ID A0A369GD38_9HYPO Unreviewed; 638 AA.
AC A0A369GD38;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE RecName: Full=L-2-hydroxyglutarate dehydrogenase, mitochondrial {ECO:0000256|ARBA:ARBA00041137};
DE EC=1.1.99.2 {ECO:0000256|ARBA:ARBA00038878};
GN ORFNames=CP532_1229 {ECO:0000313|EMBL:RDA83198.1};
OS Ophiocordyceps camponoti-leonardi (nom. inval.).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Ophiocordyceps.
OX NCBI_TaxID=2039875 {ECO:0000313|EMBL:RDA83198.1, ECO:0000313|Proteomes:UP000252748};
RN [1] {ECO:0000313|EMBL:RDA83198.1, ECO:0000313|Proteomes:UP000252748}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCC 80369 {ECO:0000313|EMBL:RDA83198.1,
RC ECO:0000313|Proteomes:UP000252748};
RA Kobmoo N., Wichadakul D., Arnamnart N., Rodriguez De La Vega R.C.,
RA Luangsa-Ard J.-J., Giraud T.;
RT "A genome scan of diversifying selection in the zombie-ant fungus
RT Ophiocordyceps unilateralis complex supports a role of enterotoxins in
RT coevolution and host-specificity.";
RL Submitted (OCT-2017) 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:RDA83198.1}.
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DR EMBL; PDHP01000198; RDA83198.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A369GD38; -.
DR STRING; 2039875.A0A369GD38; -.
DR Proteomes; UP000252748; 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:SF4; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000252748}.
FT DOMAIN 289..628
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT REGION 1..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 128..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 214..241
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..63
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 638 AA; 69383 MW; 602E3C6E4335B7E8 CRC64;
MAANNGCPES PAGSPRSASV SLQAAATMNA GLQREPSRQS SSSSLARNTT PSSPQTGRRR
STVLMNLHLN DPAVPAPGEM MHDPHQPHPN HHRAPSLGEL HQELEAEQEA HVNRLLHMIR
QQQFELQRLQ AGRPAQPSDD DAADRHAPLP STGSVGSYPR SPFDNVARAD VHSRRSRTPS
RGASPRLRAA SISAESGDWV LGGRDESAFY QAETQMLVRE NQMLRHRIRD LEKQLTDLSV
VPTEPAIPSQ LTLSSTAADE LEKESQSASL VNVTVESQEA REPLRFNCSR NSEVLHAGLY
YGADSLKAKL CVRGQRLIYD FCRRYRVPHR RVGKWIVALD GAQRGALEDI YALATQRLGL
ISLRWLSQDE IRSSGEGVFA PAGALESPDT GIVDSHGLMT CLRALFEDGG GTVALMSSVV
GVEPLGERAS DGWRVRVRDE SEASSSEDTT ITTDTIVNAA GLEAVNIHNL ICPPDSHLPP
LRFAKGSYFS YAAPRPRLSR LVYPAPSPAS AGLGTHLTVD LAGQMRFGPD VEWVDSPLDL
AVSPDRLSSV ARDVRRYLPD LDPSRLVPDY AGIRPKLSRD GAATVAGGSN FHDFIIRKDD
RYQGWVDLLG IESPGLTSSL AIAEMVEELL YGTVTASQ
//
