ID I3N3E9_ICTTR Unreviewed; 536 AA.
AC I3N3E9;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 24-JAN-2024, entry version 54.
DE RecName: Full=D-2-hydroxyglutarate dehydrogenase, mitochondrial {ECO:0000256|ARBA:ARBA00039639};
DE EC=1.1.99.39 {ECO:0000256|ARBA:ARBA00039003};
GN Name=D2HGDH {ECO:0000313|Ensembl:ENSSTOP00000018895.1};
OS Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS tridecemlineatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC Xerinae; Marmotini; Ictidomys.
OX NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000018895.1, ECO:0000313|Proteomes:UP000005215};
RN [1] {ECO:0000313|Proteomes:UP000005215}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Assembly & Analysis Group;
RG Computational R&D Group;
RG and Sequencing Platform;
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RT "The Draft Genome of Spermophilus tridecemlineatus.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSTOP00000018895.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUL-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-malate + A = AH2 + oxaloacetate; Xref=Rhea:RHEA:67460,
CC ChEBI:CHEBI:13193, ChEBI:CHEBI:15588, ChEBI:CHEBI:16452,
CC ChEBI:CHEBI:17499; Evidence={ECO:0000256|ARBA:ARBA00035965};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67461;
CC Evidence={ECO:0000256|ARBA:ARBA00035965};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the FAD-binding oxidoreductase/transferase type
CC 4 family. {ECO:0000256|ARBA:ARBA00008000}.
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DR EMBL; AGTP01102280; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01102281; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01102282; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01102283; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_005339681.1; XM_005339624.2.
DR AlphaFoldDB; I3N3E9; -.
DR STRING; 43179.ENSSTOP00000018895; -.
DR Ensembl; ENSSTOT00000020455.2; ENSSTOP00000018895.1; ENSSTOG00000023380.2.
DR GeneID; 101973691; -.
DR CTD; 728294; -.
DR eggNOG; KOG1232; Eukaryota.
DR GeneTree; ENSGT00550000075086; -.
DR HOGENOM; CLU_017779_4_1_1; -.
DR InParanoid; I3N3E9; -.
DR OMA; TPRTCGE; -.
DR OrthoDB; 1664005at2759; -.
DR TreeFam; TF323342; -.
DR Proteomes; UP000005215; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0051990; F:(R)-2-hydroxyglutarate dehydrogenase activity; IEA:Ensembl.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:Ensembl.
DR GO; GO:0006108; P:malate metabolic process; IEA:Ensembl.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.30.70.2190; -; 1.
DR Gene3D; 3.30.70.2740; -; 1.
DR Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR InterPro; IPR004113; FAD-bd_oxidored_4_C.
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; IPR006094; Oxid_FAD_bind_N.
DR InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR PANTHER; PTHR43716; D-2-HYDROXYGLUTARATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43716:SF1; D-2-HYDROXYGLUTARATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR Pfam; PF02913; FAD-oxidase_C; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR SUPFAM; SSF55103; FAD-linked oxidases, C-terminal domain; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000005215};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 110..290
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 536 AA; 58199 MW; CFC433234D3BAC2D CRC64;
MVLCHVPRWS VRLWACPGWW RPTSTLRALV RPRGPGCPGG ASGPLACRMF SKVSSCPPEV
MLTQERYPVQ RLPFSVVSEE DLAAFEHMVP GRVVTDPEEL EVSNVDWLRT ARGCSKVLLR
PRTSEEVSRI LRYCHERNLA VTPQGGNTGL VGGSVPVFDE IILSTALMNQ VTSFNSVSGI
LTCQAGCVLE GLSRYVQEQD FVMPLDLGAK GSCHIGGNVA TNAGGLRFLR YGSLRGTVLG
LEVVLADGTV LDCLTSLRKD NTGYDLKQLF IGSEGTLGVI TAVSILCPPR PKAVNVAFLG
CPGFAEVLQT FSTCRGMLGE VLSAFEFMDA ECMQLVQQHL HLASPVQESA FYLLVETSGS
STGHDAEKLG CFLEQVLGSG LVTDGTVATD ESKAQALWAL RERITEALSR DGYVYKYDVS
LPVERLYDLV PDLRARLGSQ ARHVVGYGHL GDGNLHLNVT VDAFSTALLD TLEPYVYAWT
AGQRGSISAE HGLGFRKRDA LGYSKPPHAV QLMQQLKALL DPKGILNPYK MLPTQA
//