ID W5TFD3_9NOCA Unreviewed; 454 AA.
AC W5TFD3;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
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=NONO_c11440 {ECO:0000313|EMBL:AHH15951.1};
OS Nocardia nova SH22a.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Nocardia.
OX NCBI_TaxID=1415166 {ECO:0000313|EMBL:AHH15951.1, ECO:0000313|Proteomes:UP000019150};
RN [1] {ECO:0000313|EMBL:AHH15951.1, ECO:0000313|Proteomes:UP000019150}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SH22a {ECO:0000313|EMBL:AHH15951.1};
RX PubMed=24747905;
RA Luo Q., Hiessl S., Poehlein A., Daniel R., Steinbuchel A.;
RT "Insights into the Microbial Degradation of Rubber and Gutta-Percha by
RT Analysis of the Complete Genome of Nocardia nova SH22a.";
RL Appl. Environ. Microbiol. 80:3895-3907(2014).
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; CP006850; AHH15951.1; -; Genomic_DNA.
DR AlphaFoldDB; W5TFD3; -.
DR STRING; 1415166.NONO_c11440; -.
DR KEGG; nno:NONO_c11440; -.
DR PATRIC; fig|1415166.3.peg.1161; -.
DR eggNOG; COG0160; Bacteria.
DR HOGENOM; CLU_016922_10_1_11; -.
DR OrthoDB; 9801052at2; -.
DR Proteomes; UP000019150; 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; 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.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000256|ARBA:ARBA00022576,
KW ECO:0000313|EMBL:AHH15951.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000019150};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AHH15951.1}.
SQ SEQUENCE 454 AA; 49858 MW; 8A39D7B4B8673A0D CRC64;
MTLELERPGT TDAVVTDPAP VAASRVHEIL SGHILADGFD IVLDLRKSQG RRLVDARDGT
TYLDMFGFFA SSALGMNHPA LADDESFRAE LTVAALNKPS NSDIYTVEMA RFVDTFARVL
GDPALPHLFF IDGGALAVEN ALKVAFDWKS RHNAMHSRPA DLGTRVLHLT GAFHGRTGYT
MSLTNTDPIK TDRFPKFGWP RIETPYLCPG ADIEAAESRA LAQAEAAFAE NPHDIACFIA
EPIQGEGGDR HLRPEFLRRM QQLCHDHDAL FILDEVQTGV AMTGTIWAYQ QLGLRPDVVA
FGKKTQVCGI MAGGRVDEVP GNVFETSSRL NSTWGGNLAD MVRARRILEV IESERLADRA
KDLGALLLDR LRELAERHDA LTDPRGRGLM CAVTLASPEL RDAVLAEALE REHVLLLGSG
ARGIRFRPPL TVTADELEEA VAALDRVLDR HRDE
//
