LAT_MYCTO
ID LAT_MYCTO Reviewed; 449 AA.
AC P9WQ76; L0TF67; P63509; P96895;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 25-MAY-2022, entry version 35.
DE RecName: Full=Probable L-lysine-epsilon aminotransferase;
DE Short=L-lysine aminotransferase;
DE EC=2.6.1.36;
DE AltName: Full=Lysine 6-aminotransferase;
GN Name=lat; OrderedLocusNames=MT3389;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
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 Evidence={ECO:0000250};
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; AE000516; AAK47732.1; -; Genomic_DNA.
DR PIR; C70981; C70981.
DR RefSeq; WP_003900004.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WQ76; -.
DR SMR; P9WQ76; -.
DR EnsemblBacteria; AAK47732; AAK47732; MT3389.
DR KEGG; mtc:MT3389; -.
DR PATRIC; fig|83331.31.peg.3647; -.
DR HOGENOM; CLU_016922_10_1_11; -.
DR Proteomes; UP000001020; 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; 3.40.640.10; -; 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; Pyridoxal phosphate; Transferase.
FT CHAIN 1..449
FT /note="Probable L-lysine-epsilon aminotransferase"
FT /id="PRO_0000426824"
FT MOD_RES 300
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 449 AA; 49012 MW; 9A1739F61C6D6049 CRC64;
MAAVVKSVAL AGRPTTPDRV HEVLGRSMLV DGLDIVLDLT RSGGSYLVDA ITGRRYLDMF
TFVASSALGM NPPALVDDRE FHAELMQAAL NKPSNSDVYS VAMARFVETF ARVLGDPALP
HLFFVEGGAL AVENALKAAF DWKSRHNQAH GIDPALGTQV LHLRGAFHGR SGYTLSLTNT
KPTITARFPK FDWPRIDAPY MRPGLDEPAM AALEAEALRQ ARAAFETRPH DIACFVAEPI
QGEGGDRHFR PEFFAAMREL CDEFDALLIF DEVQTGCGLT GTAWAYQQLD VAPDIVAFGK
KTQVCGVMAG RRVDEVADNV FAVPSRLNST WGGNLTDMVR ARRILEVIEA EGLFERAVQH
GKYLRARLDE LAADFPAVVL DPRGRGLMCA FSLPTTADRD ELIRQLWQRA VIVLPAGADT
VRFRPPLTVS TAEIDAAIAA VRSALPVVT