ID M8DGP7_9BACL Unreviewed; 398 AA.
AC M8DGP7;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Hydroxyglutarate oxidase {ECO:0000313|EMBL:EMT52607.1};
GN ORFNames=I532_13159 {ECO:0000313|EMBL:EMT52607.1};
OS Brevibacillus borstelensis AK1.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX NCBI_TaxID=1300222 {ECO:0000313|EMBL:EMT52607.1, ECO:0000313|Proteomes:UP000012081};
RN [1] {ECO:0000313|EMBL:EMT52607.1, ECO:0000313|Proteomes:UP000012081}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AK1 {ECO:0000313|EMBL:EMT52607.1,
RC ECO:0000313|Proteomes:UP000012081};
RA Rajan I., PoliReddy D., Sugumar T., Rathinam K., Alqarawi S., Khalil A.B.,
RA Sivakumar N.;
RT "Assembly of a new bacterial strain Brevibacillus borstelensis AK1.";
RL Submitted (MAR-2013) 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:EMT52607.1}.
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DR EMBL; APBN01000004; EMT52607.1; -; Genomic_DNA.
DR RefSeq; WP_003388754.1; NZ_APBN01000004.1.
DR AlphaFoldDB; M8DGP7; -.
DR STRING; 1300222.I532_13159; -.
DR GeneID; 72735740; -.
DR PATRIC; fig|1300222.3.peg.2752; -.
DR OrthoDB; 9801699at2; -.
DR Proteomes; UP000012081; 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:UP000012081};
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 398 AA; 44445 MW; 1975B953EFA6A461 CRC64;
MYDYVIIGGG IVGLSTGYAL VEKYPQAKIA VVEKERTLAF HQTGHNSGVI HSGIYYKPGS
LKAKLSREGG DLLRSFCNQH EIPYDMCGKV IVATDQHELP LLENLYKRGL ENQLDVSIID
ADQLAEIEPH AYGLKAIRVK EAGIVNYKRI AESLAKVIQE KGGDILLGTK VENIKESSSG
VEIECTNKTI HARYLINCAG LHCDRIAALQ GLKTDMKIVP FRGEYYELKP EKHYLVKNLI
YPVPNPNFPF LGVHFTRMMD GHVHAGPNAV LSFKREGYRK TDFDLKDITE VLTYPAFWKI
AYKNLGEGWK EMVRSFSKKV FVQSLQRLIP EVRAEDLVES ENGVRAQALT KDGKLVDDFL
IVTNQRSTHI LNAPSPAATA SIAIGRNIGE RIPEPAQI
//
