ID A0A1G8FFZ6_9NOCA Unreviewed; 446 AA.
AC A0A1G8FFZ6;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=L-lysine 6-transaminase {ECO:0000256|ARBA:ARBA00013071};
DE EC=2.6.1.36 {ECO:0000256|ARBA:ARBA00013071};
DE AltName: Full=Lysine 6-aminotransferase {ECO:0000256|ARBA:ARBA00030921};
GN ORFNames=SAMN05444695_103271 {ECO:0000313|EMBL:SDH80972.1};
OS Rhodococcus triatomae.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=300028 {ECO:0000313|EMBL:SDH80972.1, ECO:0000313|Proteomes:UP000183263};
RN [1] {ECO:0000313|EMBL:SDH80972.1, ECO:0000313|Proteomes:UP000183263}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44892 {ECO:0000313|EMBL:SDH80972.1,
RC ECO:0000313|Proteomes:UP000183263};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-lysine = (S)-2-amino-6-oxohexanoate + L-
CC glutamate; Xref=Rhea:RHEA:21200, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:32551, ChEBI:CHEBI:58321; EC=2.6.1.36;
CC Evidence={ECO:0000256|ARBA:ARBA00001087};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00008954,
CC ECO:0000256|RuleBase:RU003560}.
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; FNDN01000003; SDH80972.1; -; Genomic_DNA.
DR RefSeq; WP_072736550.1; NZ_FNDN01000003.1.
DR AlphaFoldDB; A0A1G8FFZ6; -.
DR OrthoDB; 9801052at2; -.
DR Proteomes; UP000183263; Unassembled WGS sequence.
DR GO; GO:0045484; F:L-lysine 6-transaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:InterPro.
DR CDD; cd00610; OAT_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; IPR005814; Aminotrans_3.
DR InterPro; IPR049704; Aminotrans_3_PPA_site.
DR InterPro; IPR017657; L-lysine_6-transaminase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR03251; LAT_fam; 1.
DR PANTHER; PTHR43206:SF2; 4-AMINOBUTYRATE AMINOTRANSFERASE GABT; 1.
DR PANTHER; PTHR43206; AMINOTRANSFERASE; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000256|ARBA:ARBA00022576};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000183263};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
SQ SEQUENCE 446 AA; 49274 MW; 830ABEC90FF300C3 CRC64;
MSTAIDLRGK NPGLPADRVH DVLGASILAD GFDLVLDLDE SRGSWLVDLR DGSRYLDMFS
FFASSALGMN HPDLTEERFL AELAAVAVNK PSNSDVYSVP MAQFVETFVR VLGDPRLPHL
FFVEGGGLAV ENALKAAFDW KSRLEENRGH GPACGTRVLH LTEAFHGRTG YTMSLTNTEP
IKTDRFPKFD WPRIPAPYLA DGRDVAADER HALARAAAAF EEFPRDIACF LAEPIQGEGG
DHHFRPEFLQ QMQRLCHEHD ALFVLDEVQT GCGLTGSTWA YRQLGLEPDI VAFGKKTQVC
GIMAGGRLDE VADNVFTVSS RLNSTWGGNL TDMVRARRVL EVIERDGLVD RAARLGRHLL
GGLEELAARH PEVTEPRGRG LMCAFTLPST RRRDEVVTTL REREHVLILP TGKRAIRFRP
PLTVSTGELD AALDAVSRVL RGTVQV
//
