ID   LAT_AMYLA               Reviewed;         450 AA.
AC   Q05174;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=L-lysine-epsilon aminotransferase;
DE            Short=L-lysine aminotransferase;
DE            EC=2.6.1.36;
DE   AltName: Full=Lysine 6-aminotransferase;
GN   Name=lat;
OS   Amycolatopsis lactamdurans (Nocardia lactamdurans).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Amycolatopsis.
OX   NCBI_TaxID=1913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1917857; DOI=10.1128/jb.173.19.6258-6264.1991;
RA   Coque J., Liras P., Laiz L., Martin J.;
RT   "A gene encoding lysine 6-aminotransferase, which forms the beta-lactam
RT   precursor alpha-aminoadipic acid, is located in the cluster of cephamycin
RT   biosynthetic genes in Nocardia lactamdurans.";
RL   J. Bacteriol. 173:6258-6264(1991).
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   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC   -!- PATHWAY: Antibiotic biosynthesis; cephamycin C biosynthesis.
CC   -!- SUBUNIT: Active as either a monomer or a homomer.
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
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DR   EMBL; Z21681; CAA79796.1; -; Genomic_DNA.
DR   PIR; A38171; A38171.
DR   AlphaFoldDB; Q05174; -.
DR   SMR; Q05174; -.
DR   UniPathway; UPA00183; -.
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:UniProtKB-KW.
DR   CDD; cd00610; OAT_like; 1.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR005814; Aminotrans_3.
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   Pfam; PF00202; Aminotran_3; 1.
DR   PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR03251; LAT_fam; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   3: Inferred from homology;
KW   Aminotransferase; Antibiotic biosynthesis; Pyridoxal phosphate;
KW   Transferase.
FT   CHAIN           1..450
FT                   /note="L-lysine-epsilon aminotransferase"
FT                   /id="PRO_0000120510"
FT   MOD_RES         300
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   450 AA;  48806 MW;  C24915CAF2E93EE5 CRC64;
     MVLEMPAARV PAGPDARDVR QALARHVLTD GYDLVLDLEA SAGPWLVDAV TGTRYLDLFS
     FFASAPLGIN PSCIVDDPAF VGELAAAAVN KPSNPDVYTV PYAKFVTTFA RVLGDPLLPH
     LFFVDGGALA VENALKAAFD WKAQKLGLDD RAVNRLQVLH LERSFHGRSG YTMSLTNTDP
     SKTARYPKFD WPRIPAPALE HPLTTHAEAN REAERRALEA AEEAFRAADG MIACFLAEPI
     QGEGGDNHFS AEFLQAMQDL CHRHDALFVL DEVQSGCGLT GTAWAYQQLG LRPDLVAFGK
     KTQVCGVMGG GRIGEVESNV FAVSSRISST WGGNLADMVR ATRVLETIER TDLLDSVVQR
     GKYLRDGLEA LAERHPGVVT NARGRGLMCA VDLPDTEQRD AVLRRMYTGH QVIALPCGTR
     GLRFRPPLTV TESELDQGLE ALAASLASRG