ID   Q46P26_CUPPJ            Unreviewed;       447 AA.
AC   Q46P26;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, sequence version 1.
DT   27-MAR-2024, entry version 99.
DE   SubName: Full=FAD linked oxidase, C-terminal:FAD linked oxidase, N-terminal {ECO:0000313|EMBL:AAZ65108.1};
GN   OrderedLocusNames=Reut_B5765 {ECO:0000313|EMBL:AAZ65108.1};
OS   Cupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Cupriavidus necator
OS   (strain JMP 134)).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=264198 {ECO:0000313|EMBL:AAZ65108.1};
RN   [1] {ECO:0000313|EMBL:AAZ65108.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JMP134 {ECO:0000313|EMBL:AAZ65108.1};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Goltsman E., Martinez M., Schmutz J.,
RA   Larimer F., Land M., Lykidis A., Richardson P.;
RT   "Complete sequence of chromosome 2 of Ralstonia eutropha JMP134.";
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the FAD-binding oxidoreductase/transferase type
CC       4 family. {ECO:0000256|ARBA:ARBA00008000}.
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DR   EMBL; CP000091; AAZ65108.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q46P26; -.
DR   STRING; 264198.Reut_B5765; -.
DR   KEGG; reu:Reut_B5765; -.
DR   eggNOG; COG0277; Bacteria.
DR   HOGENOM; CLU_017779_4_1_4; -.
DR   OrthoDB; 8522822at2; -.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0008152; P:metabolic process; IEA:UniProt.
DR   Gene3D; 3.30.465.10; -; 1.
DR   Gene3D; 3.30.70.2190; -; 1.
DR   Gene3D; 3.30.70.2740; -; 1.
DR   InterPro; IPR004113; FAD-bd_oxidored_4_C.
DR   InterPro; IPR016166; FAD-bd_PCMH.
DR   InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR   InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR   InterPro; IPR016164; FAD-linked_Oxase-like_C.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR   PANTHER; PTHR43716; D-2-HYDROXYGLUTARATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43716:SF1; D-2-HYDROXYGLUTARATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR   Pfam; PF02913; FAD-oxidase_C; 1.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR   SUPFAM; SSF55103; FAD-linked oxidases, C-terminal domain; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   3: Inferred from homology;
FT   DOMAIN          25..204
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   447 AA;  47822 MW;  DD59CDC922F49440 CRC64;
     MDDQLQLASS TEIDERFLRD WSGLAVGRPA QVYRPTTTAE VAAIVRRCHE EGRRITVQGG
     LTGVAGGAVP GEGDVVINLE RMNRIEEIDA LEGVMQVQAG ATLQQVQEAA ADQGWMFAVD
     LGARGSCQIG GNASTNAGGI RVMRYGTMRD SVLGVEAVLP NGTAVSSLSR LVKNSTGLDP
     RFLFIGTEGT LGIITRLTLR LHPPMGDLAA AWVSAARFEA LPQLLRALKR RLGSAMCAFE
     FMSDRFVSLA SRLTGQPAPV AAAPWHVLIE AAGNVGQSME DALQAALSDA LEAGEITDCA
     FAASLSHREA FWRLRESIPE VLTHLKPAAT LDLGLPWSET ASYIGQLEAA LRDRLPDAEH
     LFLGHLGDNN IHLISGPVDD AGVHLVDQLA YAALKGRGGT VSAEHGVGRL KKEYLLVSRK
     PEEIALMRCI KQAMDPAGIL NPGRIFD
//