ID A0A0G3IR98_9MYCO Unreviewed; 400 AA.
AC A0A0G3IR98;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Hydroxyglutarate oxidase {ECO:0000313|EMBL:AKK27816.1};
GN ORFNames=AB431_15265 {ECO:0000313|EMBL:AKK27816.1};
OS Mycobacterium sp. EPa45.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1545728 {ECO:0000313|EMBL:AKK27816.1, ECO:0000313|Proteomes:UP000035237};
RN [1] {ECO:0000313|Proteomes:UP000035237}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EPa45 {ECO:0000313|Proteomes:UP000035237};
RA Kato H., Ogawa N., Ohtsubo Y., Ohshima K., Toyoda A., Yamazoe A., Mori H.,
RA Maruyama F., Nagata Y., Hattori M., Fujiyama A., Kurokawa K., Tsuda M.;
RT "Complete Genome Sequence of a Phenanthrene Degrader, Mycobacterium sp.
RT Strain EPa45, Isolated from a Phenanthrene-Degrading Consortium.";
RL Genome Announc.0:0-0(2015).
RN [2] {ECO:0000313|EMBL:AKK27816.1, ECO:0000313|Proteomes:UP000035237}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EPa45 {ECO:0000313|EMBL:AKK27816.1,
RC ECO:0000313|Proteomes:UP000035237};
RX PubMed=26184940;
RA Kato H., Ogawa N., Ohtsubo Y., Oshima K., Toyoda A., Mori H., Nagata Y.,
RA Kurokawa K., Hattori M., Fujiyama A., Tsuda M.;
RT "Complete Genome Sequence of a Phenanthrene Degrader, Mycobacterium sp.
RT Strain EPa45 (NBRC 110737), Isolated from a Phenanthrene-Degrading
RT Consortium.";
RL Genome Announc. 3:e00782-15(2015).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the L2HGDH family.
CC {ECO:0000256|ARBA:ARBA00037941}.
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DR EMBL; CP011773; AKK27816.1; -; Genomic_DNA.
DR RefSeq; WP_047330640.1; NZ_CP011773.1.
DR AlphaFoldDB; A0A0G3IR98; -.
DR STRING; 1545728.AB431_15265; -.
DR KEGG; mye:AB431_15265; -.
DR PATRIC; fig|1545728.4.peg.3105; -.
DR OrthoDB; 9801699at2; -.
DR Proteomes; UP000035237; Chromosome.
DR GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:UniProt.
DR Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR006076; FAD-dep_OxRdtase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR PANTHER; PTHR43104; L-2-HYDROXYGLUTARATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43104:SF2; L-2-HYDROXYGLUTARATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR Pfam; PF01266; DAO; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 8..397
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
SQ SEQUENCE 400 AA; 42849 MW; 6D3D7476F36C8576 CRC64;
MTPYGRYDLV VVGAGIVGLA VAREWMARRP HDSVTVLERE AAPARHQTGH NSGVIHGGIY
YQPGSLKARL CVEGARLMYE YCEHNGIRHE RCGKLIVAVS PEELGRLGDL QERGIANAVP
GLRRVGAGEI AEIEPNAVGL QALHAPNTGI VDYPGVAGAL VGELRAAGVA VRFGTAVTAI
DGAENPVVHI ADGPLRAGTV IACAGLWADR LARRAGAPRD PQIVPFRGAY LGLKPTETPR
LNGMIYPVPN PELPFLGVHI TKHITGDVTL GPTAMMVGAR DAYSLRRLSI RDSWETVTWP
GTWRVARRYW RVGLDEIRMA ASRRAFVTAA ARYMPGLTQD DLDGSSHAGV RAQAVGRDGS
LVDDFVISRD GRVSHVRNAP SPAATSAFAL ARELVDRVTG
//
