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Database: UniProt
Entry: B2T0A9_PARPJ
LinkDB: B2T0A9_PARPJ
Original site: B2T0A9_PARPJ 
ID   B2T0A9_PARPJ            Unreviewed;       412 AA.
AC   B2T0A9;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   27-MAR-2024, entry version 83.
DE   SubName: Full=Aminotransferase class V {ECO:0000313|EMBL:ACD15214.1};
GN   OrderedLocusNames=Bphyt_0791 {ECO:0000313|EMBL:ACD15214.1};
OS   Paraburkholderia phytofirmans (strain DSM 17436 / LMG 22146 / PsJN)
OS   (Burkholderia phytofirmans).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=398527 {ECO:0000313|EMBL:ACD15214.1, ECO:0000313|Proteomes:UP000001739};
RN   [1] {ECO:0000313|EMBL:ACD15214.1, 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., 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   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|PIRSR:PIRSR000524-50, ECO:0000256|RuleBase:RU004504};
CC   -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|ARBA:ARBA00009236,
CC       ECO:0000256|RuleBase:RU004075}.
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DR   EMBL; CP001052; ACD15214.1; -; Genomic_DNA.
DR   RefSeq; WP_012431849.1; NC_010681.1.
DR   AlphaFoldDB; B2T0A9; -.
DR   STRING; 398527.Bphyt_0791; -.
DR   KEGG; bpy:Bphyt_0791; -.
DR   eggNOG; COG0075; Bacteria.
DR   HOGENOM; CLU_027686_0_0_4; -.
DR   OrthoDB; 9766472at2; -.
DR   Proteomes; UP000001739; Chromosome 1.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
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; IPR000192; Aminotrans_V_dom.
DR   InterPro; IPR020578; Aminotrans_V_PyrdxlP_BS.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   InterPro; IPR024169; SP_NH2Trfase/AEP_transaminase.
DR   PANTHER; PTHR21152:SF39; ALANINE--GLYOXYLATE AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR21152; AMINOTRANSFERASE CLASS V; 1.
DR   Pfam; PF00266; Aminotran_5; 1.
DR   PIRSF; PIRSF000524; SPT; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000313|EMBL:ACD15214.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR000524-50};
KW   Transferase {ECO:0000313|EMBL:ACD15214.1}.
FT   DOMAIN          52..342
FT                   /note="Aminotransferase class V"
FT                   /evidence="ECO:0000259|Pfam:PF00266"
FT   BINDING         359
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000524-1"
FT   MOD_RES         216
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000524-50"
SQ   SEQUENCE   412 AA;  43489 MW;  54DC9936AA0871A4 CRC64;
     MPTSSFTSAA SIVPCPVVES LDAILPEEPL LMMGAGPVPI PAAVAKANTI VINHLGATMV
     KVIGQVKTMA RYVFQTKSKW VLGVAGPGSA AMEMAISNLA WEGTRVLSIK NGFFSERMAE
     MGRRVGAHVS VLDVADGAVA SLDEVAEAIR RERPEVVTVV QGETSNTVWN YHLKDIAALA
     KAAGALVVVD AVCTLSTMPL EMDAWGIDAV ITGGQKGLSS IPGVSLIAFS DAAWTRVKTR
     TAPNAHWCLD ASLAENFWHN AGYHYTAPVS GVLALHEALR LVCAETLEKR FARHLKCSQA
     LQEGISALGL KLYAPQACRL NSVVGIEVPA GLSPGDICGH ISRHHQVEIS GSFGLPIVRI
     GQMGEQCREH NLFRTLHALG RTMVDLGSAV DLPAGVAALE KSLSGGARAV AR
//
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