LAT_MYCTU
ID LAT_MYCTU Reviewed; 449 AA.
AC P9WQ77; 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 39.
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=Rv3290c; ORFNames=MTCY71.30;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].
RX PubMed=19099550; DOI=10.1186/1752-0509-2-109;
RA Raman K., Yeturu K., Chandra N.;
RT "targetTB: a target identification pipeline for Mycobacterium tuberculosis
RT through an interactome, reactome and genome-scale structural analysis.";
RL BMC Syst. Biol. 2:109-109(2008).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
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 -!- MISCELLANEOUS: Was identified as a high-confidence drug target.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; AL123456; CCP46109.1; -; Genomic_DNA.
DR PIR; C70981; C70981.
DR RefSeq; NP_217807.1; NC_000962.3.
DR RefSeq; WP_003900004.1; NZ_NVQJ01000003.1.
DR PDB; 2CIN; X-ray; 1.98 A; A=1-449.
DR PDB; 2CJD; X-ray; 2.00 A; A=1-449.
DR PDB; 2CJG; X-ray; 1.95 A; A=1-449.
DR PDB; 2CJH; X-ray; 2.00 A; A=1-449.
DR PDB; 2JJE; X-ray; 2.20 A; A=1-449.
DR PDB; 2JJF; X-ray; 1.95 A; A=1-449.
DR PDB; 2JJG; X-ray; 2.40 A; A=1-449.
DR PDB; 2JJH; X-ray; 2.70 A; A=1-449.
DR PDBsum; 2CIN; -.
DR PDBsum; 2CJD; -.
DR PDBsum; 2CJG; -.
DR PDBsum; 2CJH; -.
DR PDBsum; 2JJE; -.
DR PDBsum; 2JJF; -.
DR PDBsum; 2JJG; -.
DR PDBsum; 2JJH; -.
DR AlphaFoldDB; P9WQ77; -.
DR SMR; P9WQ77; -.
DR STRING; 83332.Rv3290c; -.
DR BindingDB; P9WQ77; -.
DR ChEMBL; CHEMBL2259247; -.
DR DrugBank; DB08071; (2S)-1-methyl-2-[(2S,4R)-2-methyl-4-phenylpentyl]piperidine.
DR PaxDb; P9WQ77; -.
DR DNASU; 887904; -.
DR GeneID; 887904; -.
DR KEGG; mtu:Rv3290c; -.
DR TubercuList; Rv3290c; -.
DR eggNOG; COG0160; Bacteria.
DR OMA; DPPDMVT; -.
DR PhylomeDB; P9WQ77; -.
DR BRENDA; 2.6.1.36; 3445.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0003867; F:4-aminobutyrate transaminase activity; IBA:GO_Central.
DR GO; GO:0045484; F:L-lysine 6-transaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:InterPro.
DR GO; GO:0009450; P:gamma-aminobutyric acid catabolic process; IBA:GO_Central.
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 3D-structure; Aminotransferase; Pyridoxal phosphate; Reference proteome;
KW Transferase.
FT CHAIN 1..449
FT /note="Probable L-lysine-epsilon aminotransferase"
FT /id="PRO_0000120512"
FT MOD_RES 300
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255"
FT HELIX 17..19
FT /evidence="ECO:0007829|PDB:2CJG"
FT HELIX 20..25
FT /evidence="ECO:0007829|PDB:2CJG"
FT TURN 39..41
FT /evidence="ECO:0007829|PDB:2CJG"
FT STRAND 46..49
FT /evidence="ECO:0007829|PDB:2CJG"
FT TURN 50..52
FT /evidence="ECO:0007829|PDB:2CJG"
FT STRAND 55..60
FT /evidence="ECO:0007829|PDB:2CJG"
FT HELIX 61..64
FT /evidence="ECO:0007829|PDB:2CJG"
FT HELIX 73..76
FT /evidence="ECO:0007829|PDB:2CJG"
FT HELIX 79..89
FT /evidence="ECO:0007829|PDB:2CJG"
FT TURN 95..97
FT /evidence="ECO:0007829|PDB:2CJG"
FT HELIX 101..114
FT /evidence="ECO:0007829|PDB:2CJG"
FT STRAND 121..127
FT /evidence="ECO:0007829|PDB:2CJG"
FT HELIX 128..149
FT /evidence="ECO:0007829|PDB:2CJG"
FT STRAND 159..163
FT /evidence="ECO:0007829|PDB:2CJG"
FT HELIX 174..176
FT /evidence="ECO:0007829|PDB:2CJG"
FT HELIX 182..185
FT /evidence="ECO:0007829|PDB:2CJG"
FT HELIX 207..227
FT /evidence="ECO:0007829|PDB:2CJG"
FT TURN 229..231
FT /evidence="ECO:0007829|PDB:2CJG"
FT STRAND 232..237
FT /evidence="ECO:0007829|PDB:2CJG"
FT STRAND 239..241
FT /evidence="ECO:0007829|PDB:2CJG"
FT TURN 242..245
FT /evidence="ECO:0007829|PDB:2CJG"
FT STRAND 246..248
FT /evidence="ECO:0007829|PDB:2JJH"
FT HELIX 251..263
FT /evidence="ECO:0007829|PDB:2CJG"
FT STRAND 267..271
FT /evidence="ECO:0007829|PDB:2CJG"
FT TURN 273..280
FT /evidence="ECO:0007829|PDB:2CJG"
FT STRAND 281..284
FT /evidence="ECO:0007829|PDB:2CJG"
FT HELIX 286..289
FT /evidence="ECO:0007829|PDB:2CJG"
FT STRAND 294..298
FT /evidence="ECO:0007829|PDB:2CJG"
FT HELIX 300..302
FT /evidence="ECO:0007829|PDB:2CJG"
FT STRAND 303..309
FT /evidence="ECO:0007829|PDB:2CJG"
FT HELIX 311..315
FT /evidence="ECO:0007829|PDB:2CJG"
FT TURN 320..322
FT /evidence="ECO:0007829|PDB:2CJG"
FT STRAND 330..333
FT /evidence="ECO:0007829|PDB:2CJG"
FT HELIX 335..351
FT /evidence="ECO:0007829|PDB:2CJG"
FT HELIX 353..374
FT /evidence="ECO:0007829|PDB:2CJG"
FT TURN 376..378
FT /evidence="ECO:0007829|PDB:2CJG"
FT STRAND 379..385
FT /evidence="ECO:0007829|PDB:2CJG"
FT STRAND 388..392
FT /evidence="ECO:0007829|PDB:2CJG"
FT HELIX 396..408
FT /evidence="ECO:0007829|PDB:2CJG"
FT STRAND 414..416
FT /evidence="ECO:0007829|PDB:2CJG"
FT TURN 417..419
FT /evidence="ECO:0007829|PDB:2CJG"
FT STRAND 420..423
FT /evidence="ECO:0007829|PDB:2CJG"
FT HELIX 431..448
FT /evidence="ECO:0007829|PDB:2CJG"
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
