MBTG_MYCPA
ID MBTG_MYCPA Reviewed; 428 AA.
AC Q73XY8;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 89.
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=MAP_2170c;
OS Mycolicibacterium paratuberculosis (strain ATCC BAA-968 / K-10)
OS (Mycobacterium paratuberculosis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium avium complex (MAC).
OX NCBI_TaxID=262316;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-968 / K-10;
RX PubMed=16116077; DOI=10.1073/pnas.0505662102;
RA Li L., Bannantine J.P., Zhang Q., Amonsin A., May B.J., Alt D., Banerji N.,
RA Kanjilal S., Kapur V.;
RT "The complete genome sequence of Mycobacterium avium subspecies
RT paratuberculosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:12344-12349(2005).
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; AE016958; AAS04487.1; -; Genomic_DNA.
DR RefSeq; WP_003878341.1; NC_002944.2.
DR AlphaFoldDB; Q73XY8; -.
DR SMR; Q73XY8; -.
DR STRING; 262316.MAP_2170c; -.
DR EnsemblBacteria; AAS04487; AAS04487; MAP_2170c.
DR KEGG; mpa:MAP_2170c; -.
DR PATRIC; fig|262316.17.peg.2307; -.
DR eggNOG; COG3486; Bacteria.
DR HOGENOM; CLU_052650_0_0_11; -.
DR OMA; QFAEWVD; -.
DR UniPathway; UPA00011; -.
DR Proteomes; UP000000580; 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; 2.
PE 3: Inferred from homology;
KW FAD; Flavoprotein; Monooxygenase; NADP; Oxidoreductase; Reference proteome;
KW Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..428
FT /note="L-lysine N6-monooxygenase MbtG"
FT /id="PRO_0000261310"
SQ SEQUENCE 428 AA; 46532 MW; 44C8EE39A4AFA801 CRC64;
MSTLAILGAG AKAVAVAAKA SVLRDMGVEV PDVVAVERIG VAANWQASGG WTDGAHRLGT
SPEKDVGFPY RSALVPRRNA ELDERMTRYS WQSYLIATAS FAEWIDRGRP APTHRRWSQY
LSWVADHVGM TVVHGEVEQL AVTGDRWALH THETTVHADA LMITGPGQAE KSLLPGNPRM
LSIAQFWDRA ANHDRISAER VAVIGGGETA AAMLNELFRH RVSSITVISP QATLFTRGEG
YFENSLFSDP TNWPALTLAE RRDALARTDR GVFSSSVQEA LLADDRIHHL RGRVTHAVGV
QGQIRLTLST NRGSENLETV HGFDLVIDGS GADSLWFAPL FSQEALDLLE LGLGGPLSSE
RLQEAIGYDL AVTDVTPKLF LPNLSGLTQG PGFPNLSCLG LLSDRVLGST LGPTNYPARR
RHDERQPL