ID Q47NR7_THEFY Unreviewed; 438 AA.
AC Q47NR7;
DT 13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2005, sequence version 1.
DT 27-MAR-2024, entry version 108.
DE RecName: Full=L-lysine N6-monooxygenase MbtG {ECO:0000256|ARBA:ARBA00016406};
DE EC=1.14.13.59 {ECO:0000256|ARBA:ARBA00013076};
DE AltName: Full=Lysine 6-N-hydroxylase {ECO:0000256|ARBA:ARBA00032738};
DE AltName: Full=Lysine N6-hydroxylase {ECO:0000256|ARBA:ARBA00032493};
DE AltName: Full=Lysine-N-oxygenase {ECO:0000256|ARBA:ARBA00029939};
DE AltName: Full=Mycobactin synthase protein G {ECO:0000256|ARBA:ARBA00031158};
GN OrderedLocusNames=Tfu_1869 {ECO:0000313|EMBL:AAZ55902.1};
OS Thermobifida fusca (strain YX).
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Nocardiopsaceae; Thermobifida.
OX NCBI_TaxID=269800 {ECO:0000313|EMBL:AAZ55902.1};
RN [1] {ECO:0000313|EMBL:AAZ55902.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=YX {ECO:0000313|EMBL:AAZ55902.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Di Bartolo G., Chain P., Schmutz J.,
RA Larimer F., Land M., Lykidis A., Richardson P.;
RT "Complete sequence of Thermobifida fusca YX.";
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
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 Evidence={ECO:0000256|ARBA:ARBA00000168};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- PATHWAY: Siderophore biosynthesis. {ECO:0000256|ARBA:ARBA00004924}.
CC -!- SIMILARITY: Belongs to the lysine N(6)-hydroxylase/L-ornithine N(5)-
CC oxygenase family. {ECO:0000256|ARBA:ARBA00007588}.
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; CP000088; AAZ55902.1; -; Genomic_DNA.
DR AlphaFoldDB; Q47NR7; -.
DR STRING; 269800.Tfu_1869; -.
DR KEGG; tfu:Tfu_1869; -.
DR eggNOG; COG3486; Bacteria.
DR HOGENOM; CLU_020931_2_0_11; -.
DR OrthoDB; 7527071at2; -.
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; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR025700; Lys/Orn_oxygenase.
DR PANTHER; PTHR42802:SF1; L-ORNITHINE N(5)-MONOOXYGENASE; 1.
DR PANTHER; PTHR42802; MONOOXYGENASE; 1.
DR Pfam; PF13434; Lys_Orn_oxgnase; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
PE 3: Inferred from homology;
KW Monooxygenase {ECO:0000313|EMBL:AAZ55902.1};
KW Oxidoreductase {ECO:0000313|EMBL:AAZ55902.1}.
SQ SEQUENCE 438 AA; 49054 MW; 11F606F6A6E3A533 CRC64;
MTPSLDHEVS DTSERPVHDL VGVGFGPSNL GLAIALRERR AAGGKAPTGL FLERQERFSW
HQGMLLDDAT MQISFLKDLV TPRNPASDFS FLSFLHRMGR LHDFINHKTL FPLRAEFHDY
LVWCAQRVSD QVRYGQHVVA LRPVTRHGKV VYLDVVARDT AGRETVERAR NVVLAPGLRP
SMPEGVHPSD RVWHSEHLLH RLADLPAAPV HGFAVVGAGQ SAAEVVGHLH QRFADLPVHA
VFSRYGYSPS DDTPFANRIF DPEAVDAYYD APQEFKDELM HYHRNTNYSA VDPDLIAELY
RRFYAERVRG KPRLQIHNMT RVVALTETDD RVDLTLEDQV SGKQTVLTVD HVVYATGYQP
VDIRPLLGDL GHHCVFDAAG RPSLQRDYRI VTDDTVTCGL YLQGGTEHTH GISSVLLSNV
ATRAAEIIDS IEARRATS
//
