ASPG1_BACSU
ID ASPG1_BACSU Reviewed; 329 AA.
AC P26900;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=L-asparaginase 1;
DE Short=L-ASNase 1;
DE EC=3.5.1.1;
DE AltName: Full=L-asparagine amidohydrolase 1;
GN Name=ansA; OrderedLocusNames=BSU23580;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1711029; DOI=10.1128/jb.173.12.3831-3845.1991;
RA Sun D., Setlow P.;
RT "Cloning, nucleotide sequence, and expression of the Bacillus subtilis ans
RT operon, which codes for L-asparaginase and L-aspartase.";
RL J. Bacteriol. 173:3831-3845(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / JH642;
RX PubMed=8969508; DOI=10.1099/13500872-142-11-3103;
RA Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M.,
RA Kobayashi Y.;
RT "Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the
RT Bacillus subtilis genome containing the skin element and many sporulation
RT genes.";
RL Microbiology 142:3103-3111(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-23.
RX PubMed=8478318; DOI=10.1128/jb.175.9.2501-2506.1993;
RA Sun D., Setlow P.;
RT "Cloning and nucleotide sequence of the Bacillus subtilis ansR gene, which
RT encodes a repressor of the ans operon coding for L-asparaginase and L-
RT aspartase.";
RL J. Bacteriol. 175:2501-2506(1993).
RN [5]
RP INDUCTION.
RX PubMed=11914346; DOI=10.1128/jb.184.8.2148-2154.2002;
RA Fisher S.H., Wray L.V. Jr.;
RT "Bacillus subtilis 168 contains two differentially regulated genes encoding
RT L-asparaginase.";
RL J. Bacteriol. 184:2148-2154(2002).
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.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=Long;
CC IsoId=P26900-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=P26900-2; Sequence=VSP_018651;
CC -!- INDUCTION: Expression is induced by asparagine.
CC {ECO:0000269|PubMed:11914346}.
CC -!- MISCELLANEOUS: B.subtilis contains two L-asparaginase isoenzymes: L-
CC asparaginase I, a low-affinity enzyme located in the cytoplasm, and L-
CC asparaginase II, a high-affinity secreted enzyme.
CC -!- MISCELLANEOUS: [Isoform Long]: Produced in 2 x SG medium but not in 2 x
CC YT medium.
CC -!- MISCELLANEOUS: [Isoform Short]: Produced in 2 x YT medium but not in 2
CC x SG medium. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the asparaginase 1 family. {ECO:0000305}.
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DR EMBL; M63264; AAA22243.1; -; Genomic_DNA.
DR EMBL; D84432; BAA12642.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14290.1; -; Genomic_DNA.
DR EMBL; L08205; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A39440; A39440.
DR RefSeq; NP_390239.1; NC_000964.3. [P26900-1]
DR RefSeq; WP_004399032.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; P26900; -.
DR SMR; P26900; -.
DR STRING; 224308.BSU23580; -.
DR jPOST; P26900; -.
DR PaxDb; P26900; -.
DR PRIDE; P26900; -.
DR EnsemblBacteria; CAB14290; CAB14290; BSU_23580.
DR GeneID; 938722; -.
DR KEGG; bsu:BSU23580; -.
DR PATRIC; fig|224308.179.peg.2570; -.
DR eggNOG; COG0252; Bacteria.
DR InParanoid; P26900; -.
DR OMA; AIVPKLM; -.
DR PhylomeDB; P26900; -.
DR BioCyc; BSUB:BSU23580-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004067; F:asparaginase activity; IEA:UniProtKB-EC.
DR GO; GO:0006520; P:cellular amino acid metabolic process; IEA:InterPro.
DR CDD; cd08963; L-asparaginase_I; 1.
DR Gene3D; 3.40.50.1170; -; 1.
DR Gene3D; 3.40.50.40; -; 1.
DR InterPro; IPR006033; AsnA_fam.
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; IPR041725; L-asparaginase_I.
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; TIGR00519; asnASE_I; 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 2: Evidence at transcript level;
KW Alternative initiation; Cytoplasm; Hydrolase; Reference proteome.
FT CHAIN 1..329
FT /note="L-asparaginase 1"
FT /id="PRO_0000002354"
FT DOMAIN 2..322
FT /note="Asparaginase/glutaminase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01068"
FT ACT_SITE 12
FT /note="O-isoaspartyl threonine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10099,
FT ECO:0000255|PROSITE-ProRule:PRU10100"
FT BINDING 54
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 85..86
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..5
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000305"
FT /id="VSP_018651"
SQ SEQUENCE 329 AA; 36455 MW; 4977F09E58CAB6C4 CRC64;
MKKLLMLTTG GTIASVEGEN GLAPGVKADE LLSYVSKLDN DYTMETQSLM NIDSTNMQPE
YWVEIAEAVK ENYDAYDGFV ITHGTDTMAY TSAALSYMLQ HAKKPIVITG SQIPITFQKT
DAKKNITDAI RFACEGVGGV YVVFDGRVIQ GTRAIKLRTK SYDAFESINY PYIAFINEDG
IEYNKQVTEP ENDTFTVDTS LCTDVCLLKL HPGLKPEMFD ALKSMYKGIV IESYGSGGVP
FEGRDILSKV NELIESGIVV VITTQCLEEG EDMSIYEVGR RVNQDLIIRS RNMNTEAIVP
KLMWALGQSS DLPVVKRIME TPIADDVVL
