ID   L2HDH_ACHAE             Reviewed;         369 AA.
AC   A0A0M7LBC1;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   09-DEC-2015, sequence version 1.
DT   03-AUG-2022, entry version 19.
DE   RecName: Full=L-2-hydroxyglutarate dehydrogenase {ECO:0000305};
DE            EC=1.1.99.2 {ECO:0000250|UniProtKB:S2DJ52};
GN   Name=lhgO {ECO:0000312|EMBL:CUJ61502.1};
GN   ORFNames=ERS370000_04855 {ECO:0000312|EMBL:CUJ61502.1};
OS   Achromobacter aegrifaciens.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Achromobacter.
OX   NCBI_TaxID=1287736;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2789STDY5608625;
RG   Pathogen Informatics;
RL   Submitted (SEP-2015) 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; CYTK01000009; CUJ61502.1; -; Genomic_DNA.
DR   RefSeq; WP_054457440.1; NZ_CYTK01000009.1.
DR   EnsemblBacteria; CUJ61502; CUJ61502; ERS370000_04855.
DR   Proteomes; UP000044098; 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.
FT   CHAIN           1..369
FT                   /note="L-2-hydroxyglutarate dehydrogenase"
FT                   /id="PRO_0000454864"
SQ   SEQUENCE   369 AA;  38740 MW;  0F0BAFD86F4F1753 CRC64;
     MSVDVDCVVI GAGVVGLAIA RALAQSGREV LVAEATEAIG TGTSSRNSEV IHAGIYYPAG
     SLKARLCVRG KHLLYSYCAE RGVPYKRLGK LIVATTTEQA AQLEGIAQRA RANGVDDLQF
     ISGEDAMRLE PALRCTAALS SPSTGIVDSH ALMLSFQGDA ENAGAQCVFH TPLVSGRVRP
     EGGFELQFGG DDAMTLSCNV LINSAGLHAP ALARRIDGLP ASNIPKDYLC KGSYFTLSGR
     APFSRLIYPV PQHAGLGVHL TLDLGGQAKF GPDTEWVETE DYTLDPARAD VFYEAVRSYW
     PALPDDALAP GYTGIRPKIS GPHEPAADFV IAGPAAHGVP GLVNLFGIES PGLTSSLALA
     EETLARLNG