ID K0VE13_MYCFO Unreviewed; 429 AA.
AC K0VE13;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 39.
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=MFORT_16489 {ECO:0000313|EMBL:EJZ13088.1};
OS Mycolicibacterium fortuitum subsp. fortuitum DSM 46621 = ATCC 6841 = JCM
OS 6387.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=1214102 {ECO:0000313|EMBL:EJZ13088.1, ECO:0000313|Proteomes:UP000006043};
RN [1] {ECO:0000313|EMBL:EJZ13088.1, ECO:0000313|Proteomes:UP000006043}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM46621 {ECO:0000313|Proteomes:UP000006043};
RX PubMed=23105073; DOI=10.1128/JB.01461-12;
RA Ho Y.S., Adroub S.A., Aleisa F., Mahmood H., Othoum G., Rashid F.,
RA Zaher M., Ali S., Bitter W., Pain A., Abdallah A.M.;
RT "Complete Genome Sequence of Mycobacterium fortuitum subsp. fortuitum Type
RT Strain DSM46621.";
RL J. Bacteriol. 194:6337-6338(2012).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EJZ13088.1}.
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DR EMBL; ALQB01000065; EJZ13088.1; -; Genomic_DNA.
DR AlphaFoldDB; K0VE13; -.
DR PATRIC; fig|1214102.3.peg.3270; -.
DR HOGENOM; CLU_016922_10_1_11; -.
DR Proteomes; UP000006043; 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 ECO:0000313|EMBL:EJZ13088.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EJZ13088.1}.
SQ SEQUENCE 429 AA; 47142 MW; FF9B466F7DEB7B67 CRC64;
MRAVLARSIL TDGFDLVLDL DRSRGSYLVD ARTGERFLDM FTFFASSALG MNHPALAEDE
QFRAELAQAA VNKPSNSDIY SVPLARFVDT FRRVLGDPAL PHLFFVDGGA LAVENALKVA
FDWKSRHNES RGIDPALGTK VLHLRGAFHG RSGYTMSLTN TDPVKVARFP KFDWPRIDAP
YLRRGVDIAA LEADSLRQAR AAFEADPHDI ACFIAEPIQG EGGDRHMRPE FFAAMRELCD
EFDALMVFDE VQTGCGITGT SWAYQQLGVA PDVVAFGKKA QVCGVMAGRR VDEVTDNVFS
VSSRINSTWG GNLVDMVRSR RIMEVIEADD LLADVAVTGG HLLAQLDTLA ADFPDTVLDA
RGRGLMCAFS LPSAAARDEL VRRLWDRHVI MLPSGPDSVR FRPALTVTCK EIDACLDAVR
DALRSPLYG
//
