ID   ASGX_PYRHO              Reviewed;         305 AA.
AC   O57971;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 108.
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=PH0232;
OS   Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS   100139 / OT-3).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=70601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX   PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA   Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA   Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA   Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA   Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA   Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT   "Complete sequence and gene organization of the genome of a hyper-
RT   thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL   DNA Res. 5:55-76(1998).
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; BA000001; BAA29304.1; -; Genomic_DNA.
DR   PIR; A71247; A71247.
DR   RefSeq; WP_010884335.1; NC_000961.1.
DR   AlphaFoldDB; O57971; -.
DR   SMR; O57971; -.
DR   STRING; 70601.3256621; -.
DR   MEROPS; T02.002; -.
DR   EnsemblBacteria; BAA29304; BAA29304; BAA29304.
DR   GeneID; 1444122; -.
DR   KEGG; pho:PH0232; -.
DR   eggNOG; arCOG04779; Archaea.
DR   OMA; YSRMRWK; -.
DR   OrthoDB; 66502at2157; -.
DR   Proteomes; UP000000752; Chromosome.
DR   GO; GO:0004067; F:asparaginase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
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.
FT   CHAIN           1..174
FT                   /note="Putative L-asparaginase subunit alpha"
FT                   /id="PRO_0000184581"
FT   CHAIN           175..305
FT                   /note="Putative L-asparaginase subunit beta"
FT                   /id="PRO_0000329018"
FT   ACT_SITE        175
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   BINDING         202..205
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         224..227
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            174..175
FT                   /note="Cleavage; by autolysis"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   305 AA;  32543 MW;  C5391CAB69D48E03 CRC64;
     MVAIIVHGGA GTIKKEERIP KVIEGVKEAV IVGWKELRKG SALDAVEEAI KVLEDNPIFN
     AGTGSVLTID GKVEMDAAIM RGKTLEAGAV AGIWGVKNPI SVARKVMEKT DHVLLVGEGA
     VKFARLMGFP EYNPITEERI EQWKELKEKL MKGEIKYWKK LGELIKEYPE VLRSTVGAVA
     FDGEEIVAGT STGGVFLKMF GRVGDTPIIG AGTYANEVAG ASCTGLGEVA IRLALAKTAT
     DFVRLGMDAQ AASNAAISLA TKYFGKDTMG IIMVDAAGNV GFAKNTKHMS YAYMKDGMEE
     PEAGV