ID   ASPG_MYCTO              Reviewed;         315 AA.
AC   P9WPX4; L0T751; P63627; Q10759;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 33.
DE   RecName: Full=L-asparaginase {ECO:0000250|UniProtKB:P9WPX5};
DE            Short=L-ASNase {ECO:0000250|UniProtKB:P9WPX5};
DE            EC=3.5.1.1 {ECO:0000250|UniProtKB:P9WPX5};
DE   AltName: Full=L-asparagine amidohydrolase {ECO:0000250|UniProtKB:P9WPX5};
GN   Name=ansA; OrderedLocusNames=MT1590;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
CC   -!- FUNCTION: Has a dual function in both nitrogen assimilation and in
CC       protection against acid stress during infection through asparagine
CC       hydrolysis and NH4(+) release. Catalyzes asparagine hydrolysis.
CC       {ECO:0000250|UniProtKB:P9WPX5}.
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         Evidence={ECO:0000250|UniProtKB:P9WPX5};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P9WPX5}.
CC       Note=Probably secreted via the ESX-5 / type VII secretion system
CC       (T7SS). {ECO:0000250|UniProtKB:P9WPX5}.
CC   -!- SIMILARITY: Belongs to the asparaginase 1 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK45856.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AE000516; AAK45856.1; ALT_INIT; Genomic_DNA.
DR   PIR; G70760; G70760.
DR   AlphaFoldDB; P9WPX4; -.
DR   SMR; P9WPX4; -.
DR   EnsemblBacteria; AAK45856; AAK45856; MT1590.
DR   KEGG; mtc:MT1590; -.
DR   HOGENOM; CLU_019134_1_0_11; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0005576; C:extracellular region; 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   Hydrolase; Secreted.
FT   CHAIN           1..315
FT                   /note="L-asparaginase"
FT                   /id="PRO_0000426876"
FT   DOMAIN          2..315
FT                   /note="Asparaginase/glutaminase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01068"
FT   ACT_SITE        12
FT                   /note="O-isoaspartyl threonine intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P00805"
FT   BINDING         52..53
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00805"
FT   BINDING         84..85
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00805"
SQ   SEQUENCE   315 AA;  31741 MW;  AEC46476F73FA340 CRC64;
     MARLTVITTG GTISTTAGPD GVLRPTHCGA TLIAGLDMDS DIEVVDLMAL DSSKLTPADW
     DRIGAAVQEA FRGGADGVVI THGTDTLEET ALWLDLTYAG SRPVVLTGAM LSADAPGADG
     PANLRDALAV AADPAARDLG VLVSFGGRVL QPLGLHKVAN PDLCGFAGES LGFTSGGVRL
     TRTKTRPYLG DLGAAVAPRV DIVAVYPGSD AVAMDACVAA GARAVVLEAL GSGNAGAAVI
     EGVRRHCRDG SDPVVIAVST RVAGARVGAG YGPGHDLVEA GAVMVPRLPP SQARVLLMAA
     LAANSPVADV IDRWG