ASPG_MYCBO
ID ASPG_MYCBO Reviewed; 315 AA.
AC P63628; A0A1R3XYM6; Q10759; X2BIG6;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 90.
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=BQ2027_MB1565C;
OS Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=233413;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT "The complete genome sequence of Mycobacterium bovis.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA Robbe-Austerman S., Gordon S.V.;
RT "Updated reference genome sequence and annotation of Mycobacterium bovis
RT AF2122/97.";
RL Genome Announc. 5:E00157-E00157(2017).
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=SIU00168.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; LT708304; SIU00168.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_855217.1; NC_002945.3.
DR AlphaFoldDB; P63628; -.
DR SMR; P63628; -.
DR EnsemblBacteria; SIU00168; SIU00168; BQ2027_MB1565C.
DR PATRIC; fig|233413.5.peg.1711; -.
DR Proteomes; UP000001419; 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_0000171085"
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
