L2HDH_ARATH
ID L2HDH_ARATH Reviewed; 483 AA.
AC Q9LES4;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=L-2-hydroxyglutarate dehydrogenase, mitochondrial {ECO:0000305};
DE EC=1.1.99.2 {ECO:0000269|PubMed:26203119};
DE Flags: Precursor;
GN Name=L2HGDH {ECO:0000303|PubMed:26203119};
GN OrderedLocusNames=At3g56840 {ECO:0000312|Araport:AT3G56840};
GN ORFNames=T8M16_170 {ECO:0000312|EMBL:CAC00747.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP SUBCELLULAR LOCATION.
RX PubMed=24561575; DOI=10.1016/j.mito.2014.02.009;
RA Engqvist M.K., Esser C., Maier A., Lercher M.J., Maurino V.G.;
RT "Mitochondrial 2-hydroxyglutarate metabolism.";
RL Mitochondrion 19:275-281(2014).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=26203119; DOI=10.1093/pcp/pcv108;
RA Huedig M., Maier A., Scherrers I., Seidel L., Jansen E.E.,
RA Mettler-Altmann T., Engqvist M.K., Maurino V.G.;
RT "Plants possess a cyclic mitochondrial metabolic pathway similar to the
RT mammalian metabolic repair mechanism involving malate dehydrogenase and l-
RT 2-hydroxyglutarate dehydrogenase.";
RL Plant Cell Physiol. 56:1820-1830(2015).
CC -!- FUNCTION: Catalyzes the oxidation of (S)-2-hydroxyglutarate to 2-
CC oxoglutarate. Is specific for the (S) enantiomer and possesses very
CC poor activity toward (R)-2-hydroxyglutarate. Has no activity toward
CC related 2-hydroxy acids, such as glycolate, L-lactate or D-lactate.
CC {ECO:0000269|PubMed:26203119}.
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:0000269|PubMed:26203119};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:26203119};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.24 mM for (S)-2-hydroxyglutarate (with DCIP as acceptor
CC molecule) {ECO:0000269|PubMed:26203119};
CC Vmax=0.52 mmol/min/mg enzyme toward (S)-2-hydroxyglutarate (with DCIP
CC as acceptor molecule) {ECO:0000269|PubMed:26203119};
CC pH dependence:
CC Optimum pH is 7.4. {ECO:0000269|PubMed:26203119};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:24561575}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions. {ECO:0000269|PubMed:26203119}.
CC -!- SIMILARITY: Belongs to the L2HGDH family. {ECO:0000305}.
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DR EMBL; AL390921; CAC00747.1; -; Genomic_DNA.
DR EMBL; CP002686; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; T51272; T51272.
DR AlphaFoldDB; Q9LES4; -.
DR SMR; Q9LES4; -.
DR STRING; 3702.AT3G56840.1; -.
DR PaxDb; Q9LES4; -.
DR PRIDE; Q9LES4; -.
DR Araport; AT3G56840; -.
DR TAIR; locus:2103660; AT3G56840.
DR eggNOG; KOG2665; Eukaryota.
DR HOGENOM; CLU_024775_1_0_1; -.
DR InParanoid; Q9LES4; -.
DR PhylomeDB; Q9LES4; -.
DR BioCyc; ARA:AT3G56840-MON; -.
DR PRO; PR:Q9LES4; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LES4; baseline and differential.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0003973; F:(S)-2-hydroxy-acid oxidase activity; IMP:TAIR.
DR GO; GO:0047545; F:2-hydroxyglutarate dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0071949; F:FAD binding; IDA:UniProtKB.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR006076; FAD-dep_OxRdtase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR Pfam; PF01266; DAO; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 1: Evidence at protein level;
KW FAD; Flavoprotein; Mitochondrion; Oxidoreductase; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..67
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 68..483
FT /note="L-2-hydroxyglutarate dehydrogenase, mitochondrial"
FT /id="PRO_0000438327"
SQ SEQUENCE 483 AA; 53526 MW; E0C110BA3E32C747 CRC64;
MKHKPETAAF SLIRPLEAWA ANANKACNTK KMLPCLGRKW MRLSTRNLKP TWNLINVVDA
SKTIVRGISG GAETIAKERV DTVVIGAGVV GLAVARELSL RGREVLILDA ASSFGTVTSS
RNSEVVHAGI YYPPNSLKAK FCVRGRELLY KYCSEYEIPH KKIGKLIVAT GSSEIPKLDL
LMHLGTQNRV SGLRMLEGFE AMRMEPQLRC VKALLSPESG ILDTHSFMLS LVEKSFDFMV
YRDNNNLRLQ GEAQNNHATF SYNTVVLNGR VEEKKMHLYV ADTRFSESRC EAEAQLELIP
NLVVNSAGLG AQALAKRLHG LDHRFVPSSH YARGCYFTLS GIKAPPFNKL VYPIPEEGGL
GVHVTVDLNG LVKFGPDVEW IECTDDTSSF LNKFDYRVNP QRSEKFYPEI RKYYPDLKDG
SLEPGYSGIR PKLSGPKQSP ADFVIQGEET HGVPGLVNLF GIESPGLTSS LAIAEHIANK
FLR
