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Database: UniProt
Entry: A0A0M0GJF6_SPOGL
LinkDB: A0A0M0GJF6_SPOGL
Original site: A0A0M0GJF6_SPOGL 
ID   A0A0M0GJF6_SPOGL        Unreviewed;       402 AA.
AC   A0A0M0GJF6;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Hydroxyglutarate oxidase {ECO:0000313|EMBL:KON89908.1};
GN   ORFNames=AF332_25855 {ECO:0000313|EMBL:KON89908.1};
OS   Sporosarcina globispora (Bacillus globisporus).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Sporosarcina.
OX   NCBI_TaxID=1459 {ECO:0000313|EMBL:KON89908.1, ECO:0000313|Proteomes:UP000037109};
RN   [1] {ECO:0000313|Proteomes:UP000037109}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 4 {ECO:0000313|Proteomes:UP000037109};
RA   Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., Ge C.,
RA   Shi H., Pan Z., Liu X.;
RT   "Fjat-10036 dsm4.";
RL   Submitted (JUL-2015) 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:KON89908.1}.
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DR   EMBL; LGUF01000007; KON89908.1; -; Genomic_DNA.
DR   RefSeq; WP_053437273.1; NZ_LGUF01000007.1.
DR   AlphaFoldDB; A0A0M0GJF6; -.
DR   STRING; 1459.AF332_25855; -.
DR   PATRIC; fig|1459.3.peg.5681; -.
DR   OrthoDB; 9801699at2; -.
DR   Proteomes; UP000037109; 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   Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT   DOMAIN          3..389
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
SQ   SEQUENCE   402 AA;  44438 MW;  4BE2C1D702D0A606 CRC64;
     MYDYIIIGGG IVGLSTGMEL LSRFPEAKVT ILEKESHVAA HQTGHNSGVI HSGIYYKPGS
     YKARLAKMGS ESMTEFCREH GLEVDICGKV IVASEDFELP LLDNLYQRGL ENGLGIRMID
     HGELHEIEPH VNGKKAIHVP MAGIVNYKQV SEKMAEIITA KGGDILLNHK VLAIDETAQE
     VIVQTSKGEV RGAYYVNCGG LQSDRIAKLA GLKTDVKIVP FRGEYYMLKP EKSRLVKNLI
     YPVPNPNFPF LGVHFTRMIN GSIDVGPNAV LSFKREGYKK TDLNVADLME VVAYKGFWKL
     ARKYMKEGVD EMIRSASKEL FMKNVQKLMP DIQKDDIVPG PAGVRAQALK DDGSLVDDFF
     IVPSKRSIHV LNAPSPAATA SIEIGKEIVR KMDGMFKMES AV
//
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