ID A0A498SDC0_ACAVI Unreviewed; 428 AA.
AC A0A498SDC0;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 11.
DE RecName: Full=L-2-hydroxyglutarate dehydrogenase, mitochondrial {ECO:0000256|ARBA:ARBA00041137};
DE EC=1.1.99.2 {ECO:0000256|ARBA:ARBA00038878};
GN ORFNames=NAV_LOCUS1876 {ECO:0000313|EMBL:VBB27046.1};
OS Acanthocheilonema viteae (Filarial nematode worm) (Dipetalonema viteae).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Acanthocheilonema.
OX NCBI_TaxID=6277 {ECO:0000313|EMBL:VBB27046.1, ECO:0000313|Proteomes:UP000276991};
RN [1] {ECO:0000313|EMBL:VBB27046.1, ECO:0000313|Proteomes:UP000276991}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Laetsch R D., Stevens L., Kumar S., Blaxter L. M.;
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-2-hydroxyglutarate + A = 2-oxoglutarate + AH2;
CC Xref=Rhea:RHEA:21252, ChEBI:CHEBI:13193, ChEBI:CHEBI:16782,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:17499; EC=1.1.99.2;
CC Evidence={ECO:0000256|ARBA:ARBA00036066};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the L2HGDH family.
CC {ECO:0000256|ARBA:ARBA00037941}.
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DR EMBL; UPTC01000173; VBB27046.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A498SDC0; -.
DR STRING; 6277.A0A498SDC0; -.
DR Proteomes; UP000276991; Unassembled WGS sequence.
DR GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:UniProt.
DR Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR006076; FAD-dep_OxRdtase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR PANTHER; PTHR43104; L-2-HYDROXYGLUTARATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43104:SF2; L-2-HYDROXYGLUTARATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR Pfam; PF01266; DAO; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000276991}.
FT DOMAIN 42..418
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
SQ SEQUENCE 428 AA; 47649 MW; 824C6E26C547C2D6 CRC64;
MNTTAFRLLT VSRIVPDFRA SILSRKKSFY STAAGSTTSE FDVAVVGGGI VGCATARQLK
IKNPELKVTL LEKEDHVAFH QSGHNSGVLH AGIYYAPGSL KAKLCVRGID LAYEYCDEYK
VPYKRIGKLI VAVEPVEIQR LEGLKALWSP YTGIVDWGLV TKSYAQDFEN RGGIVYTKYP
LKTLLLVGES EKENVANDYP VIIESEPSLS KIRCKYVITC CGLQSDRVAK LSRGSPDPKI
IPFRGEYLLL TSEEKKKAVT TNVYPVPDPR LPFLGVHFTP RMNGDVWLGP NAVLAYKREG
YKYSQISLPD LYDALTYRGM RKLIFKFFGY GMKELYRGIW IRAQVKQLQK FMPDLRISDV
ARGPAGVRAQ AIDPDGNLID DFIFDCGQGE LSHCVLHVRN APSPGATSSL AIAEMICEKA
STVFDLKH
//
