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Database: UniProt
Entry: S4NPU0_9ACTN
LinkDB: S4NPU0_9ACTN
Original site: S4NPU0_9ACTN 
ID   S4NPU0_9ACTN            Unreviewed;       470 AA.
AC   S4NPU0;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   27-MAR-2024, entry version 38.
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=STAFG_2567 {ECO:0000313|EMBL:EPJ40364.1};
OS   Streptomyces afghaniensis 772.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1283301 {ECO:0000313|EMBL:EPJ40364.1, ECO:0000313|Proteomes:UP000015001};
RN   [1] {ECO:0000313|EMBL:EPJ40364.1, ECO:0000313|Proteomes:UP000015001}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=772 {ECO:0000313|EMBL:EPJ40364.1,
RC   ECO:0000313|Proteomes:UP000015001};
RA   Gruening B.A., Praeg A., Erxleben A., Guenther S., Fiedler H.-P.,
RA   Goodfellow M., Mueller M.;
RT   "Draft Genome Sequence of Streptomyces afghaniensis, Which Produces
RT   Compounds of the Julimycin B-Complex.";
RL   Submitted (FEB-2013) 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:EPJ40364.1}.
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DR   EMBL; AOPY01001377; EPJ40364.1; -; Genomic_DNA.
DR   RefSeq; WP_020271532.1; NZ_KE354125.1.
DR   AlphaFoldDB; S4NPU0; -.
DR   PATRIC; fig|1283301.3.peg.2541; -.
DR   HOGENOM; CLU_020931_0_0_11; -.
DR   OrthoDB; 7527071at2; -.
DR   Proteomes; UP000015001; 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   Reference proteome {ECO:0000313|Proteomes:UP000015001}.
FT   REGION          450..470
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   470 AA;  52243 MW;  9114344357AF995D CRC64;
     MNPAQTPGPD APRDLVGIGI GPFNLSLAAL AHPLGELDTA FYEQRPAFGW HPGLLIEGAT
     IQVPFLADLV SLADPTSPWT FLNYLRSRER LFPFYFAERF HIQRTEYDAY CRWVCENLPA
     LHFGHQVDAV RWNPEQDVFE VDFTQLDADG EAEALGRTHA RNVVLGIGTE PYVPDPLKPL
     VEAPGVPVVH AADYLHHREA LLAAEHVTVV GIGQSGAEIF LDLLRGRPAG REKLHWLGRT
     EAFAPMEYSK LGLEHFTPDH TRYFHALPEP ARDRLVTGQW QLHQGIDAAT IAAIHDELYR
     RTLHGGWPDA VLTPGVRVRT AGRVATTKVE LHLEHGPQDS RSRLTTDAVV LATGYRERPL
     DRILAGLDPY MRRDSQARPR IDEDYRLVLD PSVTGTVYVQ NAGTHAHGVG TPDLGLAAWR
     SAIILNSLTG REAYALPRRT AFTTFGLTQR AQVPPPREAP ALTPLVDDRR
//
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