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Isoaspartyl peptidase (EC 3.4.19.5) (Beta-aspartyl-peptidase) (EcAIII) (Isoaspartyl dipeptidase) [Cleaved into: Isoaspartyl peptidase subunit alpha; Isoaspartyl peptidase subunit beta]

 IAAA_ECOLI              Reviewed;         321 AA.
P37595; P75795;
01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 2.
28-MAR-2018, entry version 136.
RecName: Full=Isoaspartyl peptidase;
EC=3.4.19.5;
AltName: Full=Beta-aspartyl-peptidase;
AltName: Full=EcAIII;
AltName: Full=Isoaspartyl dipeptidase;
Contains:
RecName: Full=Isoaspartyl peptidase subunit alpha;
Contains:
RecName: Full=Isoaspartyl peptidase subunit beta;
Flags: Precursor;
Name=iaaA; Synonyms=spt, ybiK; OrderedLocusNames=b0828, JW0812;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=8905232; DOI=10.1093/dnares/3.3.137;
Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A.,
Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K.,
Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K.,
Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N.,
Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y.,
Yano M., Horiuchi T.;
"A 718-kb DNA sequence of the Escherichia coli K-12 genome
corresponding to the 12.7-28.0 min region on the linkage map.";
DNA Res. 3:137-155(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
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.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-52.
PubMed=3045084; DOI=10.1128/jb.170.9.4097-4102.1988;
Nohno T., Kasai Y., Saito T.;
"Cloning and sequencing of the Escherichia coli chlEN operon involved
in molybdopterin biosynthesis.";
J. Bacteriol. 170:4097-4102(1988).
[5]
PROTEIN SEQUENCE OF 179-183, FUNCTION, SUBUNIT, AND AUTOCATALYTIC
CLEAVAGE.
PubMed=11988085;
Hejazi M., Piotukh K., Mattow J., Deutzmann R., Volkmer-Engert R.,
Lockau W.;
"Isoaspartyl dipeptidase activity of plant-type asparaginases.";
Biochem. J. 364:129-136(2002).
[6]
IDENTIFICATION.
PubMed=7984428; DOI=10.1093/nar/22.22.4756;
Borodovsky M., Rudd K.E., Koonin E.V.;
"Intrinsic and extrinsic approaches for detecting genes in a bacterial
genome.";
Nucleic Acids Res. 22:4756-4767(1994).
[7]
PROBABLE AUTOCATALYTIC CLEAVAGE, SUBUNIT, AND PRELIMINARY
CRYSTALLIZATION.
STRAIN=K12 / JM108;
PubMed=11053866; DOI=10.1107/S0907444900010076;
Borek D., Jaskolski M.;
"Crystallization and preliminary crystallographic studies of a new L-
asparaginase encoded by the Escherichia coli genome.";
Acta Crystallogr. D 56:1505-1507(2000).
[8]
POSSIBLE FUNCTION IN GLUTATHIONE TRANSPORT, AND CONTROL OF EXPRESSION
BY CYSB.
STRAIN=K12;
PubMed=12007658; DOI=10.1111/j.1574-6968.2002.tb11113.x;
Parry J., Clark D.P.;
"Identification of a CysB-regulated gene involved in glutathione
transport in Escherichia coli.";
FEMS Microbiol. Lett. 209:81-85(2002).
[9]
MASS SPECTROMETRY, AND KINETIC PARAMETERS.
STRAIN=K12 / DH5-alpha;
PubMed=15265041; DOI=10.1111/j.1432-1033.2004.04254.x;
Borek D., Michalska K., Brzezinski K., Kisiel A., Podkowinski J.,
Bonthron D.T., Krowarsch D., Otlewski J., Jaskolski M.;
"Expression, purification and catalytic activity of Lupinus luteus
asparagine beta-amidohydrolase and its Escherichia coli homolog.";
Eur. J. Biochem. 271:3215-3226(2004).
[10]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 2-321.
Borek D.;
"Structural and biochemical studies of asparaginases.";
Thesis (2001), A. Mickiewicz University, Poland.
[11]
X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 2-321, AND SUBUNIT.
PubMed=15159592; DOI=10.1107/S0907444904003403;
Prahl A., Pazgier M., Hejazi M., Lockau W., Lubkowski J.;
"Structure of the isoaspartyl peptidase with L-asparaginase activity
from Escherichia coli.";
Acta Crystallogr. D 60:1173-1176(2004).
[12]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 2-315 IN COMPLEX WITH
L-ASPARTATE.
