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Database: UniProt
Entry: A0A0Q5CTM7_9BURK
LinkDB: A0A0Q5CTM7_9BURK
Original site: A0A0Q5CTM7_9BURK 
ID   A0A0Q5CTM7_9BURK        Unreviewed;       428 AA.
AC   A0A0Q5CTM7;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   SubName: Full=Ornithine monooxygenase {ECO:0000313|EMBL:KQQ35969.1};
GN   ORFNames=ASF61_07045 {ECO:0000313|EMBL:KQQ35969.1};
OS   Duganella sp. Leaf126.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Telluria group; Duganella.
OX   NCBI_TaxID=1736266 {ECO:0000313|EMBL:KQQ35969.1, ECO:0000313|Proteomes:UP000051032};
RN   [1] {ECO:0000313|EMBL:KQQ35969.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf126 {ECO:0000313|EMBL:KQQ35969.1};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQQ35969.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf126 {ECO:0000313|EMBL:KQQ35969.1};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:KQQ35969.1}.
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DR   EMBL; LMNW01000023; KQQ35969.1; -; Genomic_DNA.
DR   RefSeq; WP_056155668.1; NZ_LMNW01000023.1.
DR   AlphaFoldDB; A0A0Q5CTM7; -.
DR   STRING; 1736266.ASF61_07045; -.
DR   OrthoDB; 7527071at2; -.
DR   Proteomes; UP000051032; Unassembled WGS sequence.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
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:KQQ35969.1};
KW   Oxidoreductase {ECO:0000313|EMBL:KQQ35969.1}.
SQ   SEQUENCE   428 AA;  47447 MW;  E51A1CC29AA8FCFB CRC64;
     MAANYQVHDL IGVGFGPSNL ALAIALGEIA PADSAIDACF IEQKPDFVWH GDMLLPDTRM
     QISFLKDLVT LRNPASPYTF INYLQQHGRL QDFINLKTFY PSRHEFNDYL RWAADRCAAD
     CHYGEEVVAV EPVVTNGALD HLRVRSRLTG GAERTRHARN VVLSVGGAPH IPPTFASWRG
     DARVFHSSTY LAGMAGLPAA RRVAVIGAGQ SAAEIFLDLQ ARQADMRVDM VVRNSVLRPA
     DDSAFVNQIF NPEFTDYVYQ RDAQARRCLL EELSNTNYAV IDADLIQRIY DVLYQQKVHG
     DARHRVLFEH EVAGLRVDDG GTLAVDLRHC EGGAAITRSY DAVVLATGYR RQTHRRLLAP
     LAPWFDLADV GRDYRLRGPQ DCAAGVFLQG CCEDTHGLSD TLLSVLAIRS QEIAGAMLAR
     RRQVAAAF
//
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