ID D1A5R1_THECD Unreviewed; 445 AA.
AC D1A5R1;
DT 19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2010, sequence version 1.
DT 27-MAR-2024, entry version 65.
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 OrderedLocusNames=Tcur_2654 {ECO:0000313|EMBL:ACY98206.1};
OS Thermomonospora curvata (strain ATCC 19995 / DSM 43183 / JCM 3096 / KCTC
OS 9072 / NBRC 15933 / NCIMB 10081 / Henssen B9).
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Thermomonosporaceae; Thermomonospora.
OX NCBI_TaxID=471852 {ECO:0000313|EMBL:ACY98206.1, ECO:0000313|Proteomes:UP000001918};
RN [1] {ECO:0000313|EMBL:ACY98206.1, ECO:0000313|Proteomes:UP000001918}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19995 / DSM 43183 / JCM 3096 / KCTC 9072 / NBRC 15933 /
RC NCIMB 10081 / Henssen B9 {ECO:0000313|Proteomes:UP000001918};
RX PubMed=21475583; DOI=10.4056/sigs.1453580;
RA Chertkov O., Sikorski J., Nolan M., Lapidus A., Lucas S., Del Rio T.G.,
RA Tice H., Cheng J.F., Goodwin L., Pitluck S., Liolios K., Ivanova N.,
RA Mavromatis K., Mikhailova N., Ovchinnikova G., Pati A., Chen A.,
RA Palaniappan K., Djao O.D., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA Brettin T., Han C., Detter J.C., Rohde M., Goker M., Woyke T., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Klenk H.P., Kyrpides N.C.;
RT "Complete genome sequence of Thermomonospora curvata type strain (B9).";
RL Stand. Genomic Sci. 1:13-22(2011).
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; CP001738; ACY98206.1; -; Genomic_DNA.
DR RefSeq; WP_012852990.1; NC_013510.1.
DR AlphaFoldDB; D1A5R1; -.
DR STRING; 471852.Tcur_2654; -.
DR KEGG; tcu:Tcur_2654; -.
DR eggNOG; COG3486; Bacteria.
DR HOGENOM; CLU_020931_2_0_11; -.
DR OrthoDB; 7527071at2; -.
DR Proteomes; UP000001918; 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 PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
PE 3: Inferred from homology;
KW Monooxygenase {ECO:0000313|EMBL:ACY98206.1};
KW Oxidoreductase {ECO:0000313|EMBL:ACY98206.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001918}.
SQ SEQUENCE 445 AA; 49233 MW; BF63EFE4B600CCEF CRC64;
MPLPPTCDSA DHVHDVVGIG FGPSNLALAI ALREHNATAA EGDRIEAVFF ERQPAFGWHR
GMLIDGATMQ VSFLKDLVTM RNPTSEFSFL NYLRERGRLA DFINHKTLFP SRAEFHDYLE
WAAGHFDGQV EYGAEVVTVR PVPEQGPATA LDVVVRRGGS ADELVTHRTR NLVIAIGLEP
VLPPEAPAGE RVWHSHELLH RTPALHDPKR LLVVGAGQSA AEVTEYLHRT FPAAEICAVF
ARYGYTPADD SSFANRIFDP EAVDHFYAAP EDVKRMLLDY HHSTNYSAVD MDLIDELYRR
LYQEKVTGRR RLRLFNVSRI ADVEATGSAV RACVEFLPTG ERTELEADAL IYATGYRVGD
PSALLGEVGE HCLRRPDGTL RVERDYRIAT TDALRCGIYV QGATEHTHGI ASTLLSVTAI
RVGEIVQSLT AARSAAPNPP YALSR
//