STRAIN=K12 / DH5-alpha;
PubMed=15946951; DOI=10.1074/jbc.M504501200;
Michalska K., Brzezinski K., Jaskolski M.;
"Crystal structure of isoaspartyl aminopeptidase in complex with L-
aspartate.";
J. Biol. Chem. 280:28484-28491(2005).
[13]
X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 2-321 OF MUTANT THR-179, AND
ACTIVE SITE.
PubMed=18323626; DOI=10.1107/S0907444907068072;
Michalska K., Borek D., Hernandez-Santoyo A., Jaskolski M.;
"Crystal packing of plant-type L-asparaginase from Escherichia coli.";
Acta Crystallogr. D 64:309-320(2008).
-!- FUNCTION: 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. {ECO:0000269|PubMed:11988085}.
-!- FUNCTION: May be involved in glutathione, and possibly other
peptide, transport, although these results could also be due to
polar effects of disruption. {ECO:0000269|PubMed:11988085}.
-!- CATALYTIC ACTIVITY: Cleavage of a beta-linked Asp residue from the
N-terminus of a polypeptide.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.138 mM for beta-L-Asp-L-Leu {ECO:0000269|PubMed:15265041};
KM=3.9 mM for L-Asn {ECO:0000269|PubMed:15265041};
Note=No activity for GlcNAc-Asn, Gly-L-Asn, L-Asp, L-Asn-alpha-
amide, L-Gln, aspartylglucosamides alpha- or gamma-aspartyl
dipeptides.;
-!- SUBUNIT: Heterotetramer of two alpha and two beta chains arranged
as a dimer of alpha/beta heterodimers.
{ECO:0000269|PubMed:11053866, ECO:0000269|PubMed:11988085,
ECO:0000269|PubMed:15159592, ECO:0000269|PubMed:15946951}.
-!- INDUCTION: Repressed by cysteine, an effect that is attributed to
CysB.
-!- PTM: 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.
-!- PTM: 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 Zn(2+).
-!- MASS SPECTROMETRY: Mass=17091; Method=Electrospray; Range=2-161;
Note=Subunit alpha.; Evidence={ECO:0000269|PubMed:15265041};
-!- MASS SPECTROMETRY: Mass=13852; Method=Electrospray; Range=179-315;
Note=Subunit beta.; Evidence={ECO:0000269|PubMed:15265041};
-!- SIMILARITY: Belongs to the Ntn-hydrolase family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; U00096; AAC73915.1; -; Genomic_DNA.
EMBL; AP009048; BAA35516.1; -; Genomic_DNA.
EMBL; M21151; -; NOT_ANNOTATED_CDS; Genomic_DNA.
PIR; D64820; D64820.
RefSeq; NP_415349.1; NC_000913.3.
RefSeq; WP_000513781.1; NZ_LN832404.1.
PDB; 1JN9; X-ray; 2.30 A; A/C=2-178, B/D=179-321.
PDB; 1K2X; X-ray; 1.65 A; A/C=2-178, B/D=179-321.
PDB; 1T3M; X-ray; 1.65 A; A/C=2-178, B/D=179-321.
PDB; 2ZAK; X-ray; 2.01 A; A/B=2-321.
PDB; 2ZAL; X-ray; 1.90 A; A/C=2-161, B/D=179-315.
PDB; 3C17; X-ray; 1.95 A; A/B=2-321.
PDBsum; 1JN9; -.
PDBsum; 1K2X; -.
PDBsum; 1T3M; -.
PDBsum; 2ZAK; -.
PDBsum; 2ZAL; -.
PDBsum; 3C17; -.
ProteinModelPortal; P37595; -.
SMR; P37595; -.
BioGrid; 4259980; 8.
IntAct; P37595; 9.
STRING; 316385.ECDH10B_0897; -.
MEROPS; T02.002; -.
PaxDb; P37595; -.
PRIDE; P37595; -.
EnsemblBacteria; AAC73915; AAC73915; b0828.
EnsemblBacteria; BAA35516; BAA35516; BAA35516.
GeneID; 945456; -.
KEGG; ecj:JW0812; -.
KEGG; eco:b0828; -.
PATRIC; fig|1411691.4.peg.1450; -.
EchoBASE; EB2307; -.
EcoGene; EG12407; iaaA.
eggNOG; ENOG4105D44; Bacteria.
eggNOG; COG1446; LUCA.
HOGENOM; HOG000174613; -.
InParanoid; P37595; -.
KO; K13051; -.
OMA; GITGKWP; -.
PhylomeDB; P37595; -.
BioCyc; EcoCyc:EG12407-MONOMER; -.
BioCyc; MetaCyc:EG12407-MONOMER; -.
BRENDA; 3.4.19.5; 2026.
BRENDA; 3.5.1.1; 2026.
SABIO-RK; P37595; -.
