ID D7LVK2_ARALL Unreviewed; 488 AA.
AC D7LVK2;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=L-2-hydroxyglutarate dehydrogenase, mitochondrial {ECO:0000256|ARBA:ARBA00041137};
DE EC=1.1.99.2 {ECO:0000256|ARBA:ARBA00038878};
GN ORFNames=ARALYDRAFT_907131 {ECO:0000313|EMBL:EFH52641.1};
OS Arabidopsis lyrata subsp. lyrata (Lyre-leaved rock-cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=81972 {ECO:0000313|Proteomes:UP000008694};
RN [1] {ECO:0000313|Proteomes:UP000008694}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. MN47 {ECO:0000313|Proteomes:UP000008694};
RX PubMed=21478890; DOI=10.1038/ng.807;
RA Hu T.T., Pattyn P., Bakker E.G., Cao J., Cheng J.-F., Clark R.M.,
RA Fahlgren N., Fawcett J.A., Grimwood J., Gundlach H., Haberer G.,
RA Hollister J.D., Ossowski S., Ottilar R.P., Salamov A.A., Schneeberger K.,
RA Spannagl M., Wang X., Yang L., Nasrallah M.E., Bergelson J.,
RA Carrington J.C., Gaut B.S., Schmutz J., Mayer K.F.X., Van de Peer Y.,
RA Grigoriev I.V., Nordborg M., Weigel D., Guo Y.-L.;
RT "The Arabidopsis lyrata genome sequence and the basis of rapid genome size
RT change.";
RL Nat. Genet. 43:476-481(2011).
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; GL348717; EFH52641.1; -; Genomic_DNA.
DR RefSeq; XP_002876382.1; XM_002876336.1.
DR AlphaFoldDB; D7LVK2; -.
DR STRING; 81972.D7LVK2; -.
DR EnsemblPlants; scaffold_502835.1; scaffold_502835.1; scaffold_502835.1.
DR Gramene; scaffold_502835.1; scaffold_502835.1; scaffold_502835.1.
DR eggNOG; KOG2665; Eukaryota.
DR HOGENOM; CLU_024775_1_0_1; -.
DR Proteomes; UP000008694; 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:SF4; 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 Reference proteome {ECO:0000313|Proteomes:UP000008694}.
FT DOMAIN 86..484
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
SQ SEQUENCE 488 AA; 54225 MW; D16E98F66D67E2D6 CRC64;
MDRVRNEERW KHKPETAAFS LIRLRKLGLQ NKNKKMLACL GRKWMRLSTM NLKPTWNFVN
AVDASRTIVR GISGGGAETV AKERVDTVVI GAGVVGLAVA RELSRRGREV LILEAASSFG
TVTSSRNSEV VHAGIYYPPN SLKAKFCVRG RELLYRYCSE YEIPHKKIGK LIVATGSSEI
PKLDLLMHLG TQNGVSGLRM LDGFEAMRME PQLRCVKALL SPESGILDSH SFMLSLVEKS
FDFMVYRDNN NLRLQGEAEN NHATFSYNTV VLNGHVEEKK MHLFVADTRF SESQCEAEAQ
LQLIPNLVVN SAGLGAQALA KRFHGLDHRF VPSSHYARGC YFTLSGTKAP PFNKLVYPIP
EEGGLGVHVT VDLNGLVKFG PDVEWIECAD DTSSFLNKFD YRVNPQRAEK LYPEIRKYYP
DLKDGSLEPG YSGIRPKLSG PKQSPADFVI QGEETHGVPG FVNLFGIESP GLTSSLAIAE
HIANKLLR
//
