
1PO9 X-ray 2.00 A/B 1-390 [» ]
1POJ X-ray 3.30 A/B 1-390 [» ]
1POK X-ray 2.70 A/B 1-390 [» ]
1YBQ X-ray 2.00 A/B 1-390 [» ]
2AQO X-ray 1.95 A/B 1-390 [» ]
2AQV X-ray 1.95 A/B 1-390 [» ]
ProteinModelPortali P39377.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-10001N.
IntActi P39377. 4 interactions.
STRINGi 511145.b4328.

Protein family/group databases

MEROPSi M38.001.

Proteomic databases

PaxDbi P39377.
PRIDEi P39377.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC77284 ; AAC77284 ; b4328 .
BAE78321 ; BAE78321 ; BAE78321 .
GeneIDi 12932011.
948853.
KEGGi ecj:Y75_p4214.
eco:b4328.
PATRICi 32124258. VBIEscCol129921_4472.

Organism-specific databases

EchoBASEi EB2455.
EcoGenei EG12567. iadA.

Phylogenomic databases

eggNOGi NOG04347.
HOGENOMi HOG000275891.
KOi K01305.
OMAi IADHRSS.
OrthoDBi EOG625JTQ.
PhylomeDBi P39377.

Enzyme and pathway databases

BioCyci EcoCyc:G7925-MONOMER.
ECOL316407:JW4291-MONOMER.
MetaCyc:G7925-MONOMER.
SABIO-RK P39377.

Miscellaneous databases

EvolutionaryTracei P39377.
PROi P39377.

Gene expression databases

Genevestigatori P39377.

Family and domain databases

Gene3Di 2.30.40.10. 1 hit.
InterProi IPR011059. Metal-dep_hydrolase_composite.
IPR010229. Pept_M38_dipep.
[Graphical view ]
PIRSFi PIRSF001238. IadA. 1 hit.
SUPFAMi SSF51338. SSF51338. 2 hits.
TIGRFAMsi TIGR01975. isoAsp_dipep. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Purification and characterization of an isoaspartyl dipeptidase from Escherichia coli."
    Gary J.D., Clarke S.
    J. Biol. Chem. 270:4076-4087(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-24; 35-39; 84-91; 112-118; 122-147; 170-185; 187-204; 226-238; 247-264 AND 365-371, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  2. "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.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "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.
  5. "Purification and properties of a beta-aspartyl peptidase from Escherichia coli."
    Haley E.E.
    J. Biol. Chem. 243:5748-5752(1968) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
  6. "High-resolution X-ray structure of isoaspartyl dipeptidase from Escherichia coli."
    Thoden J.B., Marti-Arbona R., Raushel F.M., Holden H.M.
    Biochemistry 42:4874-4882(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 13-389 IN COMPLEX WITH ASPARTATE AND ZINC IONS, FUNCTION, COFACTOR, CARBAMYLATION AT LYS-162.
  7. "X-ray structure of isoaspartyl dipeptidase from E.coli: a dinuclear zinc peptidase evolved from amidohydrolases."
    Jozic D., Kaiser J.T., Huber R., Bode W., Maskos K.
    J. Mol. Biol. 332:243-256(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH INHIBITOR; ASPARAGINE AND ZINC IONS, COFACTOR, ACTIVE SITE, CARBAMYLATION AT LYS-162.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  8. "Mechanism of the reaction catalyzed by isoaspartyl dipeptidase from Escherichia coli."
    Marti-Arbona R., Fresquet V., Thoden J.B., Davis M.L., Holden H.M., Raushel F.M.
    Biochemistry 44:7115-7124(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG AND ZINC IONS, CATALYTIC ACTIVITY, FUNCTION, COFACTOR, CARBAMYLATION AT LYS-162, MUTAGENESIS OF GLU-77; TYR-137; ARG-169; ARG-233 AND ASP-285.
  9. "Functional significance of Glu-77 and Tyr-137 within the active site of isoaspartyl dipeptidase."
    Marti-Arbona R., Thoden J.B., Holden H.M., Raushel F.M.
    Bioorg. Chem. 33:448-458(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF MUTANTS GLN-77 AND PHE-137 IN COMPLEX WITH ZINC IONS, CARBAMYLATION AT LYS-162, MUTAGENESIS OF GLU-77 AND TYR-137.

Entry informationi

Entry nameiIADA_ECOLI
AccessioniPrimary (citable) accession number: P39377
Secondary accession number(s): Q2M5Y5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: July 9, 2014
This is version 127 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, Direct protein sequencing, 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. Peptidase families
    Classification of peptidase families and list of entries
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi