ID A0A024P406_9BACI Unreviewed; 401 AA.
AC A0A024P406;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=L-2-hydroxyglutarate oxidase LhgO {ECO:0000313|EMBL:CDQ22855.1};
GN Name=lhgO {ECO:0000313|EMBL:CDQ22855.1};
GN ORFNames=BN983_01072 {ECO:0000313|EMBL:CDQ22855.1};
OS Halobacillus karajensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Halobacillus.
OX NCBI_TaxID=195088 {ECO:0000313|EMBL:CDQ22855.1, ECO:0000313|Proteomes:UP000028868};
RN [1] {ECO:0000313|EMBL:CDQ22855.1, ECO:0000313|Proteomes:UP000028868}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HD-03 {ECO:0000313|EMBL:CDQ22855.1,
RC ECO:0000313|Proteomes:UP000028868};
RA Urmite Genomes U.;
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDQ22855.1, ECO:0000313|Proteomes:UP000028868}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HD-03 {ECO:0000313|EMBL:CDQ22855.1,
RC ECO:0000313|Proteomes:UP000028868};
RA Khelaifia S., Croce O., Lagier J.C., Raoult D.;
RT "Draft genome sequence of Halobacillus karajensis HK-03.";
RL Submitted (MAY-2014) 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:CDQ22855.1}.
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DR EMBL; CCDI010000001; CDQ22855.1; -; Genomic_DNA.
DR RefSeq; WP_035506328.1; NZ_CCDJ010000001.1.
DR AlphaFoldDB; A0A024P406; -.
DR Proteomes; UP000028868; 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:UP000028868};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT DOMAIN 3..391
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
SQ SEQUENCE 401 AA; 44952 MW; E60480AB64F8A4FB CRC64;
MYDYVIIGGG IVGLSTAYAL MQKYPHAKMV IVEKEQQISA HQTGRNSGVI HSGVYYKPGS
LKARMAIQGR NTMVKFCQDH DIPHEVCGKV LVATEQEELP RMEALYERVQ QNRLNVTKIN
KEELQDIEPH VNGIAGLRVP GTGIVDYSKV SEKLKELLEH AGADFMLGSA VVDIYERENE
VVVDTPENSL HSHFMINCAG LYSDRLVEMA GIHTDLRIVP FRGEYFELRE EKNHLVKGLI
YPIPNPDFPF LGVHLTKMID GGIHAGPNAV LSFKREGYRK TDFHIKDTLD ILSFPGFWKM
ARANVKEGMK EMVRSLHKQS FVKSLQRLVP EIQADDVIPT DAGVRAQAML KDGQLVDDFH
LITGKRSVHV CNAPSPAATA SLEIGKEIAR RLPQLEYTRV S
//
