ID B1TFL4_9BURK Unreviewed; 473 AA.
AC B1TFL4;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=FAD linked oxidase domain protein {ECO:0000313|EMBL:EDT37640.1};
GN ORFNames=BamMEX5DRAFT_6580 {ECO:0000313|EMBL:EDT37640.1};
OS Burkholderia ambifaria MEX-5.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=396597 {ECO:0000313|EMBL:EDT37640.1, ECO:0000313|Proteomes:UP000004814};
RN [1] {ECO:0000313|EMBL:EDT37640.1, ECO:0000313|Proteomes:UP000004814}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MEX-5 {ECO:0000313|EMBL:EDT37640.1,
RC ECO:0000313|Proteomes:UP000004814};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Larimer F., Land M.L., Hauser L.,
RA Tiedje J., Richardson P.;
RT "Sequencing of the draft genome and assembly of Burkholderia ambifaria MEX-
RT 5.";
RL Submitted (MAR-2008) 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}.
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:EDT37640.1}.
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DR EMBL; ABLK01000414; EDT37640.1; -; Genomic_DNA.
DR RefSeq; WP_006762309.1; NZ_ABLK01000414.1.
DR AlphaFoldDB; B1TFL4; -.
DR PATRIC; fig|396597.7.peg.797; -.
DR Proteomes; UP000004814; Unassembled WGS sequence.
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}.
FT DOMAIN 38..219
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 473 AA; 50548 MW; B339E4774B097110 CRC64;
MISSETFVSA CRDAIGAAGV LTDPHDTEPF LTDWRRRYKG SACAVLKPAD TAEVAALVRL
ANTHDVALVP QGGNTGLAGG ATPDASGGQA VLSLARLNRV RALDPHNNTI TVEAGVILAD
VQARAREGGR LFALSLAAEG SCTIGGNLST NAGGTAVLRY GNARELCLGL EVVTPQGEIW
DGLRGLRKDN TGYDLRDLFI GAEGTLGIIT AAVMKLHPLP AAQVTALAAL ESPHAALDFL
ALAQRAAGPL LTGFELMSDF CMQLVGKHYP QLRYPFDRPH AQTVLLELSD NESETHARAL
FEKLMEEAFE AGLVVDAVVA ENLAQSRAFW GLREHIPLAQ ADEGLNIKHD IAVPISSIAR
FIDETDAAIQ QAAPGARMVT FGHLGDGNLH YNVQTPEGGD PKAFLAEFQK PINRIVYDNV
HRHHGTISAE HGIGQLKIDD AQRYKSPVET ALMRTLKTAL DPRGLMNPGK VLR
//
