ID A0A0R0C9W9_9GAMM Unreviewed; 462 AA.
AC A0A0R0C9W9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=FAD-linked oxidase {ECO:0000313|EMBL:KRG66048.1};
GN ORFNames=ABB26_02220 {ECO:0000313|EMBL:KRG66048.1};
OS Stenotrophomonas humi.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas.
OX NCBI_TaxID=405444 {ECO:0000313|EMBL:KRG66048.1, ECO:0000313|Proteomes:UP000050864};
RN [1] {ECO:0000313|EMBL:KRG66048.1, ECO:0000313|Proteomes:UP000050864}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18929 {ECO:0000313|EMBL:KRG66048.1,
RC ECO:0000313|Proteomes:UP000050864};
RA Patil P.P., Midha S., Patil P.B.;
RT "Genome sequencing and analysis of members of genus Stenotrophomonas.";
RL Submitted (MAY-2015) 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:KRG66048.1}.
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DR EMBL; LDJI01000004; KRG66048.1; -; Genomic_DNA.
DR RefSeq; WP_057631937.1; NZ_LDJI01000004.1.
DR AlphaFoldDB; A0A0R0C9W9; -.
DR STRING; 405444.ABB26_02220; -.
DR PATRIC; fig|405444.3.peg.2854; -.
DR OrthoDB; 9811557at2; -.
DR Proteomes; UP000050864; 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 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 36..215
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 462 AA; 50373 MW; 923A9A1754239C5F CRC64;
MTDPRLHSLQ QACPSLRLKT DPSDLEHYGR DWTRRWTPAP LAIALPATVE EVQAVVRWAN
VESVAVVPSG GRTGLSGGAV AANGELVLSL ERMNKALGFD AVDRTLTVQA GMPLEAVHNA
AREHGLIYPV DFAARGSCSI GGNIATNAGG IRVIRYGNTR EWIAGLKVVA GNGELLELNK
GLIKNSSGYD FRQLMIGSEG TLGIVVEATL KLTDPPPTSN VMLLALPSFE VLMQVFSAFR
EKLQLEAFEF FTDRAVHHVT AHGAQYPFEE IHPYYVVTEY ASADEAGEAA AMAAFEYCME
QGWVLDGVIS TSEAQAQQLW RLREGITESV ARYKPYKNDV SVRISAMPAF LAESQALING
AYPHFEVVWF GHIGDGNLHI NVLKPDDTSD AEFLTQCEQV TKLLAQVLHR FHGSISAEHG
IGLVKKAYLD STRGAAEIAL MRGVKRVFDP NGLMNPGKLF DL
//
