ID Q73UF8_MYCPA Unreviewed; 446 AA.
AC Q73UF8;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 99.
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 Name=lat {ECO:0000313|EMBL:AAS05960.1};
GN OrderedLocusNames=MAP_3410c {ECO:0000313|EMBL:AAS05960.1};
OS Mycolicibacterium paratuberculosis (strain ATCC BAA-968 / K-10)
OS (Mycobacterium paratuberculosis).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium avium complex (MAC).
OX NCBI_TaxID=262316 {ECO:0000313|EMBL:AAS05960.1, ECO:0000313|Proteomes:UP000000580};
RN [1] {ECO:0000313|EMBL:AAS05960.1, ECO:0000313|Proteomes:UP000000580}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-968 / K-10 {ECO:0000313|Proteomes:UP000000580};
RX PubMed=16116077; DOI=10.1073/pnas.0505662102;
RA Li L., Bannantine J.P., Zhang Q., Amonsin A., May B.J., Alt D., Banerji N.,
RA Kanjilal S., Kapur V.;
RT "The complete genome sequence of Mycobacterium avium subspecies
RT paratuberculosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:12344-12349(2005).
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; AE016958; AAS05960.1; -; Genomic_DNA.
DR RefSeq; WP_010949951.1; NZ_CP106873.1.
DR AlphaFoldDB; Q73UF8; -.
DR STRING; 262316.MAP_3410c; -.
DR KEGG; mpa:MAP_3410c; -.
DR PATRIC; fig|262316.17.peg.3625; -.
DR eggNOG; COG0160; Bacteria.
DR HOGENOM; CLU_016922_10_1_11; -.
DR Proteomes; UP000000580; 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 Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000000580};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
SQ SEQUENCE 446 AA; 48981 MW; A1C0790C02CA9C4A CRC64;
MTAALERLAR ARSCTGPDRV HEVLSRSILT DGFDFVLDLD RSRGSVLYDA RDGRRYLDMF
TFFASSALGM NHPALARDAE FRAELAAAAL NKPSNSDVYS VPMARFVETF VRVLGDPALP
HLFFVDGGAL AVENALKVAF DWKSRHNERR GVDPALGTRV LHLRGAFHGR SGHTLSLTNT
KPVTVARFPR FDWPRIDAPH LRCGADIDAL EAESLRQARA AFAAHPHDIA CFIAEPIQGE
GGDRHFRPEF FAAMRRLCDE HDALLIFDEV QTGCGLTGTA WAYHQFGVQP DVVAFGKKTQ
VCGIMAGRRV DEVADNVFAV SSRLNSTWGG NLADMVRARR ILEVIEADEL FEHAARQGAY
LLRGLHDLAR EFPGLVLDVR GRGLMCAFSL PTTADRDELI GRLWRGGVIV LPTGDDGVRF
RPALTVSRGE IDAAIGAVRD ALPTLG
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