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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//