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Database: UniProt
Entry: A0A010YGQ2_9ACTN
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ID   A0A010YGQ2_9ACTN        Unreviewed;       430 AA.
AC   A0A010YGQ2;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 37.
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=CryarDRAFT_0485 {ECO:0000313|EMBL:EXG79450.1};
OS   Cryptosporangium arvum DSM 44712.
OC   Bacteria; Actinomycetota; Actinomycetes; Cryptosporangiales;
OC   Cryptosporangiaceae; Cryptosporangium.
OX   NCBI_TaxID=927661 {ECO:0000313|EMBL:EXG79450.1, ECO:0000313|Proteomes:UP000021053};
RN   [1] {ECO:0000313|EMBL:EXG79450.1, ECO:0000313|Proteomes:UP000021053}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44712 {ECO:0000313|EMBL:EXG79450.1,
RC   ECO:0000313|Proteomes:UP000021053};
RG   DOE Joint Genome Institute;
RA   Eisen J., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA   Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA   Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL   Submitted (JUL-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:EXG79450.1}.
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DR   EMBL; JFBT01000001; EXG79450.1; -; Genomic_DNA.
DR   RefSeq; WP_035848103.1; NZ_KK073874.1.
DR   AlphaFoldDB; A0A010YGQ2; -.
DR   PATRIC; fig|927661.3.peg.470; -.
DR   HOGENOM; CLU_020931_0_0_11; -.
DR   OrthoDB; 7527071at2; -.
DR   Proteomes; UP000021053; 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   Monooxygenase {ECO:0000313|EMBL:EXG79450.1};
KW   Oxidoreductase {ECO:0000313|EMBL:EXG79450.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000021053}.
SQ   SEQUENCE   430 AA;  47687 MW;  58EB51E278B9A482 CRC64;
     MSEPYDVLGI GIGPFNLSLA ALAEPLSDVS AVFFDGRPGF SWHPGMLIEG ATLQVPFLAD
     LVTLVDPRSR WSFLSYLQQH DRLFPFYFAE RLHVPRVEYD DYLRWVAESL PSCRFGRPVE
     SISWDAAEQL FVAEVYDVLT ARTTRVRARN TVVGVGTEPV VPAPLRPLLG KEVFHSAEYL
     DRQESLRGAQ DITVLGSGQS GAEVFLDLLR HQRDGGYRLR WLTKAPAFAP MEYSKLGLEH
     FTPEYTRYFC SLPEPVRDAL VPAQWQLYKA IDAETIDAIH SELYERTVAG GSVPVTMSPN
     VEVVGASRSE NGITLECREV LQDRETTVRT DRVVAATGYT ARPPVFLEPL ESVIRRDAAG
     RFRIDSDYRV ELDPGVTGGI YVQNAELHTH GVGTPDLGLG AHRAATILNA LTGAEAYRLP
     SQTAFTTFGV
//
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