ASPG_HELPJ
ID ASPG_HELPJ Reviewed; 332 AA.
AC Q9ZLB9;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 116.
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=jhp_0661;
OS Helicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J99 / ATCC 700824;
RX PubMed=9923682; DOI=10.1038/16495;
RA Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C.,
RA Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J.,
RA Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D.,
RA Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.;
RT "Genomic sequence comparison of two unrelated isolates of the human gastric
RT pathogen Helicobacter pylori.";
RL Nature 397:176-180(1999).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS).
RX PubMed=19966411; DOI=10.1107/s0907444909038244;
RA Dhavala P., Papageorgiou A.C.;
RT "Structure of Helicobacter pylori L-asparaginase at 1.4 A resolution.";
RL Acta Crystallogr. D 65:1253-1261(2009).
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; AE001439; AAD06238.1; -; Genomic_DNA.
DR PIR; D71904; D71904.
DR PDB; 2WLT; X-ray; 1.40 A; A=1-332.
DR PDB; 2WT4; X-ray; 1.80 A; A=1-332.
DR PDBsum; 2WLT; -.
DR PDBsum; 2WT4; -.
DR AlphaFoldDB; Q9ZLB9; -.
DR SMR; Q9ZLB9; -.
DR STRING; 85963.jhp_0661; -.
DR EnsemblBacteria; AAD06238; AAD06238; jhp_0661.
DR KEGG; hpj:jhp_0661; -.
DR eggNOG; COG0252; Bacteria.
DR OMA; RKNHTSR; -.
DR BRENDA; 3.5.1.1; 11068.
DR EvolutionaryTrace; Q9ZLB9; -.
DR Proteomes; UP000000804; 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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Hydrolase.
FT CHAIN 1..332
FT /note="Probable L-asparaginase"
FT /id="PRO_0000171082"
FT DOMAIN 6..332
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"
FT STRAND 7..15
FT /evidence="ECO:0007829|PDB:2WLT"
FT HELIX 16..18
FT /evidence="ECO:0007829|PDB:2WLT"
FT HELIX 38..41
FT /evidence="ECO:0007829|PDB:2WLT"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:2WLT"
FT STRAND 51..60
FT /evidence="ECO:0007829|PDB:2WLT"
FT HELIX 62..64
FT /evidence="ECO:0007829|PDB:2WLT"
FT HELIX 67..81
FT /evidence="ECO:0007829|PDB:2WLT"
FT STRAND 88..92
FT /evidence="ECO:0007829|PDB:2WLT"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:2WLT"
FT HELIX 98..108
FT /evidence="ECO:0007829|PDB:2WLT"
FT STRAND 115..118
FT /evidence="ECO:0007829|PDB:2WLT"
FT HELIX 131..143
FT /evidence="ECO:0007829|PDB:2WLT"
FT HELIX 145..147
FT /evidence="ECO:0007829|PDB:2WLT"
FT STRAND 152..156
FT /evidence="ECO:0007829|PDB:2WLT"
FT STRAND 159..162
FT /evidence="ECO:0007829|PDB:2WLT"
FT TURN 163..165
FT /evidence="ECO:0007829|PDB:2WLT"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:2WLT"
FT TURN 180..182
FT /evidence="ECO:0007829|PDB:2WLT"
FT STRAND 185..189
FT /evidence="ECO:0007829|PDB:2WLT"
FT STRAND 192..195
FT /evidence="ECO:0007829|PDB:2WLT"
FT HELIX 204..206
FT /evidence="ECO:0007829|PDB:2WLT"
FT HELIX 211..213
FT /evidence="ECO:0007829|PDB:2WLT"
FT STRAND 221..225
FT /evidence="ECO:0007829|PDB:2WLT"
FT HELIX 233..240
FT /evidence="ECO:0007829|PDB:2WLT"
FT STRAND 244..251
FT /evidence="ECO:0007829|PDB:2WLT"
FT TURN 252..254
FT /evidence="ECO:0007829|PDB:2WLT"
FT HELIX 258..269
FT /evidence="ECO:0007829|PDB:2WLT"
FT STRAND 273..283
FT /evidence="ECO:0007829|PDB:2WLT"
FT STRAND 287..290
FT /evidence="ECO:0007829|PDB:2WLT"
FT HELIX 292..295
FT /evidence="ECO:0007829|PDB:2WLT"
FT HELIX 305..318
FT /evidence="ECO:0007829|PDB:2WLT"
FT HELIX 322..331
FT /evidence="ECO:0007829|PDB:2WLT"
SQ SEQUENCE 332 AA; 35687 MW; 1C6FB0C7D4FC3095 CRC64;
MAQNLPTIAL LATGGTIAGS GVDASLGSYK SGELGVKELL KAIPSLNKIA RIQGEQVSNI
GSQDMNEEIW FKLAQRAQEL LDDSRIQGVV ITHGTDTLEE SAYFLNLVLH STKPVVLVGA
MRNASSLSAD GALNLYYAVS VAVNEKSANK GVLVVMDDTI FRVREVVKTH TTHISTFKAL
NSGAIGSVYY GKTRYYMQPL RKHTTESEFS LSQLKTPLPK VDIIYTHAGM TPDLFQASLN
SHAKGVVIAG VGNGNVSAGF LKAMQEASQM GVVIVRSSRV GSGGVTSGEI DDKAYGFITS
DNLNPQKARV LLQLALTKTN DKAKIQEMFE EY
