ID A0A0N0TP26_9PSEU Unreviewed; 597 AA.
AC A0A0N0TP26;
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-dependent oxidoreductase {ECO:0000313|EMBL:KOX16646.1};
GN ORFNames=ADK67_40080 {ECO:0000313|EMBL:KOX16646.1};
OS Saccharothrix sp. NRRL B-16348.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharothrix.
OX NCBI_TaxID=1415542 {ECO:0000313|EMBL:KOX16646.1, ECO:0000313|Proteomes:UP000037722};
RN [1] {ECO:0000313|EMBL:KOX16646.1, ECO:0000313|Proteomes:UP000037722}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL B-16348 {ECO:0000313|EMBL:KOX16646.1,
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 -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00010790}.
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:KOX16646.1}.
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DR EMBL; LGED01000245; KOX16646.1; -; Genomic_DNA.
DR RefSeq; WP_053721792.1; NZ_LGED01000245.1.
DR AlphaFoldDB; A0A0N0TP26; -.
DR STRING; 1415542.ADK67_40080; -.
DR PATRIC; fig|1415542.3.peg.8613; -.
DR OrthoDB; 9798604at2; -.
DR Proteomes; UP000037722; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR InterPro; IPR003953; FAD-binding_2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR000172; GMC_OxRdtase_N.
DR InterPro; IPR007867; GMC_OxRtase_C.
DR PANTHER; PTHR42784; PYRANOSE 2-OXIDASE; 1.
DR PANTHER; PTHR42784:SF1; PYRANOSE 2-OXIDASE; 1.
DR Pfam; PF00890; FAD_binding_2; 1.
DR Pfam; PF05199; GMC_oxred_C; 1.
DR Pfam; PF00732; GMC_oxred_N; 1.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 7..53
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT DOMAIN 251..334
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00732"
FT DOMAIN 463..588
FT /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05199"
SQ SEQUENCE 597 AA; 64992 MW; 3C24C6C0AE14B503 CRC64;
MADETFDAVI IGSGAGGAPI AHTLVRAGKR VLVLEKGPLF HAQHTSADGL SDFKRDEEFA
TGAEKVLRVE GVANTGVSFY SSHVEPDLND EPHVYRDSDG RDKVTIEGYT AQVVGGGTQL
YGGVSLRFAP DDFRLRTVNQ GRADLRDDVN GDVAQEARDW PFGYDELEPW YCVAEELVGI
NGTRDGQLKP ASVDNYQKPL EPNGISTHVA TGMDALGFRR YRTPLAVITE DHVPSGRTVP
LDRESIKTAF VNRYGDPLGL KSNTWVSLLY PVSTEPGFSL RANCAVTHLS ATDSRVTAVH
YRDPLGRERT VSGTVVVVAC SAIESVRLLQ LSAALDPGFA QRINGNDLLG RYFLTHCFGG
ASARVPGRHD KSRTLDSDWA TDACAAPDFV RANNLWAGGA IYNNTSDSAL PISMARTWAA
NDMDTIWKGY LYDLDMRGDG FDGYLTENFG RQLSVAFMAN QLPLPTNRIT LHPSVRDKWN
RPVAHIDKGW HSHDRAVMDV LAEQCRRILA AGGDGVQVIG YGHVGNDVRR IANHVLGGAR
FGADPADSVL DPDCRAWRFD NLYVTDGAFM PTSGGANPTL TIQANAFRVG DLLTTRV
//
