ASPG_BACLI
ID ASPG_BACLI Reviewed; 322 AA.
AC P30363;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=L-asparaginase;
DE Short=L-ASNase;
DE EC=3.5.1.1;
DE AltName: Full=L-asparagine amidohydrolase;
GN Name=ansA;
OS Bacillus licheniformis.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1402;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1916233; DOI=10.1016/0378-1097(91)90239-7;
RA van Dijl J.M., de Jong A., Smith H., Bron S., Venema G.;
RT "Lack of specific hybridization between the lep genes of Salmonella
RT typhimurium and Bacillus licheniformis.";
RL FEMS Microbiol. Lett. 65:345-351(1991).
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: Homotetramer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the asparaginase 1 family. {ECO:0000305}.
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DR EMBL; Z11497; CAA77574.1; -; Genomic_DNA.
DR PIR; S18999; S18999.
DR AlphaFoldDB; P30363; -.
DR SMR; P30363; -.
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 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.
FT CHAIN 1..322
FT /note="L-asparaginase"
FT /id="PRO_0000171076"
FT DOMAIN 3..322
FT /note="Asparaginase/glutaminase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01068"
FT ACT_SITE 13
FT /note="O-isoaspartyl threonine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10099,
FT ECO:0000255|PROSITE-ProRule:PRU10100"
FT BINDING 56
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 89..90
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 322 AA; 35442 MW; 7048BEC52D0B1DFB CRC64;
MNKKVALITT GGTIASRKTE SGRLAAGAIS GPELAEMCSL PEDVQIDVYP AFQLPSMHIT
FQHLLELKQT IERVFQDGGY DGAVVTHGTD TLEETAYFLD LTIEDERPVV VTGSQRAPEQ
QGTDAYTNIR HAVYTACSPD IKGAGTVVVF NERIFNARYV KKVHASNLQG FDVFGFGYLG
IIDNDKVYVY QKLLKRDVHQ LQRPLPAVDI VKCYLDGDGK FIRAAVREGV EGIVLEGVGR
GQVPPNMMAD IEQALNQGVY IVITTSAEEG EVYTTYDYAG SSYDLAKKGV ILGKDYDSKK
ARMKLAVLLA SYKEGIKDKF CY