ASPG_LUPLU
ID ASPG_LUPLU Reviewed; 325 AA.
AC Q9ZSD6;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Isoaspartyl peptidase/L-asparaginase;
DE Short=LlA;
DE EC=3.4.19.5;
DE AltName: Full=L-asparagine amidohydrolase;
DE AltName: Full=Potassium-independent L-asparaginase;
DE Contains:
DE RecName: Full=Isoaspartyl peptidase/L-asparaginase subunit alpha;
DE Contains:
DE RecName: Full=Isoaspartyl peptidase/L-asparaginase subunit beta;
DE Flags: Precursor;
OS Lupinus luteus (European yellow lupine).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC genistoids sensu lato; core genistoids; Genisteae; Lupinus.
OX NCBI_TaxID=3873;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Ventus; TISSUE=Root;
RA Borek D., Podkowinski J., Kisiel A., Jaskolski M.;
RT "Isolation and characterization of cDNA encoding L-asparaginase from
RT Lupinus luteus.";
RL (er) Plant Gene Register PGR99-050(1999).
RN [2]
RP AUTOCATALYTIC CLEAVAGE, SUBUNIT, KINETIC PARAMETERS, AND MASS SPECTROMETRY.
RX PubMed=15265041; DOI=10.1111/j.1432-1033.2004.04254.x;
RA Borek D., Michalska K., Brzezinski K., Kisiel A., Podkowinski J.,
RA Bonthron D.T., Krowarsch D., Otlewski J., Jaskolski M.;
RT "Expression, purification and catalytic activity of Lupinus luteus
RT asparagine beta-amidohydrolase and its Escherichia coli homolog.";
RL Eur. J. Biochem. 271:3215-3226(2004).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
RX PubMed=16725155; DOI=10.1016/j.jmb.2006.04.066;
RA Michalska K., Bujacz G., Jaskolski M.;
RT "Crystal structure of plant asparaginase.";
RL J. Mol. Biol. 360:105-116(2006).
CC -!- FUNCTION: Degrades proteins damaged by L-isoaspartyl residue formation
CC (also known as beta-Asp residues). Also has L-asparaginase activity,
CC which is used to liberate stored nitrogen during seed development.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleavage of a beta-linked Asp residue from the N-terminus of a
CC polypeptide.; EC=3.4.19.5;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.136 mM for beta-L-Asp-L-Leu {ECO:0000269|PubMed:15265041};
CC KM=4.8 mM for L-Asn {ECO:0000269|PubMed:15265041};
CC Note=No activity for GlcNAc-Asn, Gly-L-Asn, L-Asp, L-Asn-alpha-amide,
CC L-Gln or aspartylglucosamides.;
CC -!- SUBUNIT: Heterotetramer of two alpha and two beta chains arranged as a
CC dimer of alpha/beta heterodimers. {ECO:0000269|PubMed:15265041}.
CC -!- TISSUE SPECIFICITY: Expressed in ripening seeds and developing nodules.
CC -!- PTM: Cleaved into an alpha and beta chain by autocatalysis; this
CC activates the enzyme. The N-terminal residue of the beta subunit is
CC responsible for the nucleophile hydrolase activity.
CC -!- MASS SPECTROMETRY: [Isoaspartyl peptidase/L-asparaginase subunit
CC alpha]: Mass=22983; Method=Electrospray; Note=Subunit alpha
CC overexpressed as a His-tagged protein where the His tag has the mass
CC 2050.; Evidence={ECO:0000269|PubMed:15265041};
CC -!- MASS SPECTROMETRY: [Isoaspartyl peptidase/L-asparaginase subunit beta]:
CC Mass=13605; Method=Electrospray; Note=Subunit beta.;
CC Evidence={ECO:0000269|PubMed:15265041};
CC -!- SIMILARITY: Belongs to the Ntn-hydrolase family. {ECO:0000305}.
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DR EMBL; AF112444; AAD03742.1; -; mRNA.
DR PDB; 2GEZ; X-ray; 2.60 A; A/C/E/G=1-192, B/D/F/H=193-325.
DR PDBsum; 2GEZ; -.
