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Database: UniProt
Entry: A0A3M8DS11_9BACL
LinkDB: A0A3M8DS11_9BACL
Original site: A0A3M8DS11_9BACL 
ID   A0A3M8DS11_9BACL        Unreviewed;       404 AA.
AC   A0A3M8DS11;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 12.
DE   SubName: Full=L-2-hydroxyglutarate oxidase {ECO:0000313|EMBL:RNB90245.1};
GN   ORFNames=EDM56_06920 {ECO:0000313|EMBL:RNB90245.1};
OS   Brevibacillus fluminis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX   NCBI_TaxID=511487 {ECO:0000313|EMBL:RNB90245.1, ECO:0000313|Proteomes:UP000271031};
RN   [1] {ECO:0000313|EMBL:RNB90245.1, ECO:0000313|Proteomes:UP000271031}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 15716 {ECO:0000313|EMBL:RNB90245.1,
RC   ECO:0000313|Proteomes:UP000271031};
RA   Dunlap C.;
RT   "Phylogenomics of Brevibacillus.";
RL   Submitted (OCT-2018) 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 L2HGDH family.
CC       {ECO:0000256|ARBA:ARBA00037941}.
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:RNB90245.1}.
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DR   EMBL; RHHQ01000007; RNB90245.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3M8DS11; -.
DR   OrthoDB; 9801699at2; -.
DR   Proteomes; UP000271031; Unassembled WGS sequence.
DR   GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:UniProt.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000271031};
KW   Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT   DOMAIN          3..390
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
SQ   SEQUENCE   404 AA;  44423 MW;  04906CB69E49B7D8 CRC64;
     MYDFAIVGGG IVGLSTAMEL GRRYPHARIL VVEKEDSWAK HQTGHNSGVI HSGIYYKPGS
     FKAKFARAGS NSMVQFCQEN DIEHDICGKV IVATKQAELP LMDNLYDRGL ANGLAIHKIS
     AEELKEIEPH VNGLGAIRVP MAGIVNYKQV CETFAAIIGR QGGDLRLSTK VVDIREKRGE
     VELETTRGTF HTRFLINCAG LHSDRIAKLG GAKADLQIVP FRGEYYELKP EKRYLVKHLI
     YPVPNPAFPF LGVHYTRMIG GHVEAGPNAV LSLKREGYKK TDIDLKDLAE VMAFPGFWKL
     AGKFWKEGME EYIRSFSKAA FVKSLQELIP EIRSEDLEPA PAGVRAQALK PDGSLVDDFH
     IIRGASSIHV CNAPSPAATA SIEIGKAIAE QIPEPQLAKP QAIS
//
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