ID   F0W6A6_9STRA            Unreviewed;       369 AA.
AC   F0W6A6;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=L-2-hydroxyglutarate dehydrogenase, mitochondrial {ECO:0000256|ARBA:ARBA00041137};
DE            EC=1.1.99.2 {ECO:0000256|ARBA:ARBA00038878};
GN   Name=AlNc14C24G2406 {ECO:0000313|EMBL:CCA16649.1};
GN   ORFNames=ALNC14_027920 {ECO:0000313|EMBL:CCA16649.1};
OS   Albugo laibachii Nc14.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Albuginales; Albuginaceae; Albugo.
OX   NCBI_TaxID=890382 {ECO:0000313|EMBL:CCA16649.1};
RN   [1] {ECO:0000313|EMBL:CCA16649.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=21750662; DOI=10.1371/journal.pbio.1001094;
RA   Kemen E., Gardiner A., Schultz-Larsen T., Kemen A.C., Balmuth A.L.,
RA   Robert-Seilaniantz A., Bailey K., Holub E., Studholme D.J., Maclean D.,
RA   Jones J.D.;
RT   "Gene gain and loss during evolution of obligate parasitism in the white
RT   rust pathogen of Arabidopsis thaliana.";
RL   PLoS Biol. 9:e1001094-e1001094(2011).
RN   [2] {ECO:0000313|EMBL:CCA16649.1}
RP   NUCLEOTIDE SEQUENCE.
RA   MacLean D.;
RL   Submitted (FEB-2011) 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}.
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DR   EMBL; FR824069; CCA16649.1; -; Genomic_DNA.
DR   AlphaFoldDB; F0W6A6; -.
DR   EnsemblProtists; CCA16649; CCA16649; ALNC14_027920.
DR   HOGENOM; CLU_024775_1_1_1; -.
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;
FT   DOMAIN          5..364
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
SQ   SEQUENCE   369 AA;  40672 MW;  FFBD6427E399AC14 CRC64;
     MTPSLVIAGG GVIGLSIARL AAQRGLETFV LEKNAFIGQE TTSRNSQVIH AGIYYPVSGL
     KARLCVAGKE ALYRFCREHD VPYRQCGKLI VAERSQTEIL DRLYENGRKN GVYDLKMVSG
     EEARAMEPEL DCHQALFSPS TGIIDSFGLM TALENDAVRH GATILVNTAV QSVRLGANWK
     RISVVQEGEL YEVESHFFVN ATGLLAPELW PVYDVDRPRV PLKWSKGTYF RLGSGGTIPF
     QRLVYPVPEP GGLGIHFTLG IDGSVRFGPD VELVDRIEYV PIESRKALFV ERIKRYWPAV
     SADDLEVDYC GIRPKIMQAN GQIYEDFCIA GPSFHGVPGV VHLCGIESPG LTSALAIAER
     TIELLESMK
//