MBTG_MYCBO
ID MBTG_MYCBO Reviewed; 431 AA.
AC Q7TYQ9; A0A1R3Y118; X2BKA8;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=L-lysine N6-monooxygenase MbtG;
DE EC=1.14.13.59;
DE AltName: Full=Lysine 6-N-hydroxylase;
DE AltName: Full=Lysine N6-hydroxylase;
DE AltName: Full=Lysine-N-oxygenase;
DE AltName: Full=Mycobactin synthase protein G;
DE Flags: Precursor;
GN Name=mbtG; OrderedLocusNames=BQ2027_MB2399C;
OS Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=233413;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT "The complete genome sequence of Mycobacterium bovis.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA Robbe-Austerman S., Gordon S.V.;
RT "Updated reference genome sequence and annotation of Mycobacterium bovis
RT AF2122/97.";
RL Genome Announc. 5:E00157-E00157(2017).
CC -!- FUNCTION: Flavoprotein monooxygenase required for N-hydroxylation of
CC the two acylated lysine residues during mycobactin assembly, thus
CC producing the hydroxamate groups necessary for iron sequestration. Is
CC also able, but less efficiently, to hydroxylate L-lysine (non acylated)
CC in vitro (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysine + NADPH + O2 = H2O + N(6)-hydroxy-L-lysine + NADP(+);
CC Xref=Rhea:RHEA:23228, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:32551, ChEBI:CHEBI:57783, ChEBI:CHEBI:57820,
CC ChEBI:CHEBI:58349; EC=1.14.13.59;
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC -!- PATHWAY: Siderophore biosynthesis; mycobactin biosynthesis.
CC -!- SIMILARITY: Belongs to the lysine N(6)-hydroxylase/L-ornithine N(5)-
CC oxygenase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LT708304; SIU01011.1; -; Genomic_DNA.
DR RefSeq; NP_856048.1; NC_002945.3.
DR RefSeq; WP_003899296.1; NC_002945.4.
DR AlphaFoldDB; Q7TYQ9; -.
DR SMR; Q7TYQ9; -.
DR EnsemblBacteria; SIU01011; SIU01011; BQ2027_MB2399C.
DR PATRIC; fig|233413.5.peg.2636; -.
DR OMA; QFAEWVD; -.
DR UniPathway; UPA00011; -.
DR Proteomes; UP000001419; Chromosome.
DR GO; GO:0047091; F:L-lysine 6-monooxygenase (NADPH) activity; IEA:UniProtKB-EC.
DR GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR025700; Lys/Orn_oxygenase.
DR Pfam; PF13434; K_oxygenase; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 3: Inferred from homology;
KW FAD; Flavoprotein; Monooxygenase; NADP; Oxidoreductase; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..431
FT /note="L-lysine N6-monooxygenase MbtG"
FT /id="PRO_0000261309"
SQ SEQUENCE 431 AA; 46944 MW; 8D200693CB6D4EB0 CRC64;
MNPTLAVLGA GAKAVAVAAK ASVLRDMGVD VPDVIAVERI GVGANWQASG GWTDGAHRLG
TSPEKDVGFP YRSALVPRRN AELDERMTRY SWQSYLIATA SFAEWIDRGR PAPTHRRWSQ
YLAWVADHIG LKVIHGEVER LAVTGDRWAL CTHETTVQAD ALMITGPGQA EKSLLPGNPR
VLSIAQFWDR AAGHDRINAE RVAVIGGGET AASMLNELFR HRVSTITVIS PQVTLFTRGE
GFFENSLFSD PTDWAALTFD ERRDALARTD RGVFSATVQE ALLADDRIHH LRGRVAHAVG
RQGQIRLTLS TNRGSENFET VHGFDLVIDG SGADPLWFTS LFSQHTLDLL ELGLGGPLTA
DRLQEAIGYD LAVTDVTPKL FLPTLSGLTQ GPGFPNLSCL GLLSDRVLGA GIFTPTKHND
TRRSGEHQSF R