MBTG_MYCTO
ID MBTG_MYCTO Reviewed; 431 AA.
AC P9WKF6; L0TCC4; O05820; Q7D793;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 37.
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=MT2446;
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).
RN [2]
RP ROLE IN MYCOBACTIN BIOSYNTHESIS, AND PATHWAY.
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=9831524; DOI=10.1016/s1074-5521(98)90291-5;
RA Quadri L.E.N., Sello J., Keating T.A., Weinreb P.H., Walsh C.T.;
RT "Identification of a Mycobacterium tuberculosis gene cluster encoding the
RT biosynthetic enzymes for assembly of the virulence-conferring siderophore
RT mycobactin.";
RL Chem. Biol. 5:631-645(1998).
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.
CC {ECO:0000305|PubMed:9831524}.
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 {ECO:0000269|PubMed:9831524}.
CC -!- SIMILARITY: Belongs to the lysine N(6)-hydroxylase/L-ornithine N(5)-
CC oxygenase family. {ECO:0000305}.
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DR EMBL; AE000516; AAK46741.1; -; Genomic_DNA.
DR PIR; A70588; A70588.
DR RefSeq; WP_003899296.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WKF6; -.
DR SMR; P9WKF6; -.
DR EnsemblBacteria; AAK46741; AAK46741; MT2446.
DR KEGG; mtc:MT2446; -.
DR PATRIC; fig|83331.31.peg.2637; -.
DR HOGENOM; CLU_052650_0_0_11; -.
DR UniPathway; UPA00011; -.
DR Proteomes; UP000001020; 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_0000427662"
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