ID A0A1W2FB55_9PSEU Unreviewed; 416 AA.
AC A0A1W2FB55;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, 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=SAMN05660733_05427 {ECO:0000313|EMBL:SMD19145.1};
OS Lentzea albidocapillata.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Lentzea.
OX NCBI_TaxID=40571 {ECO:0000313|EMBL:SMD19145.1, ECO:0000313|Proteomes:UP000192840};
RN [1] {ECO:0000313|Proteomes:UP000192840}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44073 {ECO:0000313|Proteomes:UP000192840};
RA Varghese N., Submissions S.;
RL Submitted (APR-2017) 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}.
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DR EMBL; FWYC01000013; SMD19145.1; -; Genomic_DNA.
DR RefSeq; WP_030481201.1; NZ_JOEA01000026.1.
DR AlphaFoldDB; A0A1W2FB55; -.
DR STRING; 40571.SAMN05660733_05427; -.
DR eggNOG; COG3486; Bacteria.
DR OrthoDB; 7527071at2; -.
DR Proteomes; UP000192840; 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 PRINTS; PR00368; FADPNR.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
PE 3: Inferred from homology;
SQ SEQUENCE 416 AA; 46140 MW; 221E1939D27F6A8D CRC64;
MHPIYDIVGI GFGPSNLALA IALTEHNEQA ETPVTAVFLE RQQAFGWHRG MLLDDATMQV
SFLKDLVTMR NPTSRFSFLC YLRDRGRLID FVNHKNLFPL RVEFHDYFEW AAAQVDDMVT
YGTEAVGVEA IQDNLFEVTT ATGDVYHARN LVFATGLRPT VPEGIALSDR VWHNSEFLHR
VGTLKDPKRC VVVGAGQSAA ETVAYLHREF PGAEVCSVFS RYGYSPADDS SFANRIFDPE
AVDHYFDAPD AVKQRLMDYH RNTNYSVVDV DLIAQLYRTE YQEKVLGTER LKMMKMTRLV
AVEESADGAR AVIQSLVTGE QEFVDTDLVL LATGYDEAAP VLGALDETCS RDETGRLVVG
RDYRVQTSLK GGIYLQGGTE HSHGITSSLL SNVAVRSGEI LTSVLTNTPV PVLATA
//
