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Database: UniProt
Entry: I3N3E9_ICTTR
LinkDB: I3N3E9_ICTTR
Original site: I3N3E9_ICTTR 
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
//
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