ID   LHGD_SALHO              Reviewed;         422 AA.
AC   A0A5Y6MCT2;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   12-AUG-2020, sequence version 1.
DT   23-FEB-2022, entry version 5.
DE   RecName: Full=L-2-hydroxyglutarate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00990};
DE            Short=L2HG dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00990};
DE            EC=1.1.5.13 {ECO:0000255|HAMAP-Rule:MF_00990};
DE   AltName: Full=L2HG:quinone oxidoreductase {ECO:0000255|HAMAP-Rule:MF_00990};
GN   Name=lhgO {ECO:0000312|EMBL:ECK7332852.1};
GN   Synonyms=lhgD {ECO:0000255|HAMAP-Rule:MF_00990};
GN   ORFNames=FRN20_18950 {ECO:0000312|EMBL:ECK7332852.1};
OS   Salmonella houtenae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=59205;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=779338;
RA   Ashton P.M., Dallman T., Nair S., De Pinna E., Peters T., Grant K.;
RL   Submitted (AUG-2019) 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       to alpha-ketoglutarate and couples to the respiratory chain by feeding
CC       electrons from the reaction into the membrane quinone pool. Functions
CC       in a L-lysine degradation pathway that proceeds via cadaverine,
CC       glutarate and L-2-hydroxyglutarate (By similarity). Also displays some
CC       oxidase activity in vitro on L-2-hydroxyglutarate with O2 as the
CC       electron acceptor, but this activity is most likely not physiological
CC       (PubMed:34555022). {ECO:0000255|HAMAP-Rule:MF_00990,
CC       ECO:0000269|PubMed:34555022}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-2-hydroxyglutarate + a quinone = 2-oxoglutarate + a
CC         quinol; Xref=Rhea:RHEA:58664, ChEBI:CHEBI:16782, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:24646, ChEBI:CHEBI:132124; EC=1.1.5.13;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00990};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00990};
CC   -!- PATHWAY: Amino-acid degradation. {ECO:0000255|HAMAP-Rule:MF_00990}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_00990}.
CC   -!- SIMILARITY: Belongs to the L2HGDH family. {ECO:0000255|HAMAP-
CC       Rule:MF_00990}.
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DR   EMBL; AAJCYV010000028; ECK7332852.1; -; Genomic_DNA.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0140696; F:(S)-2-hydroxyglutarate dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0047545; F:2-hydroxyglutarate dehydrogenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0019477; P:L-lysine catabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.50.50.60; -; 1.
DR   HAMAP; MF_00990; L_hydroxyglutarate_dehydrogenase; 1.
DR   InterPro; IPR006076; FAD-dep_OxRdtase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR030862; L2HG_DH.
DR   Pfam; PF01266; DAO; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Electron transport; FAD; Flavoprotein;
KW   Membrane; Oxidoreductase; Transport.
FT   CHAIN           1..422
FT                   /note="L-2-hydroxyglutarate dehydrogenase"
FT                   /id="PRO_0000454865"
SQ   SEQUENCE   422 AA;  46028 MW;  681FBDD64FF2937A CRC64;
     MYDFVIIGGG IIGMSTAMQL IDVYPDARIA LLEKESAPAC HQTGHNSGVI HAGVYYTPGS
     LKARFCLAGN LATKTFCDQN NIRYDTCGKM LVATSELEMA RMRALWERTA ANGLEREWLS
     AAELREREPN IIGLGGIFVP SSGIVSYRDV ATAMANRFQA KGGEIIYHAE VSALTEHAAG
     VVIRTSQGRE IETATLIGCA GLMADRLVKM LGVEPGFIIC PFRGEYFRLA PRHNRIVNHL
     IYPIPDPAMP FLGVHLTRMI DGSVTVGPNA VLALKREGYR KRDVSFTDTL EVFRSAGIRR
     VLKNHLLSGL GEMKNSLCKS GYLRRVQKYC PSLTVNDLQP WPAGVRAQAV SPDGKLIDDF
     LFVATPRSIH TCNAPSPAAT SAIPIGAHIV SKVQALRESQ SNPGRTLRAA RNVDTLHAAF
     TR