ID B9BE74_9BURK Unreviewed; 474 AA.
AC B9BE74;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE SubName: Full=FAD linked oxidase domain protein {ECO:0000313|EMBL:EED97626.1};
GN ORFNames=BURMUCGD1_1914 {ECO:0000313|EMBL:EED97626.1};
OS Burkholderia multivorans CGD1.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=513051 {ECO:0000313|EMBL:EED97626.1, ECO:0000313|Proteomes:UP000005493};
RN [1] {ECO:0000313|EMBL:EED97626.1, ECO:0000313|Proteomes:UP000005493}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGD1 {ECO:0000313|EMBL:EED97626.1,
RC ECO:0000313|Proteomes:UP000005493};
RX PubMed=23105085; DOI=10.1128/JB.01306-12;
RA Varga J.J., Losada L., Zelazny A.M., Brinkac L., Harkins D., Radune D.,
RA Hostetler J., Sampaio E.P., Ronning C.M., Nierman W.C., Greenberg D.E.,
RA Holland S.M., Goldberg J.B.;
RT "Draft Genome Sequence Determination for Cystic Fibrosis and Chronic
RT Granulomatous Disease Burkholderia multivorans Isolates.";
RL J. Bacteriol. 194:6356-6357(2012).
CC -!- SIMILARITY: Belongs to the FAD-binding oxidoreductase/transferase type
CC 4 family. {ECO:0000256|ARBA:ARBA00008000}.
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:EED97626.1}.
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DR EMBL; ACFB01000014; EED97626.1; -; Genomic_DNA.
DR AlphaFoldDB; B9BE74; -.
DR Proteomes; UP000005493; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
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:SF2; BLL6224 PROTEIN; 1.
DR PANTHER; PTHR43716; 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}.
FT DOMAIN 39..220
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 474 AA; 50739 MW; 27D3563017FD1EE3 CRC64;
MMMSIDTFVS ACRDAIGAAH VLTDAHDTEP FLTDWRRRYK GAACAVLRPG STAEVAALVR
IANRHGVALV PQGGNTGLAG GATPDTSGTQ AVLSLARLNR VRALDPHNNT ITVEAGVILA
DVQARAREGG RLFALSLAAE GSCTIGGNLS TNAGGTAVLR YGNARELCLG LEVVTPQGEI
WDGLRGLRKD NTGYDLRDLF IGAEGTLGII TAAVMKLHPL PAAQVTALAA LESPHAALDF
LSLAQRAAGP LLTGFELMSD FCMQLVGKHY PQLRYPFAQT HAQTVLLELS DNESETHARA
LFEKLMEEAF DAGLVVDAVV AENLAQSRAF WDLREHIPLA QADEGLNIKH DIAVPISSIA
RFIDETDAAI QQAAPGARMV TFGHLGDGNL HYNVQTPEGG DPKAFLAQFQ APINRIVYDN
VHRHHGTISA EHGIGQLKID DAQRYKSPVE TALMRTLKTA LDPRGLMNPG KVLR
//