(data stored in ACNUC7421 zone)

SWISSPROT: Q13QZ0_PARXL

ID   Q13QZ0_PARXL            Unreviewed;       347 AA.
AC   Q13QZ0;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   05-JUL-2017, entry version 70.
DE   SubName: Full=Putative asparaginase/glutaminase {ECO:0000313|EMBL:ABE33499.1};
DE            EC=3.5.1.38 {ECO:0000313|EMBL:ABE33499.1};
GN   ORFNames=Bxe_B2492 {ECO:0000313|EMBL:ABE33499.1};
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265 {ECO:0000313|EMBL:ABE33499.1, ECO:0000313|Proteomes:UP000001817};
RN   [1] {ECO:0000313|EMBL:ABE33499.1, ECO:0000313|Proteomes:UP000001817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400 {ECO:0000313|EMBL:ABE33499.1,
RC   ECO:0000313|Proteomes:UP000001817};
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S.G., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA   Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M.,
RA   Lao V., Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A.,
RA   Marx C.J., Parnell J.J., Ramette A., Richardson P., Seeger M.,
RA   Smith D., Spilker T., Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B.,
RA   Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp
RT   genome shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
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DR   EMBL; CP000271; ABE33499.1; -; Genomic_DNA.
DR   ProteinModelPortal; Q13QZ0; -.
DR   STRING; 266265.Bxe_B2492; -.
DR   EnsemblBacteria; ABE33499; ABE33499; Bxe_B2492.
DR   KEGG; bxb:DR64_4819; -.
DR   KEGG; bxe:Bxe_B2492; -.
DR   eggNOG; COG0252; LUCA.
DR   HOGENOM; HOG000044165; -.
DR   KO; K05597; -.
DR   OMA; VRKNHTS; -.
DR   OrthoDB; POG091H00MR; -.
DR   Proteomes; UP000001817; 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:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   Gene3D; 3.40.50.1170; -; 1.
DR   Gene3D; 3.40.50.40; -; 1.
DR   Gene3D; 3.50.50.60; -; 1.
DR   InterPro; IPR006034; Asparaginase/glutaminase-like.
DR   InterPro; IPR027475; Asparaginase/glutaminase_AS2.
DR   InterPro; IPR006076; FAD-dep_OxRdtase.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR027473; L-asparaginase_C.
DR   InterPro; IPR027474; L-asparaginase_N.
DR   Pfam; PF00710; Asparaginase; 1.
DR   Pfam; PF01266; DAO; 1.
DR   PRINTS; PR00139; ASNGLNASE.
DR   SMART; SM00870; Asparaginase; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   SUPFAM; SSF53774; SSF53774; 1.
DR   PROSITE; PS00917; ASN_GLN_ASE_2; 1.
DR   PROSITE; PS51732; ASN_GLN_ASE_3; 1.
PE   4: Predicted;
DR   PRODOM; Q13QZ0.
DR   SWISS-2DPAGE; Q13QZ0.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001817};
KW   Hydrolase {ECO:0000313|EMBL:ABE33499.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001817}.
FT   DOMAIN        3    116       DAO. {ECO:0000259|Pfam:PF01266}.
FT   DOMAIN       95    215       Asparaginase. {ECO:0000259|Pfam:PF00710}.
SQ   SEQUENCE   347 AA;  37010 MW;  DAB831AF93044EE9 CRC64;
     MLRERGVRFL MNTTVDGLRR SPHGVEAFSG GAALPADHVV LASGAGAARL LKPIGIRAAI
     YPIKGYSLTF ELQAQSTAPH VSITDSGRKV VYARLELLAR NDVDGVVVTH GTDTIEETSY
     FLHLTLKSAK PVVVVGSMRP PSAMSSDAAL NLYDALAVAA HPSSRGLGAL VVANSEIHTA
     RDVVKSNSFK LDAFRSPYGA LGIVIEGTPR YYRRPARAHT LDTPWSIDTL RTLPKVDIVY
     AYGALESSAV AAIAKNARGL VFAGTGNGNV AGHLIGPLRD AARRGVRVVR ASRTGNGVVL
     HNAAQPDDEY GWLTVDDQAP LKARLLLTLA LTQTDDTNAL QAVFERY
//

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