ID A0A0Q5P8M0_9BURK Unreviewed; 375 AA.
AC A0A0Q5P8M0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN ORFNames=ASG35_08035 {ECO:0000313|EMBL:KQR78390.1};
OS Burkholderia sp. Leaf177.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia.
OX NCBI_TaxID=1736287 {ECO:0000313|EMBL:KQR78390.1, ECO:0000313|Proteomes:UP000051826};
RN [1] {ECO:0000313|EMBL:KQR78390.1, ECO:0000313|Proteomes:UP000051826}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf177 {ECO:0000313|EMBL:KQR78390.1,
RC ECO:0000313|Proteomes:UP000051826};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQR78390.1, ECO:0000313|Proteomes:UP000051826}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf177 {ECO:0000313|EMBL:KQR78390.1,
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|RuleBase:RU000481};
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|RuleBase:RU000481}.
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:KQR78390.1}.
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DR EMBL; LMPF01000021; KQR78390.1; -; Genomic_DNA.
DR RefSeq; WP_056359049.1; NZ_LMPF01000021.1.
DR AlphaFoldDB; A0A0Q5P8M0; -.
DR OrthoDB; 9803354at2; -.
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; IPR004838; NHTrfase_class1_PyrdxlP-BS.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR43510; AMINOTRANSFERASE FUNCTION, HYPOTHETICAL (EUROFUNG); 1.
DR PANTHER; PTHR43510:SF1; AMINOTRANSFERASE FUNCTION, HYPOTHETICAL (EUROFUNG); 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000256|RuleBase:RU000481,
KW ECO:0000313|EMBL:KQR78390.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051826};
KW Transferase {ECO:0000256|RuleBase:RU000481, ECO:0000313|EMBL:KQR78390.1}.
FT DOMAIN 55..353
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 375 AA; 41768 MW; 4DA8E887ED9AC7B3 CRC64;
MKIKDFLVER WMDRYEHEAR YNLAETCVES LTVDQLLTLT GKQDSIMDEL RPMKLTYGAI
EGSERLRANI ASLYDRQTPK NILVTHGAIG GNALVYETLI EPGDRVIAVL PTYQQHYSIP
ESYGADLHTM TLREENSFLP DLDELRQLAS QKTKLIAINN PNNPTGSLMD EAFLREVVAI
AQSCGAYLLC DEVYRGTDQE GSGFTASVAD LYERGISTGS MSKTWSLAGL RLGWIAGPVE
LIRAVCIHRD YNTISVGMID DHLASIALES KDKILDRNHA ITRTNLATLD AWVRQEPLVS
YVKPKAATVC LLKFDVDISS TEFCTSLIEA TGVMFTPGSA FEMEGYVRIG FANPLDVLQL
GLGRVSDFLK DIERR
//
