ID   ASGX_PYRAB              Reviewed;         305 AA.
AC   Q9V262; G8ZG47;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 107.
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=PYRAB02120; ORFNames=PAB0145;
OS   Pyrococcus abyssi (strain GE5 / Orsay).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=272844;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GE5 / Orsay;
RX   PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA   Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA   Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA   Weissenbach J., Zivanovic Y., Forterre P.;
RT   "An integrated analysis of the genome of the hyperthermophilic archaeon
RT   Pyrococcus abyssi.";
RL   Mol. Microbiol. 47:1495-1512(2003).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=GE5 / Orsay;
RX   PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA   Gao J., Wang J.;
RT   "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT   Pyrococcus furiosus DSM 3638.";
RL   Curr. Microbiol. 64:118-129(2012).
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; AJ248283; CAB49136.1; -; Genomic_DNA.
DR   EMBL; HE613800; CCE69588.1; -; Genomic_DNA.
DR   PIR; A75211; A75211.
DR   RefSeq; WP_010867336.1; NC_000868.1.
DR   AlphaFoldDB; Q9V262; -.
DR   SMR; Q9V262; -.
DR   STRING; 272844.PAB0145; -.
DR   MEROPS; T02.002; -.
DR   PRIDE; Q9V262; -.
DR   EnsemblBacteria; CAB49136; CAB49136; PAB0145.
DR   GeneID; 1495101; -.
DR   KEGG; pab:PAB0145; -.
DR   PATRIC; fig|272844.11.peg.228; -.
DR   eggNOG; arCOG04779; Archaea.
DR   HOGENOM; CLU_021603_1_2_2; -.
DR   OMA; YSRMRWK; -.
DR   OrthoDB; 66502at2157; -.
DR   PhylomeDB; Q9V262; -.
DR   Proteomes; UP000000810; Chromosome.
DR   Proteomes; UP000009139; 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_0000184579"
FT   CHAIN           175..305
FT                   /note="Putative L-asparaginase subunit beta"
FT                   /id="PRO_0000329016"
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;  32591 MW;  5B2A1DE8F6FB2F7B CRC64;
     MVAIIVHGGA GTIRKEERIP KVLEGVREAV LAGWKELKKG SALDAVEEAI KVLEDNPIFN
     AGTGSVLTID GKVEMDAAIM RGKTLEAGAV AGIWGVKNPI SVARKVMEKT DHVLLVGEGA
     VKFARIMGFP EYDPTTEERR KQWQELKEKL MKGEVRHWKK LGELIKEHPE VLRSTVGAVA
     FDGEEVVAGT STGGVFLKMF GRVGDTPIIG AGTYANEVAG ASCTGLGEVA IKLALAKTAT
     DFVRLGLDAQ AASEAAIELA TKHFGKDTMG IIMVDSRGNV GFAKNTKHMS YAFMKEGMNE
     PEAGV