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Database: UniProt
Entry: A0A166RUH8_9ACTN
LinkDB: A0A166RUH8_9ACTN
Original site: A0A166RUH8_9ACTN 
ID   A0A166RUH8_9ACTN        Unreviewed;       500 AA.
AC   A0A166RUH8;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 26.
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=UG55_10098 {ECO:0000313|EMBL:OAA27127.1};
OS   Frankia sp. EI5c.
OC   Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae; Frankia.
OX   NCBI_TaxID=683316 {ECO:0000313|EMBL:OAA27127.1, ECO:0000313|Proteomes:UP000077018};
RN   [1] {ECO:0000313|EMBL:OAA27127.1, ECO:0000313|Proteomes:UP000077018}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EI5c {ECO:0000313|EMBL:OAA27127.1,
RC   ECO:0000313|Proteomes:UP000077018};
RX   PubMed=27389275;
RA   D'Angelo T., Oshone R., Abebe-Akele F., Simpson S., Morris K., Thomas W.K.,
RA   Tisa L.S.;
RT   "Permanent Draft Genome Sequence for Frankia sp. Strain EI5c, a Single-
RT   Spore Isolate of a Nitrogen-Fixing Actinobacterium, Isolated from the Root
RT   Nodules of Elaeagnus angustifolia.";
RL   Genome Announc. 4:e00660-16(2016).
RN   [2] {ECO:0000313|EMBL:OAA27127.1, ECO:0000313|Proteomes:UP000077018}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EI5c {ECO:0000313|EMBL:OAA27127.1,
RC   ECO:0000313|Proteomes:UP000077018};
RA   Wen L., He K., Yang H.;
RL   Submitted (FEB-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; mycobactin biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00005102}.
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:OAA27127.1}.
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DR   EMBL; LRTK01000009; OAA27127.1; -; Genomic_DNA.
DR   STRING; 683316.UG55_10098; -.
DR   PATRIC; fig|683316.3.peg.1659; -.
DR   Proteomes; UP000077018; Unassembled WGS sequence.
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   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:OAA27127.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077018}.
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          456..500
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        470..487
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   500 AA;  53736 MW;  C59B083B4E7A48CB CRC64;
     MTSSSPAAGA ALPGDPPDHP PXHLPAEVPA ARTEPYDLLG VGLGPFNLSL AALADGVPGL
     RAVFLDQAES FHWHPXLLLD GTSLQVPFLA DLVTLVDPTS RWSFLSYLRE HDRLFRFYFY
     ERFHLPRREY DDYCGWVARG LPSTRFGSRV ESVSWDPATA LFQVTVTASA GGPRRITIIA
     ARNLVLGIGT EPATPAAFGG VLGPRVFHSA EYGPRRGELA GARHVTVVGS GQSGAEVFAD
     LLRSQPATGH SLAWITRTPA FAXMEYSKLG LEQFTPDYVR YFHGLDQRTK DALVPGQWQL
     YKGIDAQTIA EIYDLLYERS IGGAEPDALL LPNVSVAAVT SPGAGHAYTL RCRHQGQHRE
     FAVGTDAVVL ATGYAPRRPA LLDPLAHLLD LDTAGRFKVD ERYRVATAPE LTGRIHVQNA
     ELHTHGVGAP DLGLGAWRAA VILDDLTGGR AYRLPRPTAF TTFGSPEQPS APAPASPPSP
     GHRAGEPVPP QPADLGGAGR
//
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