ID M7ABJ0_9ACTN Unreviewed; 456 AA.
AC M7ABJ0;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 2.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=FAD-linked oxidase {ECO:0000313|EMBL:EMP13952.2};
GN ORFNames=ISGA_1536 {ECO:0000313|EMBL:EMP13952.2};
OS Gordonia sp. NB41Y.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Gordonia.
OX NCBI_TaxID=875808 {ECO:0000313|EMBL:EMP13952.2, ECO:0000313|Proteomes:UP000011989};
RN [1] {ECO:0000313|EMBL:EMP13952.2, ECO:0000313|Proteomes:UP000011989}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NB4-1Y {ECO:0000313|EMBL:EMP13952.2,
RC ECO:0000313|Proteomes:UP000011989};
RX PubMed=23744905; DOI=10.1099/mic.0.068932-0;
RA Van Hamme J.D., Bottos E.M., Bilbey N.J., Brewer S.E.;
RT "Genomic and proteomic characterization of Gordonia sp. NB4-1Y in relation
RT to 6 : 2 fluorotelomer sulfonate biodegradation.";
RL Microbiology 159:1618-1628(2013).
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:EMP13952.2}.
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DR EMBL; APHK02000086; EMP13952.2; -; Genomic_DNA.
DR RefSeq; WP_053778132.1; NZ_CP132196.1.
DR AlphaFoldDB; M7ABJ0; -.
DR STRING; 1241906.ISGA_1536; -.
DR Proteomes; UP000011989; 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 Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 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; IPR016167; FAD-bd_PCMH_sub1.
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;
KW Reference proteome {ECO:0000313|Proteomes:UP000011989}.
FT DOMAIN 34..219
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 456 AA; 46803 MW; 7F1F269D7C858CB2 CRC64;
MNLTRRLGEI VGTAHVLTDP DATAGYLTDW MGRYTGHADA VVRPRTTDEV AAVVTLCAAE
GVRICVQGGN TGLVGGSVPP SHADGSRPTI LLSTARMTDV DEIDIVGQSV GVQAGASVAT
IDTAAGRAGL MFGVDLASRE SATAGGVVAT NAGGVRMIRH GNTRSQVLGI EAVLADGRIL
RRWSPLVKDN VGYDIPGLLA GSEGTLAVIT GVLLRLVRPA TGAEVAVIAL RAVDDATALI
GAARDAGLTI EAAELMTDAG VTLVHEHGVR RPVATAAPFY LLLEVSGTGG VQDVLLGVLE
TADGVLDAVV EPGPGRALWE VRERHTESIS RSTATPVVKL DVSVPIHALG DAVADLEALA
GSRDHRCRPI LFGHVGDGNI HVNLLDVPPD DADGLTEAVF AVIAGHGGSI SAEHGIGRAK
SAWTHLGRSA VDLATMRAIK DALDPQGLLN PGVLFG
//
