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Database: UniProt
Entry: A0A257DEV9_9BURK
LinkDB: A0A257DEV9_9BURK
Original site: A0A257DEV9_9BURK 
ID   A0A257DEV9_9BURK        Unreviewed;       381 AA.
AC   A0A257DEV9;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Aminotransferase {ECO:0000313|EMBL:OYT99834.1};
GN   ORFNames=CFE40_00340 {ECO:0000313|EMBL:OYT99834.1};
OS   Burkholderiales bacterium PBB1.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales.
OX   NCBI_TaxID=2015563 {ECO:0000313|EMBL:OYT99834.1, ECO:0000313|Proteomes:UP000216950};
RN   [1] {ECO:0000313|EMBL:OYT99834.1, ECO:0000313|Proteomes:UP000216950}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PBB1 {ECO:0000313|EMBL:OYT99834.1};
RA   Kojadinovic M., Villain A., Puppo C., Fon Sing S., Prioretti L., Hubert P.,
RA   Gregori G., Zhang Y., Sassi J.-F., Claverie J.-M., Blanc G., Gontero B.;
RT   "A metagenomic investigation of the 'star' freshwater diatom Asterionella
RT   formosa and its bacterial cohort.";
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|PIRSR:PIRSR000524-50};
CC   -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|ARBA:ARBA00009236}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OYT99834.1}.
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DR   EMBL; NKIN01000001; OYT99834.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A257DEV9; -.
DR   Proteomes; UP000216950; Unassembled WGS sequence.
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; 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.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000313|EMBL:OYT99834.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR000524-50};
KW   Reference proteome {ECO:0000313|Proteomes:UP000216950};
KW   Transferase {ECO:0000313|EMBL:OYT99834.1}.
FT   DOMAIN          22..324
FT                   /note="Aminotransferase class V"
FT                   /evidence="ECO:0000259|Pfam:PF00266"
FT   BINDING         348
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000524-1"
FT   MOD_RES         197
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000524-50"
SQ   SEQUENCE   381 AA;  41496 MW;  22B1DC26EB7CCBA2 CRC64;
     MPGLLPDVDP DGLLEYSVVY TDRAINHMSK RFQQVMKDIS ATLKEVYHAK AAVIVPGSGT
     FGMEAVARQF ATGRKVLVIR NGWFSYRWTQ IFEMGSIPSH ATVLKARRIG AGAQAPFAPA
     PIDEVVAAIK EQRPEVVFAP HVETSAGMIL PDGYLRAVAD AVHSVGGLFV LDCIASGTIW
     VDMVATGVDV LVSAPQKGWS GPPCCAMVML SEQARQRIDS TQSTSYACDL RKWLQIMEAY
     EGGAHAYHAT MPTDALARVR DVMFETRAYG FDQVRDEQQQ LGDAVRSMLT QRGFKSVAAP
     GFQAPGVVVC YTDDAEMQSG KKWLGLGLQI AAGVPLQCDE GPDFRSFRIG LFGLDKLHQR
     ERTVKSLSDA LDRLLAPATT V
//
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