ASGX_PYRFU
ID ASGX_PYRFU Reviewed; 306 AA.
AC Q8U4E6;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 85.
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=PF0142;
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
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; AE009950; AAL80266.1; -; Genomic_DNA.
DR RefSeq; WP_011011255.1; NZ_CP023154.1.
DR AlphaFoldDB; Q8U4E6; -.
DR SMR; Q8U4E6; -.
DR IntAct; Q8U4E6; 1.
DR MINT; Q8U4E6; -.
DR STRING; 186497.PF0142; -.
DR MEROPS; T02.002; -.
DR PRIDE; Q8U4E6; -.
DR EnsemblBacteria; AAL80266; AAL80266; PF0142.
DR GeneID; 41711932; -.
DR KEGG; pfu:PF0142; -.
DR PATRIC; fig|186497.12.peg.148; -.
DR eggNOG; arCOG04779; Archaea.
DR HOGENOM; CLU_021603_1_2_2; -.
DR OMA; YSRMRWK; -.
DR OrthoDB; 66502at2157; -.
DR PhylomeDB; Q8U4E6; -.
DR Proteomes; UP000001013; 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; Reference proteome.
FT CHAIN 1..175
FT /note="Putative L-asparaginase subunit alpha"
FT /id="PRO_0000184580"
FT CHAIN 176..306
FT /note="Putative L-asparaginase subunit beta"
FT /id="PRO_0000329017"
FT ACT_SITE 176
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 203..206
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 225..228
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 175..176
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000255"
SQ SEQUENCE 306 AA; 32855 MW; 68410D8FE6DE9EE2 CRC64;
MVAIIVHGGA GTIRKEERIP KIIEGVREAV LTGWRELKKG SALDAVEEAV KVLEDNPLFN
AGTGSVLTLD GKVEMDAAIM RGKTLDAGAV AGIWGVKNPI SVARKVMEKT DHVLLIGEGA
VKFARLMGFP EYDPTTEERR KQWEELRKKL LETGEIRHWK KLSELIKEYP EVLRSTVGAV
AFDGEEIVAG TSTGGVFLKM FGRVGDTPII GAGTYANEVA GASCTGLGEV AIKLSLAKTA
TDFVRLGLDA QAASEAAIRL ATKYFGPDTM GIIMVDSNGN VGFAKNTKHM SYAFMKEGMK
EPEAGV
