ID   A0A0Q5PFU4_9BURK        Unreviewed;       393 AA.
AC   A0A0Q5PFU4;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Aminotransferase {ECO:0000313|EMBL:KQR85953.1};
GN   ORFNames=ASG35_24850 {ECO:0000313|EMBL:KQR85953.1};
OS   Burkholderia sp. Leaf177.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia.
OX   NCBI_TaxID=1736287 {ECO:0000313|EMBL:KQR85953.1, ECO:0000313|Proteomes:UP000051826};
RN   [1] {ECO:0000313|EMBL:KQR85953.1, ECO:0000313|Proteomes:UP000051826}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf177 {ECO:0000313|EMBL:KQR85953.1,
RC   ECO:0000313|Proteomes:UP000051826};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQR85953.1, ECO:0000313|Proteomes:UP000051826}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf177 {ECO:0000313|EMBL:KQR85953.1,
RC   ECO:0000313|Proteomes:UP000051826};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
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:KQR85953.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LMPF01000003; KQR85953.1; -; Genomic_DNA.
DR   RefSeq; WP_056353911.1; NZ_LMPF01000003.1.
DR   AlphaFoldDB; A0A0Q5PFU4; -.
DR   OrthoDB; 9763453at2; -.
DR   Proteomes; UP000051826; Unassembled WGS sequence.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   CDD; cd00609; AAT_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; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR43807; FI04487P; 1.
DR   PANTHER; PTHR43807:SF20; FI04487P; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   4: Predicted;
KW   Aminotransferase {ECO:0000313|EMBL:KQR85953.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051826};
KW   Transferase {ECO:0000313|EMBL:KQR85953.1}.
FT   DOMAIN          40..390
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   393 AA;  43165 MW;  A0DE286056406852 CRC64;
     MNASHDLPHS AAVPAITSRL PSVGTTIFTV MSALAAQKGA VNLGQGFPDF ACDPRIVDAV
     ANAMRDGHNQ YPPMAGAAPL RHAISEKIER LYGRKYDVER EITVTAGATQ AILTAILCCV
     HPGDEVIVIE PMYDCYVPAI ELAGGKPVFV SLEAPDYALP FDKIAAAITP KTRLLIINTP
     HNPTGRVWRA ADMQKLDEIM RGTNVLILSD EVYEHMVFDG APHESVSRYP DLAARSFVVS
     SFGKTFHVTG WKVGYVAAPA ALTAEFRKVH QFNVFTVNTP MQVGIAEYLK DPSPYMDLPA
     FYQQKRDFFR AGLANSRFKL LPCDGTYFQC VDYSAISDLP EAEFSQWLTS EIGVAAIPVS
     AFYHESHESG VVRFCFAKKE ETLRTALERL ASL
//