ID A0A0M5LUN8_9PSEU Unreviewed; 452 AA.
AC A0A0M5LUN8;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
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=XF36_26580 {ECO:0000313|EMBL:ALE86262.1};
OS Pseudonocardia sp. HH130629-09.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Pseudonocardia.
OX NCBI_TaxID=1641402 {ECO:0000313|EMBL:ALE86262.1, ECO:0000313|Proteomes:UP000062082};
RN [1] {ECO:0000313|EMBL:ALE86262.1, ECO:0000313|Proteomes:UP000062082}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HH130629-09 {ECO:0000313|EMBL:ALE86262.1,
RC ECO:0000313|Proteomes:UP000062082};
RX PubMed=26438860; DOI=10.1073/pnas.1515348112;
RA Sit C.S., Van Arnam E.B., Ramadhar T.R.;
RT "Variable genetic architectures produce virtually identical molecules in
RT bacterial symbionts of fungus-growing ants.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:13150-13154(2015).
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}.
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DR EMBL; CP011868; ALE86262.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M5LUN8; -.
DR KEGG; pseh:XF36_26580; -.
DR PATRIC; fig|1641402.3.peg.5692; -.
DR OrthoDB; 7527071at2; -.
DR Proteomes; UP000062082; 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; 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 SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
PE 3: Inferred from homology;
KW Monooxygenase {ECO:0000313|EMBL:ALE86262.1};
KW Oxidoreductase {ECO:0000313|EMBL:ALE86262.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000062082}.
SQ SEQUENCE 452 AA; 50947 MW; 372A8E35C026FF17 CRC64;
MCTCKSDVYD VVGIGFGPSN LSLAIALGEH QGNRAGHPVK AAFFERQQSF GWHRNMLLPE
TTMQISFMKD LVTFRNPRSR FSFVNYLHES GRLTQFCNNQ DFFPTRQEFH RYLEWVGSSF
DDQVSYDSEV LGVTLAPEPC ECAQLYLKLE ISNGAIGATE IVNARNISIS TGLVPKVPDN
VPTGDRIWHS SQFLEKLRDV DPADLRNVAV VGGGQSAAEI ARYLHATLPE AQIYAIVPSY
GYSVADDTPF ANQVFDPEAV DDYYFGSDET RDAFWRYHRN TNYSVVDDDI IRDLHRASYA
EQVTGERRLH FLNLTRVRAV TRNGATNRVS LHSLIDRETR ELDIDALVLA TGYTEMTPTG
LIGDVDHFCH RDPEGRYRIE RDYRLMTDPE FPCGIYLQGG TEHTHGLTSS LLSNVAVRGG
EIADSVITRT RADAPTMQRS TRRIEQAWER AG
//
