ID A0A0M8YN65_9PSEU Unreviewed; 457 AA.
AC A0A0M8YN65;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=FAD-linked oxidase {ECO:0000313|EMBL:KOX35080.1};
GN ORFNames=ADK67_00760 {ECO:0000313|EMBL:KOX35080.1};
OS Saccharothrix sp. NRRL B-16348.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharothrix.
OX NCBI_TaxID=1415542 {ECO:0000313|EMBL:KOX35080.1, ECO:0000313|Proteomes:UP000037722};
RN [1] {ECO:0000313|EMBL:KOX35080.1, ECO:0000313|Proteomes:UP000037722}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL B-16348 {ECO:0000313|EMBL:KOX35080.1,
RC ECO:0000313|Proteomes:UP000037722};
RA Noorani M.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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:KOX35080.1}.
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DR EMBL; LGED01000001; KOX35080.1; -; Genomic_DNA.
DR RefSeq; WP_053714373.1; NZ_LGED01000001.1.
DR AlphaFoldDB; A0A0M8YN65; -.
DR STRING; 1415542.ADK67_00760; -.
DR PATRIC; fig|1415542.3.peg.156; -.
DR OrthoDB; 9811557at2; -.
DR Proteomes; UP000037722; 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; 3.30.70.2740; -; 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; PTHR42934; GLYCOLATE OXIDASE SUBUNIT GLCD; 1.
DR PANTHER; PTHR42934:SF2; GLYCOLATE OXIDASE SUBUNIT GLCD; 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 4: Predicted;
FT DOMAIN 36..215
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 457 AA; 47877 MW; 1EF18DDEA128774B CRC64;
MDALLAELRS AVGAGAVLTD VDVTASYQRD MMPLAPYGQP LAVVLPTSAE QVQAVVRACA
AARTPIVPRG AGSGLSGAAN AVDGCVVLVT TKMNAIVEVD PDNRLAVVEP GVVNLDLRGA
VEKHGLFYPP DPSSYDWCTI GGNLSTNAGG LCCVKYGVTT DSVLGLDVVL ADGELLRTGR
RTVKGVAGYD LTKLFVGSEG TLGVITRATL ALRPLPQAPV TLVAAFNSTA DAGAAVSRVV
TEGIVPSLME IMDRTSIRAV EQYLKTDLNA DAALLLCQSD SGGEAGRHEL AAIEQACVAA
GAELVYATDD LGEGRDLLTA RRAVLNALEV YGAWLTDDVC VPRTKIADLI AGCERISESV
ALRIAVVGHA GDGNMHPTIV YDPESADEFA RARRAFDEIL ELGLALGGTI TGEHGVGKIK
REWLAREIGP IGLRVHREIK RALDPENLFN PGSMFSV
//