DR AlphaFoldDB; Q9ZSD6; -.
DR SMR; Q9ZSD6; -.
DR MEROPS; T02.A01; -.
DR BRENDA; 3.4.19.5; 3093.
DR SABIO-RK; Q9ZSD6; -.
DR EvolutionaryTrace; Q9ZSD6; -.
DR GO; GO:0008798; F:beta-aspartyl-peptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR000246; Peptidase_T2.
DR PANTHER; PTHR10188; PTHR10188; 1.
DR Pfam; PF01112; Asparaginase_2; 1.
DR SUPFAM; SSF56235; SSF56235; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Autocatalytic cleavage; Hydrolase; Protease.
FT CHAIN 1..192
FT /note="Isoaspartyl peptidase/L-asparaginase subunit alpha"
FT /id="PRO_0000045456"
FT CHAIN 193..325
FT /note="Isoaspartyl peptidase/L-asparaginase subunit beta"
FT /id="PRO_0000045457"
FT ACT_SITE 193
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 221..224
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 243..246
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 192..193
FT /note="Cleavage; by autolysis"
FT STRAND 5..13
FT /evidence="ECO:0007829|PDB:2GEZ"
FT HELIX 21..43
FT /evidence="ECO:0007829|PDB:2GEZ"
FT HELIX 48..61
FT /evidence="ECO:0007829|PDB:2GEZ"
FT STRAND 65..68
FT /evidence="ECO:0007829|PDB:2GEZ"
FT STRAND 81..87
FT /evidence="ECO:0007829|PDB:2GEZ"
FT TURN 88..91
FT /evidence="ECO:0007829|PDB:2GEZ"
FT STRAND 92..103
FT /evidence="ECO:0007829|PDB:2GEZ"
FT HELIX 105..115
FT /evidence="ECO:0007829|PDB:2GEZ"
FT STRAND 119..122
FT /evidence="ECO:0007829|PDB:2GEZ"
FT HELIX 123..133
FT /evidence="ECO:0007829|PDB:2GEZ"
FT HELIX 140..143
FT /evidence="ECO:0007829|PDB:2GEZ"
FT HELIX 146..158
FT /evidence="ECO:0007829|PDB:2GEZ"
FT STRAND 194..199
FT /evidence="ECO:0007829|PDB:2GEZ"
FT STRAND 205..211
FT /evidence="ECO:0007829|PDB:2GEZ"
FT TURN 229..231
FT /evidence="ECO:0007829|PDB:2GEZ"
FT STRAND 232..234
FT /evidence="ECO:0007829|PDB:2GEZ"
FT STRAND 236..244
FT /evidence="ECO:0007829|PDB:2GEZ"
FT HELIX 246..251
FT /evidence="ECO:0007829|PDB:2GEZ"
FT HELIX 254..265
FT /evidence="ECO:0007829|PDB:2GEZ"
FT HELIX 269..278
FT /evidence="ECO:0007829|PDB:2GEZ"
FT STRAND 285..292
FT /evidence="ECO:0007829|PDB:2GEZ"
FT STRAND 301..312
FT /evidence="ECO:0007829|PDB:2GEZ"
FT STRAND 317..322
FT /evidence="ECO:0007829|PDB:2GEZ"
SQ SEQUENCE 325 AA; 34449 MW; 52949AA1765B7892 CRC64;
MGGWSIALHG GAGDIPFSLP PERRKPREEG LRHCLQIGVE ALKAQKPPLD VVELVVRELE
NIEHFNAGIG SVLTNSGTVE MEASIMDGNT MKCGAVSGLS TVLNPISLAR LVMDKTPHIY
LAFQGAQDFA KQQGVETVDS SHLITAENVE RLKLAIEANR VQVDYSQYNY PEPVKDDAEK
ELPLTNGDSQ IGTVGCVAVD SHGNLASATS TGGLVNKMVG RIGDTPLIGA GTYANELCAV
SATGKGEEII RATVARDVAA LMEFKGLSLK EAADFVIHER TPKGTVGLIA VSAAGEIAMP
FNTTGMFRAC ATEDGYSEIA IWPTT
