ASGX_SYNY3
ID ASGX_SYNY3 Reviewed; 329 AA.
AC P74383;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Isoaspartyl peptidase/L-asparaginase;
DE EC=3.4.19.5;
DE AltName: Full=Beta-aspartyl-peptidase;
DE AltName: Full=Isoaspartyl dipeptidase;
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;
GN OrderedLocusNames=sll0422;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP PROTEIN SEQUENCE OF 173-179, FUNCTION, SUBUNIT, AND AUTOCATALYTIC CLEAVAGE.
RX PubMed=11988085; DOI=10.1042/bj3640129;
RA Hejazi M., Piotukh K., Mattow J., Deutzmann R., Volkmer-Engert R.,
RA Lockau W.;
RT "Isoaspartyl dipeptidase activity of plant-type asparaginases.";
RL Biochem. J. 364:129-136(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
RN [3]
RP PROTEIN SEQUENCE OF 1-14 AND 173-189.
RX PubMed=9298645; DOI=10.1002/elps.1150180806;
RA Sazuka T., Ohara O.;
RT "Towards a proteome project of cyanobacterium Synechocystis sp. strain
RT PCC6803: linking 130 protein spots with their respective genes.";
RL Electrophoresis 18:1252-1258(1997).
CC -!- FUNCTION: Degrades proteins damaged by L-isoaspartyl residue formation
CC (also known as beta-Asp residues). Probably performs the final step in
CC the degradation of the reserve polymer cyanophycin (depolymerizes the
CC building block L-beta-Asp-Arg). Also has L-asparaginase activity.
CC {ECO:0000269|PubMed:11988085}.
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=0.66 mM for L-Asn;
CC KM=1.0 mM for L-beta-Asp-Ala;
CC KM=0.32 mM for L-beta-Asp-Arg;
CC KM=1.6 mM for L-beta-Asp-Gly;
CC KM=0.33 mM for L-beta-Asp-Leu;
CC KM=0.55 mM for L-beta-Asp-Lys;
CC KM=0.56 mM for L-beta-Asp-Phe;
CC Vmax=1.6 umol/min/mg enzyme with L-Asn as substrate;
CC Vmax=7.3 umol/min/mg enzyme with L-beta-Asp-Ala as substrate;
CC Vmax=21.0 umol/min/mg enzyme with L-beta-Asp-Arg as substrate;
CC Vmax=2.4 umol/min/mg enzyme with L-beta-Asp-Gly as substrate;
CC Vmax=14.7 umol/min/mg enzyme with L-beta-Asp-Leu as substrate;
CC Vmax=29.4 umol/min/mg enzyme with L-beta-Asp-Lys as substrate;
CC Vmax=23.6 umol/min/mg enzyme with L-beta-Asp-Phe as substrate;
CC Note=Enzyme is inactive on alpha-aspartyl dipeptides.;
CC -!- SUBUNIT: Heterotetramer of two alpha and two beta chains arranged as a
CC dimer of alpha/beta heterodimers. {ECO:0000305|PubMed:11988085}.
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 -!- SIMILARITY: Belongs to the Ntn-hydrolase family. {ECO:0000305}.
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DR EMBL; BA000022; BAA18480.1; -; Genomic_DNA.
DR PIR; S76221; S76221.
DR AlphaFoldDB; P74383; -.
DR SMR; P74383; -.
DR STRING; 1148.1653567; -.
DR MEROPS; T02.002; -.
DR PaxDb; P74383; -.
DR EnsemblBacteria; BAA18480; BAA18480; BAA18480.
DR KEGG; syn:sll0422; -.
DR eggNOG; COG1446; Bacteria.
DR InParanoid; P74383; -.
DR OMA; YSRMRWK; -.
DR PhylomeDB; P74383; -.
DR SABIO-RK; P74383; -.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004067; F:asparaginase activity; IBA:GO_Central.
DR GO; GO:0008798; F:beta-aspartyl-peptidase activity; IBA:GO_Central.
DR GO; GO:0016540; P:protein autoprocessing; IBA:GO_Central.
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 Autocatalytic cleavage; Direct protein sequencing; Hydrolase; Protease;
KW Reference proteome.
FT CHAIN 1..172
FT /note="Isoaspartyl peptidase/L-asparaginase subunit alpha"
FT /id="PRO_0000184578"
FT CHAIN 173..329
FT /note="Isoaspartyl peptidase/L-asparaginase subunit beta"
FT /id="PRO_0000329015"
FT ACT_SITE 173
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 201..204
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 222..225
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 172..173
FT /note="Cleavage; by autolysis"
SQ SEQUENCE 329 AA; 34895 MW; EBD70950B7F684F5 CRC64;
MTPKLIIHGG ASSLDDKGGL ATVRQSLHQI VAAVYETLTA GGSAMDAVVQ GCELLENEPR
FNAGTGSVLQ SDGQVRMSAS LMDGDRQNFS GVINVSRIKN PIQMAQFLQG QTDRILSDYG
AADLAREMQL PIYDPATDFR IQEWMEERGE DVRKKMARLI ADPTVGIEAR KGTIGVVALD
ANGKIAAGTS TGGKGLERIG RVSDSAMPAG NYATRFAGVS CTGVGEDIIN ECLAAKVVIR
VKDGQNLAQA MAKSITEALE NNTDLGAIAL DHQGHIAWGK TCPVLLAAYH TGTAIGDTLE
LTDGDHYGNA SILKLQKTVK KIQTKTRGK
