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Database: UniProt
Entry: B4E922_BURCJ
LinkDB: B4E922_BURCJ
Original site: B4E922_BURCJ 
ID   B4E922_BURCJ            Unreviewed;       480 AA.
AC   B4E922;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 76.
DE   SubName: Full=Aminotransferase {ECO:0000313|EMBL:CAR50908.1};
GN   ORFNames=BCAL0599 {ECO:0000313|EMBL:CAR50908.1};
OS   Burkholderia cenocepacia (strain ATCC BAA-245 / DSM 16553 / LMG 16656 /
OS   NCTC 13227 / J2315 / CF5610) (Burkholderia cepacia (strain J2315)).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=216591 {ECO:0000313|EMBL:CAR50908.1, ECO:0000313|Proteomes:UP000001035};
RN   [1] {ECO:0000313|EMBL:CAR50908.1, ECO:0000313|Proteomes:UP000001035}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-245 / DSM 16553 / LMG 16656 / NCTC 13227 / J2315 /
RC   CF5610 {ECO:0000313|Proteomes:UP000001035};
RX   PubMed=18931103; DOI=10.1128/JB.01230-08;
RA   Holden M.T., Seth-Smith H.M., Crossman L.C., Sebaihia M., Bentley S.D.,
RA   Cerdeno-Tarraga A.M., Thomson N.R., Bason N., Quail M.A., Sharp S.,
RA   Cherevach I., Churcher C., Goodhead I., Hauser H., Holroyd N., Mungall K.,
RA   Scott P., Walker D., White B., Rose H., Iversen P., Mil-Homens D.,
RA   Rocha E.P., Fialho A.M., Baldwin A., Dowson C., Barrell B.G., Govan J.R.,
RA   Vandamme P., Hart C.A., Mahenthiralingam E., Parkhill J.;
RT   "The genome of Burkholderia cenocepacia J2315, an epidemic pathogen of
RT   cystic fibrosis patients.";
RL   J. Bacteriol. 191:261-277(2009).
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|ARBA:ARBA00008954,
CC       ECO:0000256|RuleBase:RU003560}.
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DR   EMBL; AM747720; CAR50908.1; -; Genomic_DNA.
DR   RefSeq; WP_012492360.1; NC_011000.1.
DR   AlphaFoldDB; B4E922; -.
DR   KEGG; bcj:BCAL0599; -.
DR   eggNOG; COG0161; Bacteria.
DR   HOGENOM; CLU_016922_4_1_4; -.
DR   BioCyc; BCEN216591:G1G1V-681-MONOMER; -.
DR   Proteomes; UP000001035; Chromosome 1.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   CDD; cd00610; OAT_like; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR005814; Aminotrans_3.
DR   InterPro; IPR049704; Aminotrans_3_PPA_site.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR43094; AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR43094:SF1; AMINOTRANSFERASE CLASS-III; 1.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 2.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000313|EMBL:CAR50908.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560}; Transferase {ECO:0000313|EMBL:CAR50908.1}.
SQ   SEQUENCE   480 AA;  52432 MW;  0FBAAD75CEFDF60A CRC64;
     MTYRNESAWI QPAAPTATAA APRATQARST AEYRALDAAH HIHPFSDMGA LNRAGSRVIV
     KADGVYLWDS DGNKVIDGMA GLWCVNVGYG RKELADAAYR QIQELPFYNT FFKTTHPPVI
     ELSAMLAEVT PAGFNHFFYC NSGSEGNDTV LRLVHQYWRV QGKPQKKYVI SRKNGYHGST
     IAGGTLGGMG YMHEQMPSKV EHIVHIDQPY FFGEAQAGET LEAFGLARAQ QLEAKILELG
     AENVAAFIGE PFQGAGGVIF PPSTYWPEIQ RICRKYDILL VADEVIGGFG RTGEWFAHQH
     FGFEPDLITM AKGLTSGYVP MGAVGIHERV ARPIIDNGEF NHGLTYSGHP VAAAVAIANL
     KLLRDEGIVE RVKTDTGPYF QALMRETFAR HPIVGEVHGH GMVASLQLAE APAARLRFAN
     GGDVGTICRD FCFNGNLIMR ATGDRMLLSP PLVISRQEID ELVSKAKKAV DATAQQLGIS
//
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