ID   C1AZQ9_RHOOB            Unreviewed;       454 AA.
AC   C1AZQ9;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 82.
DE   SubName: Full=Putative FAD-linked oxidase {ECO:0000313|EMBL:BAH54330.1};
GN   OrderedLocusNames=ROP_60830 {ECO:0000313|EMBL:BAH54330.1};
OS   Rhodococcus opacus (strain B4).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=632772 {ECO:0000313|EMBL:BAH54330.1, ECO:0000313|Proteomes:UP000002212};
RN   [1] {ECO:0000313|EMBL:BAH54330.1, ECO:0000313|Proteomes:UP000002212}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4 {ECO:0000313|EMBL:BAH54330.1,
RC   ECO:0000313|Proteomes:UP000002212};
RA   Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA   Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT   "Comparison of the complete genome sequences of Rhodococcus erythropolis
RT   PR4 and Rhodococcus opacus B4.";
RL   Submitted (MAR-2009) 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; AP011115; BAH54330.1; -; Genomic_DNA.
DR   AlphaFoldDB; C1AZQ9; -.
DR   STRING; 632772.ROP_60830; -.
DR   KEGG; rop:ROP_60830; -.
DR   PATRIC; fig|632772.20.peg.6352; -.
DR   HOGENOM; CLU_017779_4_1_11; -.
DR   OrthoDB; 9811557at2; -.
DR   Proteomes; UP000002212; Chromosome.
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;
FT   DOMAIN          35..214
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   454 AA;  47673 MW;  3B913D64544BD0AD CRC64;
     MDSLRAALAG VVGERFVTVD ADVLATRATD HTGRYSGRAS ALVRPADAAE VSAVLGICRR
     AGVKVTVQGG RTGLEAGTVP EHDDVLLSTE RLTSGGAVDG ENLRVTVGAG VTLAAVRRAA
     SDAGLLFGVD LASRDSATIG GMVSTNAGGL HTVRYGHMSA QVLGLEVVLP DGAIVRRTMR
     VGAENCGYDL PALWVGSEGT LGVVTTVDLT LHPVPEFRVT ALAGFAQLSG LIDAVRVVRR
     LAGVDAVEML DGRGLELASS RLGFAIPTGL PWYLLVDLAG HRDLTGELAG ALERCDPGDE
     PAVGIDPAGR ARVWAAREAF AEVVGLFGPP LKFDAALPLD ALAAFVADGV ALVASRAPDA
     VPIFFGHVAD GNVHLNVLRC PDESVLYRPV TELIRDHGGN IASEHGVGAH KRNYLDLALS
     REDITAMWSI KRAFDPDDYL NPAVMFPDWL RRPR
//