ID   ASPG_HELPY              Reviewed;         330 AA.
AC   O25424;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Probable L-asparaginase;
DE            Short=L-ASNase;
DE            EC=3.5.1.1;
DE   AltName: Full=L-asparagine amidohydrolase;
GN   Name=ansA; Synonyms=asn; OrderedLocusNames=HP_0723;
OS   Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=85962;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700392 / 26695;
RX   PubMed=9252185; DOI=10.1038/41483;
RA   Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA   Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA   Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA   Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA   McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA   Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA   Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA   Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT   "The complete genome sequence of the gastric pathogen Helicobacter
RT   pylori.";
RL   Nature 388:539-547(1997).
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the asparaginase 1 family. {ECO:0000305}.
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DR   EMBL; AE000511; AAD07772.1; -; Genomic_DNA.
DR   PIR; C64610; C64610.
DR   RefSeq; NP_207517.1; NC_000915.1.
DR   AlphaFoldDB; O25424; -.
DR   SMR; O25424; -.
DR   DIP; DIP-3115N; -.
DR   IntAct; O25424; 1.
DR   MINT; O25424; -.
DR   STRING; 85962.C694_03720; -.
DR   PaxDb; O25424; -.
DR   EnsemblBacteria; AAD07772; AAD07772; HP_0723.
DR   KEGG; hpy:HP_0723; -.
DR   PATRIC; fig|85962.47.peg.772; -.
DR   eggNOG; COG0252; Bacteria.
DR   OMA; RKNHTSR; -.
DR   PhylomeDB; O25424; -.
DR   Proteomes; UP000000429; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004067; F:asparaginase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006528; P:asparagine metabolic process; IEA:InterPro.
DR   CDD; cd08964; L-asparaginase_II; 1.
DR   Gene3D; 3.40.50.1170; -; 1.
DR   Gene3D; 3.40.50.40; -; 1.
DR   InterPro; IPR004550; AsnASE_II.
DR   InterPro; IPR036152; Asp/glu_Ase-like_sf.
DR   InterPro; IPR006034; Asparaginase/glutaminase-like.
DR   InterPro; IPR020827; Asparaginase/glutaminase_AS1.
DR   InterPro; IPR027475; Asparaginase/glutaminase_AS2.
DR   InterPro; IPR040919; Asparaginase_C.
DR   InterPro; IPR027473; L-asparaginase_C.
DR   InterPro; IPR027474; L-asparaginase_N.
DR   InterPro; IPR037152; L-asparaginase_N_sf.
DR   Pfam; PF00710; Asparaginase; 1.
DR   Pfam; PF17763; Asparaginase_C; 1.
DR   PIRSF; PIRSF001220; L-ASNase_gatD; 1.
DR   PRINTS; PR00139; ASNGLNASE.
DR   SMART; SM00870; Asparaginase; 1.
DR   SUPFAM; SSF53774; SSF53774; 1.
DR   TIGRFAMs; TIGR00520; asnASE_II; 1.
DR   PROSITE; PS00144; ASN_GLN_ASE_1; 1.
DR   PROSITE; PS00917; ASN_GLN_ASE_2; 1.
DR   PROSITE; PS51732; ASN_GLN_ASE_3; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Hydrolase; Reference proteome.
FT   CHAIN           1..330
FT                   /note="Probable L-asparaginase"
FT                   /id="PRO_0000171081"
FT   DOMAIN          6..330
FT                   /note="Asparaginase/glutaminase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01068"
FT   ACT_SITE        16
FT                   /note="O-isoaspartyl threonine intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10099,
FT                   ECO:0000255|PROSITE-ProRule:PRU10100"
FT   BINDING         62
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         95..96
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   330 AA;  35539 MW;  9A2BB6DC7ED9D7DB CRC64;
     MAQNLPTIAL LATGGTIAGS GASASLGSYK SGELGIKELL KAIPSLNRLA RIQGEQISNI
     GSQDMNEEVW FKLAKRAQEL LDDSRIQGVV ITHGTDTLEE SAYFLNLVLR STKPVVLVGA
     MRNAASLSAD GALNLYNAVS VALNEKSANK GVLVVMDDNI FSAREVIKTH TTHTSTFKAL
     NSGAIGSVYY GKTRYYMQPL RKHTTESEFS LSQLKTPLPK VDIIYTHAGM TPDLFQASLN
     SHAKGVVIAG VGNGNVSAGF LKAMQEASQM GVVIVRSSRV NSGEITSGEI DDKAFITSDN
     LNPQKARVLL QLALTKTNNK EKIQEMFEEY