ID A0A0T6B500_9SCAR Unreviewed; 450 AA.
AC A0A0T6B500;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=L-2-hydroxyglutarate dehydrogenase, mitochondrial {ECO:0000256|ARBA:ARBA00041137};
DE EC=1.1.99.2 {ECO:0000256|ARBA:ARBA00038878};
DE Flags: Fragment;
GN ORFNames=AMK59_4426 {ECO:0000313|EMBL:KRT82277.1};
OS Oryctes borbonicus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Scarabaeiformia;
OC Scarabaeidae; Dynastinae; Oryctes.
OX NCBI_TaxID=1629725 {ECO:0000313|EMBL:KRT82277.1, ECO:0000313|Proteomes:UP000051574};
RN [1] {ECO:0000313|EMBL:KRT82277.1, ECO:0000313|Proteomes:UP000051574}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OB123 {ECO:0000313|EMBL:KRT82277.1};
RC TISSUE=Whole animal {ECO:0000313|EMBL:KRT82277.1};
RA Meyer J.M., Markov G.V., Baskaran P., Herrmann M., Sommer R.J.,
RA Roedelsperger C.;
RT "Draft genome of the scarab beetle Oryctes borbonicus.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-2-hydroxyglutarate + A = 2-oxoglutarate + AH2;
CC Xref=Rhea:RHEA:21252, ChEBI:CHEBI:13193, ChEBI:CHEBI:16782,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:17499; EC=1.1.99.2;
CC Evidence={ECO:0000256|ARBA:ARBA00036066};
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:KRT82277.1}.
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DR EMBL; LJIG01009839; KRT82277.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0T6B500; -.
DR OrthoDB; 1815533at2759; -.
DR Proteomes; UP000051574; Unassembled WGS sequence.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000051574}.
FT DOMAIN 43..441
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRT82277.1"
SQ SEQUENCE 450 AA; 50692 MW; CEA668AAF8204A99 CRC64;
SCELKFRPFR VNMSKLPYSV PFKRLKNFVN IRKLSTSKKR NYDIVVIGGG IVGVSTAREF
LQRHKNFKMA ILEKEHKLAV HQTGHNSGVI HAGIYYKPGS LKAKLCVEGH HLCYKYFDEK
QIPYKKVGKL IVATNQVELE RLKDLHERGL KNNVPGLELI EGKKIQQIEP HCKGLKALWS
PHTGIVDFAL VTDYYAKDFK HLGGDIHLNF QVNKFSEGAD PDFPVVIHSQ DGTMINAKYV
LTCGGLYSDK LAELSGCSSN PKIVPFRGEY LLLDKSKCPM IKGNIYPVPD PNFPFLGVHF
TPRMNGDVWL GPNAVLAFKR EGYTFFDINL KELLESLTYS GFRKLAFKYA FSGLDELVRS
LILPLQMKEL QKFIPDITLK DIRRGPAGVR AQALDENGNL LDDFFFDMGD KGTLSKRVLH
CRNAPSPGAT SSLAIAKMIA DKLENNFKIS
//
