ASPG_MYCLE
ID ASPG_MYCLE Reviewed; 310 AA.
AC Q9X7E6;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 113.
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=ML1198; ORFNames=MLCB458.13c;
OS Mycobacterium leprae (strain TN).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=272631;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TN;
RX PubMed=11234002; DOI=10.1038/35059006;
RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA Barrell B.G.;
RT "Massive gene decay in the leprosy bacillus.";
RL Nature 409:1007-1011(2001).
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}.
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DR EMBL; AL049478; CAB39578.1; -; Genomic_DNA.
DR EMBL; AL583921; CAC31579.1; -; Genomic_DNA.
DR PIR; H87058; H87058.
DR RefSeq; NP_301872.1; NC_002677.1.
DR RefSeq; WP_010908193.1; NC_002677.1.
DR AlphaFoldDB; Q9X7E6; -.
DR SMR; Q9X7E6; -.
DR STRING; 272631.ML1198; -.
DR EnsemblBacteria; CAC31579; CAC31579; CAC31579.
DR KEGG; mle:ML1198; -.
DR PATRIC; fig|272631.5.peg.2200; -.
DR Leproma; ML1198; -.
DR eggNOG; COG0252; Bacteria.
DR HOGENOM; CLU_019134_1_0_11; -.
DR OMA; RKNHTSR; -.
DR Proteomes; UP000000806; 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; Reference proteome; Secreted.
FT CHAIN 1..310
FT /note="L-asparaginase"
FT /id="PRO_0000171083"
FT DOMAIN 2..310
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 50..51
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00805"
FT BINDING 82..83
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00805"
SQ SEQUENCE 310 AA; 31798 MW; 09471CFF3B781727 CRC64;
MSRLTVIATG GTISTSTDHD GVRRPAYSGT ELTAHVAVDV DVVDLMTVDS SQLIPTDWDR
IRAAVHTATR NGARGVVVTH GTDTMEETAL WLDLTYAGNV PVVLTGAMRS ADAPNADGPT
NLREALAVAA SPAARGVGVL VSFAGRVLQP LGLRKAATQD LSGFAGELLG TSSSGFALTA
AKTRPYLGDL CAADAPRVDI VAAYLGSDSV ALDAYVSTGA RGIVLEALGS GNAGAAVVDG
VRRHCHNGIV IAVSTRVPEG HVSAGYGPGH DLVEAGAVLV PWLRPSQVRV LLMAALAANL
PIADVIERWG
