ID   LAT_STRCL               Reviewed;         457 AA.
AC   Q01767; Q53823;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   03-AUG-2022, entry version 103.
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   Streptomyces clavuligerus.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1901;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 27064 / DSM 738 / JCM 4710 / NBRC 13307 / NCIMB 12785 / NRRL
RC   3585 / VKM Ac-602;
RX   PubMed=1917855; DOI=10.1128/jb.173.19.6223-6229.1991;
RA   Tobin M.B., Kovacevic S., Madduri K., Hoskins J.A., Skatrud P.L.,
RA   Vining L.C., Stuttard C., Miller J.R.;
RT   "Localization of the lysine epsilon-aminotransferase (lat) and delta-(L-
RT   alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase (pcbAB) genes from
RT   Streptomyces clavuligerus and production of lysine epsilon-aminotransferase
RT   activity in Escherichia coli.";
RL   J. Bacteriol. 173:6223-6229(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 27064 / DSM 738 / JCM 4710 / NBRC 13307 / NCIMB 12785 / NRRL
RC   3585 / VKM Ac-602;
RX   PubMed=7881554; DOI=10.1099/13500872-140-12-3367;
RA   Yu H., Serpe E., Romero J., Coque J.J., Maeda K., Oelgeschlager M.,
RA   Hintermann G., Liras P., Martin J.F., Demain A.L., Piret J.;
RT   "Possible involvement of the lysine epsilon-aminotransferase gene (lat) in
RT   the expression of the genes encoding ACV synthetase (pcbAB) and
RT   isopenicillin N synthase (pcbC) in Streptomyces clavuligerus.";
RL   Microbiology 140:3367-3377(1994).
RN   [3]
RP   CHARACTERIZATION.
RC   STRAIN=ATCC 27064 / DSM 738 / JCM 4710 / NBRC 13307 / NCIMB 12785 / NRRL
RC   3585 / VKM Ac-602;
RX   PubMed=9172431; DOI=10.1038/sj.jim.2900370;
RA   Romero J., Martin J.F., Liras P., Demain A.L., Rius N.;
RT   "Partial purification, characterization and nitrogen regulation of the
RT   lysine epsilon-aminotransferase of Streptomyces clavuligerus.";
RL   J. Ind. Microbiol. Biotechnol. 18:241-246(1997).
CC   -!- FUNCTION: Catalyzes the transfer of the terminal amino group of L-
CC       lysine or L-ornithine to alpha-ketoglutarate. Oxaloacetate and pyruvate
CC       can also be used as acceptors of the amino group but with very low
CC       efficiency.
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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 7.0-7.5.;
CC       Temperature dependence:
CC         Optimum temperature is 30 degrees Celsius.;
CC   -!- PATHWAY: Antibiotic biosynthesis; cephamycin C biosynthesis.
CC   -!- SUBUNIT: Active as either a monomer or a homomer.
CC   -!- MISCELLANEOUS: Present only in beta-lactam producing actinomycetes.
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
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DR   EMBL; M64834; AAA26777.1; -; Genomic_DNA.
DR   EMBL; U12015; AAB39899.1; -; Genomic_DNA.
DR   PIR; A38169; A38169.
DR   RefSeq; WP_003952504.1; NZ_CP032052.1.
DR   AlphaFoldDB; Q01767; -.
DR   SMR; Q01767; -.
DR   STRING; 443255.SCLAV_4201; -.
DR   GeneID; 61469718; -.
DR   eggNOG; COG0160; Bacteria.
DR   OrthoDB; 572533at2; -.
DR   BioCyc; MetaCyc:MON-12388; -.
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   1: Evidence at protein level;
KW   Aminotransferase; Antibiotic biosynthesis; Pyridoxal phosphate;
KW   Transferase.
FT   CHAIN           1..457
FT                   /note="L-lysine-epsilon aminotransferase"
FT                   /id="PRO_0000120511"
FT   MOD_RES         304
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        123
FT                   /note="R -> P (in Ref. 2; AAB39899)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        452
FT                   /note="P -> A (in Ref. 2; AAB39899)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   457 AA;  49975 MW;  94C660C027795FAF CRC64;
     MGEAARHPDG DFSDVGNLHA QDVHQALEQH MLVDGYDLVL DLDASSGVWL VDAVTQKRYL
     DLFSFFASAP LGINPPSIVE DPAFMRELAV AAVNKPSNPD LYSVPYARFV KTFARVLGDP
     RLRRLFFVDG GALAVENALK AALDWKAQKL GLAEPDTDRL QVLHLERSFH GRSGYTMSLT
     NTEPSKTARF PKFGWPRISS PALQHPPAEH TGANQEAERR ALEAAREAFA AADGMIACFI
     AEPIQGEGGD NHLSAEFLQA MQRLCHENDA LFVLDEVQSG CGITGTAWAY QQLGLQPDLV
     AFGKKTQVCG VMGGGRIDEV PENVFAVSSR ISSTWGGNLA DMVRATRLLE TIERTQVFDT
     VVQRGKYFRD GLEDLAARHP SVVTNARGRG LMCAVDLPDT RTRNEVLRLM YTEHQVIALP
     CGGRSLRFRP ALTIAEHEID QALQALASSV TPVAESV