ID F4G7L4_ALIDK Unreviewed; 488 AA.
AC F4G7L4;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=Monooxygenase FAD-binding protein {ECO:0000313|EMBL:AEB86611.1};
GN OrderedLocusNames=Alide2_4296 {ECO:0000313|EMBL:AEB86611.1};
OS Alicycliphilus denitrificans (strain DSM 14773 / CIP 107495 / K601).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Alicycliphilus.
OX NCBI_TaxID=596154 {ECO:0000313|EMBL:AEB86611.1, ECO:0000313|Proteomes:UP000007938};
RN [1] {ECO:0000313|EMBL:AEB86611.1, ECO:0000313|Proteomes:UP000007938}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14773 / CIP 107495 / K601
RC {ECO:0000313|Proteomes:UP000007938};
RX PubMed=21742888; DOI=10.1128/JB.00365-11;
RA Oosterkamp M.J., Veuskens T., Plugge C.M., Langenhoff A.A., Gerritse J.,
RA van Berkel W.J., Pieper D.H., Junca H., Goodwin L.A., Daligault H.E.,
RA Bruce D.C., Detter J.C., Tapia R., Han C.S., Land M.L., Hauser L.J.,
RA Smidt H., Stams A.J.;
RT "Genome Sequences of Alicycliphilus denitrificans Strains BC and K601T.";
RL J. Bacteriol. 193:5028-5029(2011).
RN [2] {ECO:0000313|EMBL:AEB86611.1, ECO:0000313|Proteomes:UP000007938}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14773 / CIP 107495 / K601
RC {ECO:0000313|Proteomes:UP000007938};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Zeytun A., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Mikhailova N., Pagani I., Oosterkamp M.,
RA Pieper D., van Berkel W., Langenhoff A., Smidt H., Stams A., Woyke T.;
RT "Complete sequence of chromosome of Alicycliphilus denitrificans K601.";
RL Submitted (APR-2011) 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}.
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DR EMBL; CP002657; AEB86611.1; -; Genomic_DNA.
DR RefSeq; WP_013723102.1; NC_015422.1.
DR AlphaFoldDB; F4G7L4; -.
DR STRING; 596154.Alide2_4296; -.
DR KEGG; adk:Alide2_4296; -.
DR eggNOG; COG2072; Bacteria.
DR HOGENOM; CLU_044076_0_0_4; -.
DR OrthoDB; 8671611at2; -.
DR Proteomes; UP000007938; Chromosome.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
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; IPR002938; FAD-bd.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR025700; Lys/Orn_oxygenase.
DR PANTHER; PTHR43539:SF91; FAD-DEPENDENT URATE HYDROXYLASE; 1.
DR PANTHER; PTHR43539; FLAVIN-BINDING MONOOXYGENASE-LIKE PROTEIN (AFU_ORTHOLOGUE AFUA_4G09220); 1.
DR Pfam; PF01494; FAD_binding_3; 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:AEB86611.1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000007938}.
FT DOMAIN 46..94
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
SQ SEQUENCE 488 AA; 52962 MW; 257D10EA032711AA CRC64;
MSVSPPMGMA GLAALEERLA HDLLTLNWRA RPWLPTRSHG GQAVIDVLVI GAGQAGLAAS
MALAQQGVAA VLLDRAPADY EGPWATTARM ETLRSPKELT GPALGVPSLT FRAWFEAQWG
RDAWDALDKI PRLQWMDYLR WYRRVTGADV RNGHAATAVR PRADGLVEVD VQAPAGHATW
LARRVVLATG RDGLGGPQIP PFMQDVERGL WAHSSDVLDY ATLAGKRVGV IGMGSSAMDS
ASTALECGAA SVDLIARRAA MPMVNKSKGS GVPGLTQGHY DLPDAWKWRI RHYINAQQVP
PPHGSTLRVS RHANAFFHFG CAVHAVTQAG RELRVATARG TFAFNFLILA TGFAIDWAQK
PEFAPFARHV RTWGERYRPP PGEEDRELFD SPDLGPVFEF QEKAPGTCPG LDRIHCFCYP
AALSHGTVSG DIPAISDGAR RLASGIAGLL YREDVEHHHA VLQAYAEPEL LGDEWTPADT
SQRVLPSP
//
