ID A0A0Q7KBW6_9ACTN Unreviewed; 458 AA.
AC A0A0Q7KBW6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=FAD-linked oxidase {ECO:0000313|EMBL:KQX72332.1};
GN ORFNames=ASD10_15135 {ECO:0000313|EMBL:KQX72332.1};
OS Aeromicrobium sp. Root472D3.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Aeromicrobium.
OX NCBI_TaxID=1736540 {ECO:0000313|EMBL:KQX72332.1, ECO:0000313|Proteomes:UP000050971};
RN [1] {ECO:0000313|EMBL:KQX72332.1, ECO:0000313|Proteomes:UP000050971}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root472D3 {ECO:0000313|EMBL:KQX72332.1,
RC ECO:0000313|Proteomes:UP000050971};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQX72332.1, ECO:0000313|Proteomes:UP000050971}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root472D3 {ECO:0000313|EMBL:KQX72332.1,
RC ECO:0000313|Proteomes:UP000050971};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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:KQX72332.1}.
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DR EMBL; LMET01000002; KQX72332.1; -; Genomic_DNA.
DR RefSeq; WP_056610781.1; NZ_LMET01000002.1.
DR AlphaFoldDB; A0A0Q7KBW6; -.
DR STRING; 1736540.ASD10_15135; -.
DR OrthoDB; 9811557at2; -.
DR Proteomes; UP000050971; 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;
KW Reference proteome {ECO:0000313|Proteomes:UP000050971}.
FT DOMAIN 38..217
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 458 AA; 47239 MW; 31467C785E90D6EC CRC64;
MPVNATDALA LGELGSVVLS TDPDVTAAYA HDESRLTARA IPFAVLAPTC TQEVSDCLRI
ASRQGWRVVT RGAGSGLSGA ANGDGEFVVL STHRMDAIVS VDPVERLAVA QPGVVTGDLR
AAVAEQGLFY PPDPGSVGFS TIGGNVATNA GGMCCVKYGV TGDFVLGLEV VLADGRVMRT
GRRTAKGVAG YDLTHLVVGS EGTLGVVTEV TVRLLPAPSP ALTLVATFAS LADAGRAVAA
VTGSGVPVSM LEIMDRTTLQ AVDRMARMGF EPDTAAMLLA QCDTTDAAGV LAAVAGHCDS
AGAVDVAVGD DPQEGAQLLE ARRLALPALE QLGDWLLDDV CVPRGRIVEL LERIETVAAD
EGLTIGVFGH AGDGNMHPTI IYDDNDEAGR AAAMRAFDRI TEHALDLGGT ITGEHGVGRL
KRSWLARELD ATSLDVQRAV RAALDPGGVL NPGNLFDA
//
