D2HDH_BOVIN
ID D2HDH_BOVIN Reviewed; 544 AA.
AC Q1JPD3; A5PKH4;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 2.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=D-2-hydroxyglutarate dehydrogenase, mitochondrial;
DE EC=1.1.99.39 {ECO:0000250|UniProtKB:Q8N465};
DE Flags: Precursor;
GN Name=D2HGDH;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Ascending colon;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the oxidation of D-2-hydroxyglutarate (D-2-HG) to
CC alpha-ketoglutarate (By similarity). Also catalyzes the oxidation of
CC other D-2-hydroxyacids, such as D-malate (D-MAL) and D-lactate (D-LAC)
CC (By similarity). Exhibits high activities towards D-2-HG and D-MAL but
CC a very weak activity towards D-LAC (By similarity).
CC {ECO:0000250|UniProtKB:Q8N465}.
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 Evidence={ECO:0000250|UniProtKB:Q8N465};
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:0000250|UniProtKB:Q8N465};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67461;
CC Evidence={ECO:0000250|UniProtKB:Q8N465};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000305};
CC -!- ACTIVITY REGULATION: Activated by zinc and cobalt ions.
CC {ECO:0000250|UniProtKB:Q8N465}.
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; BT025420; ABF57376.1; -; mRNA.
DR EMBL; BC142488; AAI42489.1; -; mRNA.
DR RefSeq; NP_001069446.1; NM_001075978.1.
DR RefSeq; XP_005205097.1; XM_005205040.2.
DR RefSeq; XP_005205098.1; XM_005205041.3.
DR RefSeq; XP_010802204.1; XM_010803902.2.
DR RefSeq; XP_010802205.1; XM_010803903.2.
DR AlphaFoldDB; Q1JPD3; -.
DR SMR; Q1JPD3; -.
DR STRING; 9913.ENSBTAP00000003690; -.
DR PaxDb; Q1JPD3; -.
DR PRIDE; Q1JPD3; -.
DR Ensembl; ENSBTAT00000003690; ENSBTAP00000003690; ENSBTAG00000002847.
DR Ensembl; ENSBTAT00000081426; ENSBTAP00000062563; ENSBTAG00000002847.
DR GeneID; 533003; -.
DR KEGG; bta:533003; -.
DR CTD; 728294; -.
DR VEuPathDB; HostDB:ENSBTAG00000002847; -.
DR VGNC; VGNC:27861; D2HGDH.
DR eggNOG; KOG1232; Eukaryota.
DR GeneTree; ENSGT00550000075086; -.
DR HOGENOM; CLU_017779_4_1_1; -.
DR InParanoid; Q1JPD3; -.
DR OMA; CNDNMLA; -.
DR OrthoDB; 515900at2759; -.
DR TreeFam; TF323342; -.
DR Reactome; R-BTA-880009; Interconversion of 2-oxoglutarate and 2-hydroxyglutarate.
DR Proteomes; UP000009136; Chromosome 3.
DR Bgee; ENSBTAG00000002847; Expressed in laryngeal cartilage and 105 other tissues.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0051990; F:(R)-2-hydroxyglutarate dehydrogenase activity; ISS:UniProtKB.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0006108; P:malate metabolic process; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW FAD; Flavoprotein; Metal-binding; Mitochondrion; Oxidoreductase;
KW Reference proteome; Transit peptide; Zinc.
FT TRANSIT 1..10
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 11..544
FT /note="D-2-hydroxyglutarate dehydrogenase, mitochondrial"
FT /id="PRO_0000347234"
FT DOMAIN 119..298
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT BINDING 409
FT /ligand="(R)-2-hydroxyglutarate"
FT /ligand_id="ChEBI:CHEBI:15801"
FT /evidence="ECO:0000250|UniProtKB:Q8N465"
FT BINDING 409
FT /ligand="(R)-lactate"
FT /ligand_id="ChEBI:CHEBI:16004"
FT /evidence="ECO:0000250|UniProtKB:Q8N465"
FT BINDING 409
FT /ligand="(R)-malate"
FT /ligand_id="ChEBI:CHEBI:15588"
FT /evidence="ECO:0000250|UniProtKB:Q8N465"
FT BINDING 413
FT /ligand="(R)-2-hydroxyglutarate"
FT /ligand_id="ChEBI:CHEBI:15801"
FT /evidence="ECO:0000250|UniProtKB:Q8N465"
FT BINDING 413
FT /ligand="(R)-malate"
FT /ligand_id="ChEBI:CHEBI:15588"
FT /evidence="ECO:0000250|UniProtKB:Q8N465"
FT BINDING 424
FT /ligand="(R)-2-hydroxyglutarate"
FT /ligand_id="ChEBI:CHEBI:15801"
FT /evidence="ECO:0000250|UniProtKB:Q8N465"
FT BINDING 424
FT /ligand="(R)-malate"
FT /ligand_id="ChEBI:CHEBI:15588"
FT /evidence="ECO:0000250|UniProtKB:Q8N465"
FT BINDING 457
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q8N465"
FT BINDING 464
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q8N465"
FT BINDING 466
FT /ligand="(R)-2-hydroxyglutarate"
FT /ligand_id="ChEBI:CHEBI:15801"
FT /evidence="ECO:0000250|UniProtKB:Q8N465"
FT BINDING 498
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q8N465"
FT BINDING 499
FT /ligand="(R)-2-hydroxyglutarate"
FT /ligand_id="ChEBI:CHEBI:15801"
FT /evidence="ECO:0000250|UniProtKB:Q8N465"
FT BINDING 499
FT /ligand="(R)-lactate"
FT /ligand_id="ChEBI:CHEBI:16004"
FT /evidence="ECO:0000250|UniProtKB:Q8N465"
FT BINDING 499
FT /ligand="(R)-malate"
FT /ligand_id="ChEBI:CHEBI:15588"
FT /evidence="ECO:0000250|UniProtKB:Q8N465"
FT MOD_RES 124
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8CIM3"
FT CONFLICT 418
FT /note="R -> H (in Ref. 1; ABF57376)"
FT /evidence="ECO:0000305"
FT CONFLICT 433
FT /note="R -> Q (in Ref. 1; ABF57376)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 544 AA; 59056 MW; 323FB6FBFE09CCA5 CRC64;
MMMPRLVPRW PAWLFCWRAA CIQGASVRQK MWAGPSKIPG LGGPRGAWGT SPLVPRGSCS
ASSRTPEVTL TPERYPVQRL PFSVVSEDDL AALERVVPGR VITDPEELEP PNVDWLRTVR
GSSKVLLRPR TTQEVAHILR YCHERNLAVN PQGGNTGMVG GSTPVFDEII LSTALMNQVL
SFHDVSGVLV CQAGCVLEAL SQYVEERGFI MPLDLGAKGS CHIGGNVATN AGGLRVLRYG
SLRGTVLGLE VVLADGTVLN CLTSLRKDNT GYDLKQLFIG SEGTLGVITA VSILCPPKPS
TVNVAFLGCP GFAEVLQTFR TCRAMLGEIL SAFEFMDAEC MKLVRLHLGL SCPVQESPFY
VLIETAGSGP GHDAEKLGCF LEQVLDSGLV TDGTLGSDER RIKMLWALRE RITEALSRDG
YVYKYDLSLP LDRLYDLVGD LRARLGPSAK HVVGYGHLGD GNLHLNVTSE AFSTSLLGAL
EPYVYEWTAG QRGSVSAEHG LGFKKKDVLG YSKPPEALQL MRQLKALLDP KGILNPYKML
PTHA
