ID   LHGD_ECOLU              Reviewed;         422 AA.
AC   B7N6P4;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   23-FEB-2022, entry version 54.
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=ygaF {ECO:0000312|EMBL:CAR14155.1};
GN   Synonyms=lhgD {ECO:0000255|HAMAP-Rule:MF_00990};
GN   OrderedLocusNames=ECUMN_2984 {ECO:0000312|EMBL:CAR14155.1};
OS   Escherichia coli O17:K52:H18 (strain UMN026 / ExPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585056;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UMN026 / ExPEC;
RX   PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA   Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA   Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA   Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA   Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA   Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA   Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA   Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT   "Organised genome dynamics in the Escherichia coli species results in
RT   highly diverse adaptive paths.";
RL   PLoS Genet. 5:E1000344-E1000344(2009).
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; CU928163; CAR14155.1; -; Genomic_DNA.
DR   RefSeq; WP_000271983.1; NC_011751.1.
DR   RefSeq; YP_002413677.1; NC_011751.1.
DR   STRING; 585056.ECUMN_2984; -.
DR   EnsemblBacteria; CAR14155; CAR14155; ECUMN_2984.
DR   KEGG; eum:ECUMN_2984; -.
DR   PATRIC; fig|585056.7.peg.3160; -.
DR   HOGENOM; CLU_024775_0_1_6; -.
DR   OMA; GVHFTRM; -.
DR   Proteomes; UP000007097; Chromosome.
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_0000454866"
SQ   SEQUENCE   422 AA;  46067 MW;  6A339BDEA0865BEB CRC64;
     MYDFVIIGGG IIGMSTAMQL IDVYPDARIA LLEKESGPAC HQTGHNSGVI HAGVYYTPGS
     LKAQFCLAGN RATKAFCDQN GIRYDNCGKM LVATSELEME RMRALWERTA ANGIEREWLN
     AEELREREPN ITGLGGIFVP SSGIVSYREV TAAMAKIFQA RGGEIIYNAE VSGLSEHKNG
     VVIRTRQGGE YEASTLISCS GLMADRLVKM LGLEPGFIIC PFRGEYFRLA PEHNQIVNHL
     IYPIPDPAMP FLGVHLTRMI DGSVTVGPNA VLAFKREGYR KRDFSFSDTL EILGSSGIRR
     VLQNHLRSGL GEMKNSLCKS GYLRLVQKYC PRLSLSDLQP WPAGVRAQAV SPDGKLIDDF
     LFVTTPRTIH TCNAPSPAAT SAIPIGAHIV SKVQTLLASQ SNPGRTLRAA RSVDALHAAF
     NQ