(data stored in SCRATCH zone)

SWISSPROT: 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   11-DEC-2019, entry version 135.
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}.
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   SMR; P26900; -.
DR   STRING; 224308.BSU23580; -.
DR   jPOST; P26900; -.
DR   PaxDb; P26900; -.
DR   PRIDE; P26900; -.
DR   EnsemblBacteria; CAB14290; CAB14290; BSU23580.
DR   GeneID; 938722; -.
DR   KEGG; bsu:BSU23580; -.
DR   PATRIC; fig|224308.179.peg.2570; -.
DR   eggNOG; ENOG4105HDK; Bacteria.
DR   eggNOG; COG0252; LUCA.
DR   HOGENOM; HOG000227974; -.
DR   InParanoid; P26900; -.
DR   KO; K01424; -.
DR   OMA; YFEYKLY; -.
DR   PhylomeDB; P26900; -.
DR   BioCyc; BSUB:BSU23580-MONOMER; -.
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;
DR   PRODOM; P26900.
DR   SWISS-2DPAGE; P26900.
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   REGION          85..86
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000250"
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                   /note="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
//

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