ID   L2HDH_ACCSB             Reviewed;         388 AA.
AC   A0A011QK89;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   11-JUN-2014, sequence version 1.
DT   03-AUG-2022, entry version 22.
DE   RecName: Full=L-2-hydroxyglutarate dehydrogenase {ECO:0000305};
DE            EC=1.1.99.2 {ECO:0000250|UniProtKB:S2DJ52};
GN   Name=lhgO_1 {ECO:0000312|EMBL:EXI89792.1};
GN   ORFNames=AW11_01282 {ECO:0000312|EMBL:EXI89792.1};
OS   Accumulibacter sp. (strain BA-93).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Candidatus Accumulibacter;
OC   unclassified Candidatus Accumulibacter.
OX   NCBI_TaxID=1454004;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BA-93;
RA   Skennerton C.T., Barr J.J., Slater F.R., Bond P.L., Tyson G.W.;
RT   "Expanding our view of genomic diversity in Candidatus Accumulibacter
RT   clades.";
RL   Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, AND IN VITRO ACTIVITY.
RX   PubMed=34555022; DOI=10.1371/journal.pcbi.1009446;
RA   Rembeza E., Engqvist M.K.M.;
RT   "Experimental and computational investigation of enzyme functional
RT   annotations uncovers misannotation in the EC 1.1.3.15 enzyme class.";
RL   PLoS Comput. Biol. 17:e1009446-e1009446(2021).
CC   -!- FUNCTION: Catalyzes the dehydrogenation of L-2-hydroxyglutarate (L2HG
CC       or(S)-2-hydroxyglutarate) to 2-oxoglutarate (alpha-ketoglutarate) (By
CC       similarity). Also displays some oxidase activity in vitro on L-2-
CC       hydroxyglutarate with O2 as the electron acceptor, but this activity is
CC       most likely not physiological (PubMed:34555022).
CC       {ECO:0000250|UniProtKB:S2DJ52, ECO:0000269|PubMed:34555022}.
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:0000250|UniProtKB:S2DJ52};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000250|UniProtKB:Q9H9P8};
CC   -!- SIMILARITY: Belongs to the L2HGDH family. {ECO:0000305}.
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DR   EMBL; JEMY01000013; EXI89792.1; -; Genomic_DNA.
DR   STRING; 1454004.AW11_01282; -.
DR   EnsemblBacteria; EXI89792; EXI89792; AW11_01282.
DR   PATRIC; fig|1454004.3.peg.1337; -.
DR   eggNOG; COG0579; Bacteria.
DR   Proteomes; UP000022141; Unassembled WGS sequence.
DR   GO; GO:0003973; F:(S)-2-hydroxy-acid oxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0047545; F:2-hydroxyglutarate dehydrogenase activity; IEA:RHEA.
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   3: Inferred from homology;
KW   FAD; Flavoprotein; Oxidoreductase; Reference proteome.
FT   CHAIN           1..388
FT                   /note="L-2-hydroxyglutarate dehydrogenase"
FT                   /id="PRO_0000454863"
SQ   SEQUENCE   388 AA;  40540 MW;  BE147168B26922AD CRC64;
     MESIEAVVIG AGVVGLACAR ELARRGFETV ILERHGAFGT ETSARNSEVI HAGLYYPTDS
     LKARLCVAGR QQLYAFCATH AISHQRCGKL VVATSPAQES RLAALQKQGE ANGVDDLQRL
     SAAEARALEP GLACTAALLS PSTGIVDSHG LMLALLGDAE TAGAALALHS PLLRGSLDAN
     TPGIVLESGG ADGLRFKARR VINAAGLWAP QVAASLAGFP RTLIPANFHA KGSYYALTGR
     TPFSRLVYPL PEAGGLGVHL TLDLGGQARF GPDVEWLPDP TPGQPIDEPD YRVDPARADA
     FYAEIRRYWP ALPDAALTPA YAGIRPKIVG PGAPAADFLI QGPAQHGIAG LVNLFGIESP
     GLTACLAIAE RAADAADGTR ERQFRAHG