ID A0A0E3XTX8_MYCCH Unreviewed; 434 AA.
AC A0A0E3XTX8;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=GR01_17735 {ECO:0000313|EMBL:AKC41559.1};
OS Mycobacteroides chelonae (Mycobacterium chelonae).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacteroides.
OX NCBI_TaxID=1774 {ECO:0000313|EMBL:AKC41559.1, ECO:0000313|Proteomes:UP000033056};
RN [1] {ECO:0000313|EMBL:AKC41559.1, ECO:0000313|Proteomes:UP000033056}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35752 {ECO:0000313|EMBL:AKC41559.1,
RC ECO:0000313|Proteomes:UP000033056};
RX PubMed=26021923;
RA Hasan N.A., Davidson R.M., de Moura V.C., Garcia B.J., Reynolds P.R.,
RA Epperson L.E., Farias-Hesson E., DeGroote M.A., Jackson M., Strong M.;
RT "Draft Genome Sequence of Mycobacterium chelonae Type Strain ATCC 35752.";
RL Genome Announc. 3:e00536-15(2015).
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}.
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DR EMBL; CP010946; AKC41559.1; -; Genomic_DNA.
DR RefSeq; WP_046255958.1; NZ_MLCH01000004.1.
DR AlphaFoldDB; A0A0E3XTX8; -.
DR GeneID; 31681189; -.
DR PATRIC; fig|1774.35.peg.3602; -.
DR HOGENOM; CLU_016922_10_1_11; -.
DR Proteomes; UP000033056; Chromosome.
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 ECO:0000313|EMBL:AKC41559.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AKC41559.1}.
SQ SEQUENCE 434 AA; 48097 MW; 82880B3684F560B3 CRC64;
MTPDRVHEVL RRSILADGMD LVLDLERSRG AHLVDARDGT TYLDMFTFFA SSALGMNHPM
LAEDGEFRAE LTRAAINKPS NSDIYTVEMA RFVDTFARVL GDPALPHLFF VDGGALAVEN
ALKVAFDWKS RWNEAHGIDP ALGTKVLHLR EAFHGRSGYT MSLTNTDPNK VARFPKFDWP
RIDAPYLRPD ADIEELEAAA LAQARRVFAE NPHDIACFIA EPIQGEGGDH HFRPDFFHAM
RALCHENDAL FVFDEVQTGC GLTGTAWAFQ QLGVTPDIVA FGKKTQVCGV MAGGRVDEVA
DNVFAVSSRI NSTWGGNLVD MVRSRRILEV IESQRLFGNA ARMGEYLLDR LQTLALRHGE
IGDVRGRGLM CAFSLPTTQE RDHLVERLWS QERVILLPSG KNSVRFRPPL IVSAEEIDAA
VAAVSRVLAQ SPQA
//
