ID A0A176KTW9_9ACTN Unreviewed; 443 AA.
AC A0A176KTW9;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
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 ORFNames=A6P39_37250 {ECO:0000313|EMBL:OAA95768.1};
OS Streptomyces sp. FXJ1.172.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=710705 {ECO:0000313|EMBL:OAA95768.1};
RN [1] {ECO:0000313|EMBL:OAA95768.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FXJ1.172 {ECO:0000313|EMBL:OAA95768.1};
RA Liu M., Liu N., Shang F., Huang Y.;
RT "Activation and identification of NC-1, a novel cryptic cyclodepsipeptide
RT from red soil-derived Streptomyces sp. FXJ1.172.";
RL Submitted (APR-2016) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OAA95768.1}.
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DR EMBL; LWRP01000192; OAA95768.1; -; Genomic_DNA.
DR RefSeq; WP_067055944.1; NZ_CP119133.1.
DR AlphaFoldDB; A0A176KTW9; -.
DR STRING; 710705.A6P39_37250; -.
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 PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
PE 3: Inferred from homology;
KW Monooxygenase {ECO:0000313|EMBL:OAA95768.1};
KW Oxidoreductase {ECO:0000313|EMBL:OAA95768.1}.
SQ SEQUENCE 443 AA; 48576 MW; 633079FF27AB50E6 CRC64;
MGNPRDNFSP VYDVVGIGFG PANLALAIAL EEHNDSAPRD QAVTALFLER QPSFGWHRGM
LIDGATMQVS FLKDLATLRN PTSRFGFVPY LHARGRLVDF INHKILYPTR EEFHDYLEWA
AAGVDHLVSY SSEVTEVRAA GDLLEVVVQG PGGSTVHRAR NVVVACGLRP RMPDGVKPGA
NVWHSSELLT RLAGRTADAR RFVVVGAGQS AAEAAEYLHR TYPQAEVQAV FARYGYSPAD
DSPYANRVFD PEAVDVYYDA DQDAKDRLMA YHRNTNYAVV DLDLIEELYR RAYQEKVRGQ
ARLHIRGVSE VTDVRDEGTG VTLRIRSQAT GTEETVTADA AVFATGYDEQ DPVPLLGPLA
PYVSRDTAGR LRIGRDYRLS LDGPGDAGIY VQGGTEHTHG ITSSLLSMVA VRSGEILRSV
LEHRDAAKDR DDTALALEGA AHD
//
