ID Q0K065_CUPNH Unreviewed; 477 AA.
AC Q0K065;
DT 03-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 100.
DE SubName: Full=FAD/FMN-containing dehydrogenase {ECO:0000313|EMBL:CAJ96609.1};
GN OrderedLocusNames=H16_B1827 {ECO:0000313|EMBL:CAJ96609.1};
OS Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442
OS / H16 / Stanier 337) (Ralstonia eutropha).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=381666 {ECO:0000313|EMBL:CAJ96609.1, ECO:0000313|Proteomes:UP000008210};
RN [1] {ECO:0000313|EMBL:CAJ96609.1, ECO:0000313|Proteomes:UP000008210}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier
RC 337 {ECO:0000313|Proteomes:UP000008210};
RX PubMed=16964242; DOI=10.1038/nbt1244;
RA Pohlmann A., Fricke W.F., Reinecke F., Kusian B., Liesegang H., Cramm R.,
RA Eitinger T., Ewering C., Potter M., Schwartz E., Strittmatter A., Voss I.,
RA Gottschalk G., Steinbuechel A., Friedrich B., Bowien B.;
RT "Genome sequence of the bioplastic-producing 'Knallgas' bacterium Ralstonia
RT eutropha H16.";
RL Nat. Biotechnol. 24:1257-1262(2006).
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; AM260480; CAJ96609.1; -; Genomic_DNA.
DR RefSeq; WP_011617494.1; NZ_CP039288.1.
DR AlphaFoldDB; Q0K065; -.
DR STRING; 381666.H16_B1827; -.
DR GeneID; 57647729; -.
DR KEGG; reh:H16_B1827; -.
DR eggNOG; COG0277; Bacteria.
DR HOGENOM; CLU_017779_4_1_4; -.
DR OrthoDB; 8522822at2; -.
DR Proteomes; UP000008210; Chromosome 2.
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 Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 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; IPR016167; FAD-bd_PCMH_sub1.
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;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022827};
KW Reference proteome {ECO:0000313|Proteomes:UP000008210}.
FT DOMAIN 34..216
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 477 AA; 50499 MW; DA9DCCA50872AD8B CRC64;
MSLVLKLKDL LGPDAVLTEP ADVAAYIEDW RGRYKGPALC VVLPASTAQV AAVVQAAVQA
SVPVLPQGGN TSLCGGAVPA PDGTPPIVIS LARMRRIRAI DAANNSMEVE AGCVLAAIQQ
AAAEQGRLYP VSLGAEGSCQ IGGNIATNAG GTGVLRYGNT RDNVLGLEVV LPDGQVWNGL
YRLRKNNTGL DLKHLFIGSE GTLGVITAAT LKLHPLPTAH AMAWLAVSTP QAALEMLGRF
QQRCGATLSA FEMLNDVQLQ IVLDHVPGRR APLPASHPWH VLVELADTGR RELLDQVLQE
VLEQGVAEGL VDDAVVAASG AQREAMWQVR HSVSEGNKKA GLGLNTDCAV PVSAVPQFIE
RATAAAHAVL PDLPIIVVAH LGDGNVHFIP LVPFPQWQAL PERDAVAARI KHAIDQVAYE
LGGTFSAEHG IGQVLTEEMA QFKPAVEIAM MHGIKRMLDP RDLFNPGRLL PSPPSQQ
//
