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Database: UniProt/TrEMBL
Entry: Q13LB9_PARXL
LinkDB: Q13LB9_PARXL
Original site: Q13LB9_PARXL 
ID   Q13LB9_PARXL            Unreviewed;       429 AA.
AC   Q13LB9;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   25-OCT-2017, entry version 71.
DE   SubName: Full=4-aminobutyrate aminotransferase apoenzyme {ECO:0000313|EMBL:ABE35120.1};
DE            EC=2.6.1.19 {ECO:0000313|EMBL:ABE35120.1};
GN   ORFNames=Bxe_B0834 {ECO:0000313|EMBL:ABE35120.1};
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265 {ECO:0000313|EMBL:ABE35120.1, ECO:0000313|Proteomes:UP000001817};
RN   [1] {ECO:0000313|EMBL:ABE35120.1, ECO:0000313|Proteomes:UP000001817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400 {ECO:0000313|EMBL:ABE35120.1,
RC   ECO:0000313|Proteomes:UP000001817};
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S., 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).
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|RuleBase:RU003560}.
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DR   EMBL; CP000271; ABE35120.1; -; Genomic_DNA.
DR   ProteinModelPortal; Q13LB9; -.
DR   STRING; 266265.Bxe_B0834; -.
DR   EnsemblBacteria; ABE35120; ABE35120; Bxe_B0834.
DR   KEGG; bxe:Bxe_B0834; -.
DR   eggNOG; ENOG4108JPW; Bacteria.
DR   eggNOG; COG0160; LUCA.
DR   HOGENOM; HOG000020206; -.
DR   KO; K07250; -.
DR   OMA; RVGNYLT; -.
DR   OrthoDB; POG091H0APS; -.
DR   Proteomes; UP000001817; Chromosome 2.
DR   GO; GO:0034386; F:4-aminobutyrate:2-oxoglutarate transaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0009448; P:gamma-aminobutyric acid metabolic process; IEA:InterPro.
DR   CDD; cd00610; OAT_like; 1.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 2.
DR   InterPro; IPR004632; 4NH2But_aminotransferase_bac.
DR   InterPro; IPR005814; Aminotrans_3.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_sub2.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 2.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR00700; GABAtrnsam; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000313|EMBL:ABE35120.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001817};
KW   Pyridoxal phosphate {ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001817};
KW   Transferase {ECO:0000313|EMBL:ABE35120.1}.
SQ   SEQUENCE   429 AA;  46058 MW;  C3C2CD720580FBE5 CRC64;
     MTMKNAELKS RKDAATPRGV GVMCDFYAER AENAELWDIE GRRFIDFAAG IAVCNTGHRH
     PKIVAAIRDQ LDHFTHTAYQ IVPYASYVEL AEKLNERAPG DYPKKTAFFT TGAEAVENAI
     KIARAATGRP GVIAFTGAFH GRTLMGMALT GKVAPYKIGF GPFPSDVFHA PFPNPLHGVT
     TADSLKAIEF LFKADIDPKR VAAIIFEPVQ GEGGFYPAPA EFVRALRKLC NEHGILLIAD
     EVQTGFARTG KLFAMNHYDV VPDLMTVAKS LAGGMPLSGV IGRADVMDAA APGGLGGTYA
     GNPLAVAAAH AVLDIIDEEK LCERATLLGD RIKAKLIALQ SDVPQIADVR GPGGMVAVEF
     CKAGTTEPDA EFTKRVQSRA LERGLLLLVC GVYSNVVRFL FPLTIQEAVF DEALAILEDV
     IKDSVAITV
//
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