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Database: UniProt
Entry: A0A0A0D528_9PROT
LinkDB: A0A0A0D528_9PROT
Original site: A0A0A0D528_9PROT 
ID   A0A0A0D528_9PROT        Unreviewed;       470 AA.
AC   A0A0A0D528;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=FAD-linked oxidase {ECO:0000313|EMBL:KGM33165.1};
GN   ORFNames=P409_17335 {ECO:0000313|EMBL:KGM33165.1};
OS   Inquilinus limosus MP06.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Inquilinus.
OX   NCBI_TaxID=1398085 {ECO:0000313|EMBL:KGM33165.1, ECO:0000313|Proteomes:UP000029995};
RN   [1] {ECO:0000313|EMBL:KGM33165.1, ECO:0000313|Proteomes:UP000029995}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MP06 {ECO:0000313|EMBL:KGM33165.1,
RC   ECO:0000313|Proteomes:UP000029995};
RA   Pino M., Di Conza J., Gutkind G.;
RT   "Genome sequence determination for a cystic fibrosis isolate, Inquilinus
RT   limosus.";
RL   Submitted (JAN-2014) 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:KGM33165.1}.
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DR   EMBL; JANX01000217; KGM33165.1; -; Genomic_DNA.
DR   RefSeq; WP_034840140.1; NZ_JANX01000217.1.
DR   AlphaFoldDB; A0A0A0D528; -.
DR   OrthoDB; 9815648at2; -.
DR   Proteomes; UP000029995; 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          45..224
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   470 AA;  49298 MW;  8FB9918B1933890E CRC64;
     MQQATASDRL PDALIPSLAA ALGAASVLAG PDIPARNESD WSTLGPLRPL AVVRPVDTAG
     VAAAMRICAE HGVPVVPQGG LTGLCGGARP VAGSVALSLE RMVGVEEIDT ASATMTVRAG
     TPLQAVQQAA DEAGFLIPLD LGARGSCAIG GNLSTNAGGN RVIRYGMARE MVLGIEVVLP
     GGEVVTSLNK MLKNNAGYDL KHLFIGSEGT LGVITRAVLR LFPKPGCTMA ALCGLSSYGH
     TVRLLNAARR GLGPLLSAFE VMWPDYWDVV TQKVPGIRSP ISGGHAGYVL VEAQGTDEAV
     DGPRFQAWLE RQAEDGVIAD AAVAQSLGDI RAFWGVRDAA AEFRQVLGPH ESFDIGLPVA
     AMDDYVRACR AALEQRLPGI FALFYGHIGD GNLHIVAGVP GAEPQPKQEI VETVYAMVRE
     FGGTVSAEHG IGLTKKPFLP YVRSEAELAL MRRLKDALDP RGLLNPSKVL
//
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