(data stored in ACNUC7421 zone)

SWISSPROT: B2TET8_PARPJ

ID   B2TET8_PARPJ            Unreviewed;       330 AA.
AC   B2TET8;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   08-MAY-2019, entry version 73.
DE   SubName: Full=L-asparaginase, type II {ECO:0000313|EMBL:ACD18609.1};
DE            EC=3.5.1.38 {ECO:0000313|EMBL:ACD18609.1};
GN   OrderedLocusNames=Bphyt_4228 {ECO:0000313|EMBL:ACD18609.1};
OS   Paraburkholderia phytofirmans (strain DSM 17436 / LMG 22146 / PsJN)
OS   (Burkholderia phytofirmans).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=398527 {ECO:0000313|EMBL:ACD18609.1, ECO:0000313|Proteomes:UP000001739};
RN   [1] {ECO:0000313|EMBL:ACD18609.1, ECO:0000313|Proteomes:UP000001739}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17436 / LMG 22146 / PsJN
RC   {ECO:0000313|Proteomes:UP000001739};
RX   PubMed=21551308; DOI=10.1128/JB.05055-11;
RA   Weilharter A., Mitter B., Shin M.V., Chain P.S., Nowak J.,
RA   Sessitsch A.;
RT   "Complete genome sequence of the plant growth-promoting endophyte
RT   Burkholderia phytofirmans strain PsJN.";
RL   J. Bacteriol. 193:3383-3384(2011).
CC   -!- SIMILARITY: Belongs to the asparaginase 1 family.
CC       {ECO:0000256|RuleBase:RU004456}.
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DR   EMBL; CP001053; ACD18609.1; -; Genomic_DNA.
DR   RefSeq; WP_012426125.1; NC_010676.1.
DR   STRING; 398527.Bphyt_4228; -.
DR   EnsemblBacteria; ACD18609; ACD18609; Bphyt_4228.
DR   KEGG; bpy:Bphyt_4228; -.
DR   eggNOG; ENOG4105HDK; Bacteria.
DR   eggNOG; COG0252; LUCA.
DR   HOGENOM; HOG000044165; -.
DR   KO; K05597; -.
DR   OMA; VRKNHTS; -.
DR   OrthoDB; 1659551at2; -.
DR   BioCyc; BPHY398527:GJEX-4223-MONOMER; -.
DR   Proteomes; UP000001739; Chromosome 2.
DR   GO; GO:0004067; F:asparaginase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0050417; F:glutamin-(asparagin-)ase 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   TIGRFAMs; TIGR00520; asnASE_II; 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;
DR   PRODOM; B2TET8.
DR   SWISS-2DPAGE; B2TET8.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001739};
KW   Hydrolase {ECO:0000313|EMBL:ACD18609.1}.
FT   DOMAIN        6    198       Asparaginase. {ECO:0000259|Pfam:PF00710}.
FT   DOMAIN      218    327       Asparaginase_C. {ECO:0000259|Pfam:
FT                                PF17763}.
FT   REGION       95     96       Substrate binding. {ECO:0000256|PIRSR:
FT                                PIRSR001220-2}.
FT   ACT_SITE     15     15       {ECO:0000256|PROSITE-ProRule:PRU10099}.
FT   ACT_SITE     15     15       Acyl-ester intermediate.
FT                                {ECO:0000256|PIRSR:PIRSR604550-50}.
FT   ACT_SITE     15     15       O-isoaspartyl threonine intermediate.
FT                                {ECO:0000256|PIRSR:PIRSR001220-1}.
FT   ACT_SITE     95     95       {ECO:0000256|PROSITE-ProRule:PRU10100}.
FT   BINDING      62     62       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001220-2}.
SQ   SEQUENCE   330 AA;  35100 MW;  425707C36955C857 CRC64;
     MTAKANIVVI GTGGTIAGQG KASVNTSTYM CSVLGIDEIL GSIPHAGELA NLRAEQLLQT
     GSENFNNTHL LAIGNRVAEL LARNDVDGVV ITHGTDTIEE TAYFLHLTLK SAKPVVVVGS
     MRPPSAMSSD AALNLYDALA VATHPSSRGL GTLVVANNEI HTARDVVKSN SFKLDAFRSP
     YGALGYVIEG APRYYRRPAR AHTLDTPWSI TTLRSLPKVD IVYAYGALEP GAISAITANA
     RGLIYVGTGN GNVASHLIDP LRDAARRGVH VVRASRTGSG IVLHNGAQPD HEYGWLTVDD
     QIPQKARILL TLALTQTDDT AALQAVFERY
//

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