ID   ASGX_THEKO              Reviewed;         306 AA.
AC   Q5JHT1;
DT   25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Putative L-asparaginase;
DE            EC=3.5.1.1;
DE   AltName: Full=L-asparagine amidohydrolase;
DE   Contains:
DE     RecName: Full=Putative L-asparaginase subunit alpha;
DE   Contains:
DE     RecName: Full=Putative L-asparaginase subunit beta;
DE   Flags: Precursor;
GN   OrderedLocusNames=TK2246;
OS   Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS   (Pyrococcus kodakaraensis (strain KOD1)).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=69014;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX   PubMed=15710748; DOI=10.1101/gr.3003105;
RA   Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT   "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT   kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL   Genome Res. 15:352-363(2005).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-asparagine = L-aspartate + NH4(+);
CC         Xref=Rhea:RHEA:21016, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:29991, ChEBI:CHEBI:58048; EC=3.5.1.1;
CC   -!- SUBUNIT: Heterodimer of an alpha and beta chain produced by
CC       autocleavage. This heterodimer may then dimerize in turn, giving rise
CC       to a heterotetramer (By similarity). {ECO:0000250}.
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 (By similarity).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the Ntn-hydrolase family. {ECO:0000305}.
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DR   EMBL; AP006878; BAD86435.1; -; Genomic_DNA.
DR   RefSeq; WP_011251196.1; NC_006624.1.
DR   AlphaFoldDB; Q5JHT1; -.
DR   SMR; Q5JHT1; -.
DR   STRING; 69014.TK2246; -.
DR   EnsemblBacteria; BAD86435; BAD86435; TK2246.
DR   GeneID; 3234510; -.
DR   KEGG; tko:TK2246; -.
DR   PATRIC; fig|69014.16.peg.2201; -.
DR   eggNOG; arCOG04779; Archaea.
DR   HOGENOM; CLU_021603_1_2_2; -.
DR   InParanoid; Q5JHT1; -.
DR   OMA; YSRMRWK; -.
DR   OrthoDB; 66502at2157; -.
DR   PhylomeDB; Q5JHT1; -.
DR   BRENDA; 3.5.1.1; 5246.
DR   Proteomes; UP000000536; 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: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   3: Inferred from homology;
KW   Autocatalytic cleavage; Hydrolase; Protease; Reference proteome.
FT   CHAIN           1..175
FT                   /note="Putative L-asparaginase subunit alpha"
FT                   /id="PRO_0000184582"
FT   CHAIN           176..306
FT                   /note="Putative L-asparaginase subunit beta"
FT                   /id="PRO_0000329019"
FT   ACT_SITE        176
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P37595"
FT   BINDING         203..206
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P37595"
FT   BINDING         225..228
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P37595"
FT   SITE            175..176
FT                   /note="Cleavage; by autolysis"
FT                   /evidence="ECO:0000250|UniProtKB:P37595"
SQ   SEQUENCE   306 AA;  32642 MW;  0290276B98DDC5F9 CRC64;
     MAAIIVHGGA GTIRKEERIP KVIEGVREAV LAGWRELKRG SALDAVEEAV KALEDNPIFN
     AGTGSVLTLD GKVEMDAAIM RGKTLDAGAV AGIWGVKNPI SVARKVMEKT DHVLLIGEGA
     VKFARLLGFE EYDPITEERL KQWEELRKKL IEKGETKHWK KLNELIKEYP EVLRSTVGAV
     AFDGEEVVAG TSTGGVFLKM FGRVGDTPII GGGTYANEVA GASCTGLGEV AIKLALAKSA
     ADFVRLGMDA QTASEAAISL ATKYFGPDTM GIIMVDAKGN VGFAKNTKHM SYAFMKDGMD
     EPEAGV