ID   D2HDH_ORYSI             Reviewed;         559 AA.
AC   B8B7X6;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Probable D-2-hydroxyglutarate dehydrogenase, mitochondrial;
DE            EC=1.1.99.39;
DE   Flags: Precursor;
GN   Name=D2HGDH; ORFNames=OsI_25178;
OS   Oryza sativa subsp. indica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39946;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. 93-11;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
CC   -!- FUNCTION: Catalyzes the oxidation of D-2-hydroxyglutarate to alpha-
CC       ketoglutarate. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-2-hydroxyglutarate + A = 2-oxoglutarate + AH2;
CC         Xref=Rhea:RHEA:38295, ChEBI:CHEBI:13193, ChEBI:CHEBI:15801,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:17499; EC=1.1.99.39;
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC       Note=Binds 1 FAD per monomer. {ECO:0000250};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the FAD-binding oxidoreductase/transferase type
CC       4 family. {ECO:0000305}.
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DR   EMBL; CM000132; EEC81643.1; -; Genomic_DNA.
DR   AlphaFoldDB; B8B7X6; -.
DR   SMR; B8B7X6; -.
DR   STRING; 39946.B8B7X6; -.
DR   EnsemblPlants; BGIOSGA025294-TA; BGIOSGA025294-PA; BGIOSGA025294.
DR   Gramene; BGIOSGA025294-TA; BGIOSGA025294-PA; BGIOSGA025294.
DR   HOGENOM; CLU_017779_4_1_1; -.
DR   OMA; CNDNMLA; -.
DR   Proteomes; UP000007015; Chromosome 7.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0051990; F:(R)-2-hydroxyglutarate dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0047545; F:2-hydroxyglutarate dehydrogenase activity; IEA:EnsemblPlants.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0010230; P:alternative respiration; IEA:EnsemblPlants.
DR   GO; GO:0006807; P:nitrogen compound metabolic process; IEA:EnsemblPlants.
DR   GO; GO:0009853; P:photorespiration; IEA:EnsemblPlants.
DR   Gene3D; 1.10.45.10; -; 1.
DR   Gene3D; 3.30.43.10; -; 1.
DR   Gene3D; 3.30.465.10; -; 1.
DR   InterPro; IPR016166; FAD-bd_PCMH.
DR   InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR   InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR   InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR   InterPro; IPR016164; FAD-linked_Oxase-like_C.
DR   InterPro; IPR004113; FAD-linked_oxidase_C.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR   Pfam; PF02913; FAD-oxidase_C; 1.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   SUPFAM; SSF55103; SSF55103; 1.
DR   SUPFAM; SSF56176; SSF56176; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   3: Inferred from homology;
KW   FAD; Flavoprotein; Mitochondrion; Oxidoreductase; Reference proteome;
KW   Transit peptide.
FT   TRANSIT         1..80
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           81..559
FT                   /note="Probable D-2-hydroxyglutarate dehydrogenase,
FT                   mitochondrial"
FT                   /id="PRO_0000393391"
FT   DOMAIN          131..310
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
SQ   SEQUENCE   559 AA;  61129 MW;  317DC89B55028DDE CRC64;
     MARRAAAGLL RRHLGPLAAG ETLQARGMYP KQYGAANHAF SRFYSIQGQQ RSLYGFRTNV
     ETDDTQQSAR MNFEVQKRSF SSAAAHVQRN PAYSVLNSDD VSYFKSILGD SGVVQDEDRV
     SVANMDWMGK YKGSSQLLLL PKSTAEVSKI LSYCNSRRLA VVPQGGNTGL VGGSVPVYDE
     VIISLGGMDK IITFDNVNGI LTCEAGCVLE NLSSYVENKG FIMPLDLGAK GSCHIGGNIS
     TNAGGLRFIR YGSLHGSVLG LEVVLADGTV LDMLTTLRKD NTGYDLKHLF IGSEGSLGIV
     TKIAILTPAK LPSTNVAFLS CNDYISCQKL LLAARRSLGE ILSAFEFMDR HCINLAMKYL
     EGVHNPLPVS PYNFYVLIET TGSDESYDKA KLEAFLLRSM EDGLVADGVI AQDISQASNF
     WRIREGISEA SVKVGAVYKY DLSIPVEKLY DIVEEMRSRV GDMGQVLGYG HLGDGNLHLN
     ILSTKYSDKM LAQIEPFVYE WTSKQRGSIS AEHGLGLMKA DKIHYSKSSE AVQLMTSIKK
     LLDPNSILNP YKVLPQSVL