EvolutionaryTrace; P37595; -.
PRO; PR:P37595; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0004067; F:asparaginase activity; IDA:EcoCyc.
GO; GO:0008798; F:beta-aspartyl-peptidase activity; IDA:EcoCyc.
GO; GO:0016787; F:hydrolase activity; IDA:EcoliWiki.
GO; GO:0016540; P:protein autoprocessing; IMP:EcoCyc.
InterPro; IPR029055; Ntn_hydrolases_N.
InterPro; IPR000246; Peptidase_T2.
PANTHER; PTHR10188; PTHR10188; 2.
Pfam; PF01112; Asparaginase_2; 1.
SUPFAM; SSF56235; SSF56235; 1.
1: Evidence at protein level;
3D-structure; Autocatalytic cleavage; Complete proteome;
Direct protein sequencing; Hydrolase; Protease; Reference proteome.
INIT_MET 1 1 Removed.
CHAIN 2 178 Isoaspartyl peptidase subunit alpha.
/FTId=PRO_0000002349.
CHAIN 179 321 Isoaspartyl peptidase subunit beta.
/FTId=PRO_0000329014.
REGION 207 210 Substrate binding. {ECO:0000244|PDB:2ZAL,
ECO:0000269|PubMed:15946951}.
REGION 230 233 Substrate binding. {ECO:0000244|PDB:2ZAL,
ECO:0000269|PubMed:15946951}.
ACT_SITE 179 179 Nucleophile.
{ECO:0000305|PubMed:18323626}.
SITE 178 179 Cleavage; by autolysis.
{ECO:0000269|PubMed:11988085}.
MUTAGEN 179 179 T->A: Catalytically inactive.
{ECO:0000305|PubMed:18323626}.
STRAND 5 13 {ECO:0000244|PDB:1K2X}.
HELIX 17 19 {ECO:0000244|PDB:1K2X}.
HELIX 22 44 {ECO:0000244|PDB:1K2X}.
HELIX 49 62 {ECO:0000244|PDB:1K2X}.
STRAND 66 69 {ECO:0000244|PDB:1K2X}.
STRAND 82 88 {ECO:0000244|PDB:1K2X}.
TURN 89 91 {ECO:0000244|PDB:1K2X}.
STRAND 94 102 {ECO:0000244|PDB:1K2X}.
HELIX 106 116 {ECO:0000244|PDB:1K2X}.
STRAND 120 123 {ECO:0000244|PDB:1K2X}.
HELIX 124 132 {ECO:0000244|PDB:1K2X}.
TURN 133 135 {ECO:0000244|PDB:1K2X}.
HELIX 141 144 {ECO:0000244|PDB:1K2X}.
HELIX 147 156 {ECO:0000244|PDB:1K2X}.
STRAND 170 172 {ECO:0000244|PDB:3C17}.
TURN 174 176 {ECO:0000244|PDB:3C17}.
STRAND 180 185 {ECO:0000244|PDB:1K2X}.
STRAND 191 197 {ECO:0000244|PDB:1K2X}.
TURN 214 216 {ECO:0000244|PDB:1K2X}.
STRAND 217 220 {ECO:0000244|PDB:1K2X}.
STRAND 224 231 {ECO:0000244|PDB:1K2X}.
HELIX 233 238 {ECO:0000244|PDB:1K2X}.
HELIX 241 250 {ECO:0000244|PDB:1K2X}.
HELIX 256 265 {ECO:0000244|PDB:1K2X}.
HELIX 267 270 {ECO:0000244|PDB:1K2X}.
STRAND 275 281 {ECO:0000244|PDB:1K2X}.
STRAND 290 301 {ECO:0000244|PDB:1K2X}.
STRAND 307 311 {ECO:0000244|PDB:1K2X}.
SEQUENCE 321 AA; 33394 MW; 85C6D5377DA0B84D CRC64;
MGKAVIAIHG GAGAISRAQM SLQQELRYIE ALSAIVETGQ KMLEAGESAL DVVTEAVRLL
EECPLFNAGI GAVFTRDETH ELDACVMDGN TLKAGAVAGV SHLRNPVLAA RLVMEQSPHV
MMIGEGAENF AFARGMERVS PEIFSTSLRY EQLLAARKEG ATVLDHSGAP LDEKQKMGTV
GAVALDLDGN LAAATSTGGM TNKLPGRVGD SPLVGAGCYA NNASVAVSCT GTGEVFIRAL
AAYDIAALMD YGGLSLAEAC ERVVMEKLPA LGGSGGLIAI DHEGNVALPF NTEGMYRAWG
YAGDTPTTGI YREKGDTVAT Q


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