ID A0A0C2BYJ1_9BILA Unreviewed; 147 AA.
AC A0A0C2BYJ1;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=D-2-hydroxyglutarate dehydrogenase, mitochondrial {ECO:0000256|ARBA:ARBA00039639};
DE EC=1.1.99.39 {ECO:0000256|ARBA:ARBA00039003};
GN ORFNames=ANCDUO_27628 {ECO:0000313|EMBL:KIH42387.1};
OS Ancylostoma duodenale.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC Ancylostomatinae; Ancylostoma.
OX NCBI_TaxID=51022 {ECO:0000313|EMBL:KIH42387.1, ECO:0000313|Proteomes:UP000054047};
RN [1] {ECO:0000313|EMBL:KIH42387.1, ECO:0000313|Proteomes:UP000054047}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Zhejiang {ECO:0000313|EMBL:KIH42387.1,
RC ECO:0000313|Proteomes:UP000054047};
RA Mitreva M.;
RT "Draft genome of the parsitic nematode Ancylostoma duodenale.";
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
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};
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DR EMBL; KN795780; KIH42387.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C2BYJ1; -.
DR Proteomes; UP000054047; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR Gene3D; 3.30.70.2740; -; 1.
DR InterPro; IPR004113; FAD-bd_oxidored_4_C.
DR InterPro; IPR016164; FAD-linked_Oxase-like_C.
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 SUPFAM; SSF55103; FAD-linked oxidases, C-terminal domain; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000054047}.
FT DOMAIN 2..145
FT /note="FAD-binding oxidoreductase/transferase type 4 C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02913"
SQ SEQUENCE 147 AA; 16494 MW; 242A7A5FBE18649D CRC64;
MTAQSVAESA AMWRLRESAP LAVAADGFVF KNDVSLPLKH FYGLTEEVRA RCSSMTKRIV
TYGHLGDGNS HLNIVAEEYS KELYDKLYPF IYEWVNAHDG SISAEHGIGQ LKLPYSGLGK
SPAERELVRR IKSMFDPHGI LNPYKSF
//
