ID A0A0Q5NZA7_9BURK Unreviewed; 477 AA.
AC A0A0Q5NZA7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=2-aminoadipate aminotransferase {ECO:0000313|EMBL:KQR78990.1};
GN ORFNames=ASG35_09580 {ECO:0000313|EMBL:KQR78990.1};
OS Burkholderia sp. Leaf177.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia.
OX NCBI_TaxID=1736287 {ECO:0000313|EMBL:KQR78990.1, ECO:0000313|Proteomes:UP000051826};
RN [1] {ECO:0000313|EMBL:KQR78990.1, ECO:0000313|Proteomes:UP000051826}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf177 {ECO:0000313|EMBL:KQR78990.1,
RC ECO:0000313|Proteomes:UP000051826};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQR78990.1, ECO:0000313|Proteomes:UP000051826}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf177 {ECO:0000313|EMBL:KQR78990.1,
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 -!- SIMILARITY: In the C-terminal section; belongs to the class-I
CC pyridoxal-phosphate-dependent aminotransferase family.
CC {ECO:0000256|ARBA:ARBA00005384}.
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:KQR78990.1}.
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DR EMBL; LMPF01000021; KQR78990.1; -; Genomic_DNA.
DR RefSeq; WP_056359804.1; NZ_LMPF01000021.1.
DR AlphaFoldDB; A0A0Q5NZA7; -.
DR OrthoDB; 9804020at2; -.
DR Proteomes; UP000051826; Unassembled WGS sequence.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
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 CDD; cd07377; WHTH_GntR; 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 Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding 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 InterPro; IPR000524; Tscrpt_reg_HTH_GntR.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR46577; HTH-TYPE TRANSCRIPTIONAL REGULATORY PROTEIN GABR; 1.
DR PANTHER; PTHR46577:SF2; TRANSCRIPTIONAL REGULATORY PROTEIN; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR Pfam; PF00392; GntR; 1.
DR SMART; SM00345; HTH_GNTR; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS50949; HTH_GNTR; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:KQR78990.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051826};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Transferase {ECO:0000313|EMBL:KQR78990.1}.
FT DOMAIN 1..69
FT /note="HTH gntR-type"
FT /evidence="ECO:0000259|PROSITE:PS50949"
SQ SEQUENCE 477 AA; 52874 MW; BB2BC97F392FE779 CRC64;
MMLYEKLAAE VEEAMRRGVF AVGERVPSVR QASAQYGVSI KTVLRAYALL ESRGLLETRP
QSGYFVREMP AAKAETPAVS QPPAVASTVD VSRLVLSTLR SIRSEDATPL GSPYPDPSLF
PWRKINQLAN AIARRHSSWN LIDDLPPGNP ELIRQIARRY AENGVPVDPD EIVITVGATE
AINLSLQAVA KPGDTVAVES PTYYAMLHAI ERMGMRAIEV PTHPAAGIDI DALANIIGEH
EIAACMVMPN FQNPLGFVMS DANKQRLVAL LAEHDIPVIE NDVYQELYYG DARPSALKNF
DKKGLVLHCA SFSKSLTASY RIGWAMPGRY RGQVEKLKFL NTLTTPSVPQ VAVADYLKQG
GYDHHLRHVR RVYRQQARLM IATVLRFFPA GTQTSEPMGG YVLWVELPAN VDSMKLYKAA
LDRGITIGPG TMFSSRDAFR HFIRLNYSYP WNIQTEAALK TLGELAASMA GRRQHER
//