ID A0A0M2H4Z7_9MICO Unreviewed; 473 AA.
AC A0A0M2H4Z7;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=2-aminoadipate transaminase {ECO:0000313|EMBL:KJL38864.1};
DE EC=2.6.1.39 {ECO:0000313|EMBL:KJL38864.1};
GN Name=lysN {ECO:0000313|EMBL:KJL38864.1};
GN ORFNames=RS81_02271 {ECO:0000313|EMBL:KJL38864.1};
OS Microbacterium ketosireducens.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=92835 {ECO:0000313|EMBL:KJL38864.1, ECO:0000313|Proteomes:UP000033956};
RN [1] {ECO:0000313|EMBL:KJL38864.1, ECO:0000313|Proteomes:UP000033956}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12510 {ECO:0000313|EMBL:KJL38864.1,
RC ECO:0000313|Proteomes:UP000033956};
RA Corretto E.;
RT "Draft genome sequences of ten Microbacterium spp. with emphasis on heavy
RT metal contaminated environments.";
RL Submitted (FEB-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:KJL38864.1}.
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DR EMBL; JYIZ01000053; KJL38864.1; -; Genomic_DNA.
DR RefSeq; WP_045276207.1; NZ_JYIZ01000053.1.
DR AlphaFoldDB; A0A0M2H4Z7; -.
DR STRING; 92835.RS81_02271; -.
DR PATRIC; fig|92835.4.peg.2307; -.
DR OrthoDB; 199743at2; -.
DR Proteomes; UP000033956; Unassembled WGS sequence.
DR GO; GO:0047536; F:2-aminoadipate transaminase activity; IEA:UniProtKB-EC.
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:0009058; P:biosynthetic process; IEA:InterPro.
DR CDD; cd00609; AAT_like; 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; 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:SF1; HTH-TYPE TRANSCRIPTIONAL REGULATORY PROTEIN GABR; 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:KJL38864.1};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000033956};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Transferase {ECO:0000313|EMBL:KJL38864.1}.
FT DOMAIN 21..89
FT /note="HTH gntR-type"
FT /evidence="ECO:0000259|PROSITE:PS50949"
SQ SEQUENCE 473 AA; 50892 MW; C0F3A81471D176E5 CRC64;
MDSRISARAL TAALGGWRTR EPAYEALADG IRLLCLDNRL APRTALPAER ELAHALSVSR
STVAAAYRSL RDSEHIASLR GSGSVTLPLR RRDASRLDAV DGMIDLQQAT PPAWPGLAGV
ISDLASQSAA LVARVGYDVL GRADLREIIA QRYTDRGIVT SPAEVLVTTG AQSAIHLLGS
LLLGRGDRVV IETPTYPHAA ESLRRAGARL VGVPVTVDDG WDLDRAEQAF ARTLPVLAYL
MPDFHNPTGR SMSEIERATI LSAAERSGSV LILDETTAEL DIDRGPLDPG FPGDSEAVVR
IGSLGKTVWG GLRVGWIRAH SDLIRRLVAV RPAHDLGTPE FEQAVAASVL ADFDPVVAQR
GDLLRSGRDR LAAAIAARLP EWTVPRARGG VSLWIELDAP LSTPLVLEAR SRGILLTAGP
RFAVAGGYDR HLRIPFTAPP DDLEYTIDVL AQSWRHVREG APARYLETLD AVV
//
