ID   MBTG_MYCTU              Reviewed;         431 AA.
AC   O05820; Q7D793;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   16-JUN-2009, entry version 49.
DE   RecName: Full=L-lysine 6-monooxygenase mbtG;
DE            EC=1.14.13.59;
DE   AltName: Full=Lysine 6-N-hydroxylase;
DE   AltName: Full=Lysine N(6)-hydroxylase;
DE   AltName: Full=Lysine-N-oxygenase;
DE   AltName: Full=Mycobactin synthetase protein G;
DE   Flags: Precursor;
GN   Name=mbtG; OrderedLocusNames=Rv2378c, MT2446;
OS   Mycobacterium tuberculosis.
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Corynebacterineae; Mycobacteriaceae; Mycobacterium;
OC   Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=1773;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   MEDLINE=98295987; PubMed=9634230; DOI=10.1038/31159;
RA   Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M.,
RA   Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III,
RA   Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T.,
RA   Connor R., Davies R.M., Devlin K., Feltwell T., Gentles S., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S.,
RA   Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A.,
RA   Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R.,
RA   Sulston J.E., Taylor K., Whitehead S., Barrell B.G.;
RT   "Deciphering the biology of Mycobacterium tuberculosis from the
RT   complete genome sequence.";
RL   Nature 393:537-544(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   MEDLINE=22206494; PubMed=12218036;
RX   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.,
RA   Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D.,
RA   Salzberg S.L., Delcher A., Utterback T.R., Weidman J.F., Khouri H.M.,
RA   Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C.,
RA   Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
RN   [3]
RP   ROLE IN MYCOBACTIN BIOSYNTHESIS.
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
RT   the biosynthetic enzymes for assembly of the virulence-conferring
RT   siderophore mycobactin.";
RL   Chem. Biol. 5:631-645(1998).
RN   [4]
RP   FUNCTION, AND COFACTOR.
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=16461464; DOI=10.1073/pnas.0507924103;
RA   Krithika R., Marathe U., Saxena P., Ansari M.Z., Mohanty D.,
RA   Gokhale R.S.;
RT   "A genetic locus required for iron acquisition in Mycobacterium
RT   tuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:2069-2074(2006).
CC   -!- FUNCTION: Flavoprotein monooxygenase required for N-hydroxylation
CC       of the two acylated lysine residues during mycobactin assembly,
CC       thus producing the hydroxamate groups necessary for iron
CC       sequestration. Is also able, but less efficiently, to hydroxylate
CC       L-lysine (non acylated) in vitro.
CC   -!- CATALYTIC ACTIVITY: L-lysine + NADPH + O(2) = N(6)-hydroxy-L-
CC       lysine + NADP(+) + H(2)O.
CC   -!- COFACTOR: FAD.
CC   -!- PATHWAY: Siderophore biosynthesis; mycobactin biosynthesis.
CC   -!- INDUCTION: Induced by iron starvation conditions and during
CC       infection of human THP-1 macrophages. Transcriptionally repressed
CC       by ideR and iron (By similarity).
CC   -!- SIMILARITY: Belongs to the lysine N(6)-hydroxylase/L-ornithine
CC       N(5)-oxygenase family.
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DR   EMBL; BX842579; CAB08475.1; -; Genomic_DNA.
DR   EMBL; AE000516; AAK46741.1; -; Genomic_DNA.
DR   PIR; A70588; A70588.
DR   RefSeq; NP_216894.1; -.
DR   RefSeq; NP_336927.1; -.
DR   GeneID; 885648; -.
DR   GeneID; 925901; -.
DR   GenomeReviews; AE000516_GR; MT2446.
DR   GenomeReviews; AL123456_GR; Rv2378c.
DR   KEGG; mtc:MT2446; -.
DR   KEGG; mtu:Rv2378c; -.
DR   TIGR; MT2446; -.
DR   TubercuList; Rv2378c; -.
DR   HOGENOM; O05820; -.
DR   OMA; O05820; SIAQFWH.
DR   BRENDA; 1.14.13.59; 809.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0047091; F:L-lysine 6-monooxygenase (NADPH) activity; IEA:EC.
DR   GO; GO:0006826; P:iron ion transport; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
PE   2: Evidence at transcript level;
KW   Complete proteome; FAD; Flavoprotein; Ion transport; Iron;
KW   Iron transport; Monooxygenase; NADP; Oxidoreductase; Signal;
KW   Transport.
FT   SIGNAL        1     21       Potential.
FT   CHAIN        22    431       L-lysine 6-monooxygenase mbtG.
FT                                /FTId=PRO_0000261312.
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
//