LHGD_ECOLI
ID LHGD_ECOLI Reviewed; 422 AA.
AC P37339; P76622; P77020;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 3.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=L-2-hydroxyglutarate dehydrogenase {ECO:0000303|PubMed:30498244};
DE Short=L2HG dehydrogenase {ECO:0000303|PubMed:30498244};
DE EC=1.1.5.13 {ECO:0000269|PubMed:30498244};
DE AltName: Full=L2HG:quinone oxidoreductase {ECO:0000303|PubMed:30498244};
GN Name=lhgD {ECO:0000303|PubMed:30498244};
GN Synonyms=lhgO {ECO:0000303|PubMed:18390652}, ygaF;
GN OrderedLocusNames=b2660, JW2635;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 219-422.
RC STRAIN=K12 / JM103 / ATCC 39403 / DSM 2829 / KCTC 1112 / NCIMB 12044;
RX PubMed=8297211; DOI=10.1007/bf00245306;
RA Niegemann E., Schulz A., Bartsch K.;
RT "Molecular organization of the Escherichia coli gab cluster: nucleotide
RT sequence of the structural genes gabD and gabP and expression of the GABA
RT permease gene.";
RL Arch. Microbiol. 160:454-460(1993).
RN [5]
RP IDENTIFICATION.
RX PubMed=7984428; DOI=10.1093/nar/22.22.4756;
RA Borodovsky M., Rudd K.E., Koonin E.V.;
RT "Intrinsic and extrinsic approaches for detecting genes in a bacterial
RT genome.";
RL Nucleic Acids Res. 22:4756-4767(1994).
RN [6]
RP INDUCTION.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=14731280; DOI=10.1046/j.1365-2958.2003.03867.x;
RA Metzner M., Germer J., Hengge R.;
RT "Multiple stress signal integration in the regulation of the complex sigma
RT S-dependent csiD-ygaF-gabDTP operon in Escherichia coli.";
RL Mol. Microbiol. 51:799-811(2004).
RN [7]
RP COFACTOR.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=18390652; DOI=10.1128/jb.01977-07;
RA Kalliri E., Mulrooney S.B., Hausinger R.P.;
RT "Identification of Escherichia coli YgaF as an L-2-hydroxyglutarate
RT oxidase.";
RL J. Bacteriol. 190:3793-3798(2008).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY, AND SUBCELLULAR LOCATION.
RC STRAIN=K12 / BW25113;
RX PubMed=30498244; DOI=10.1038/s41467-018-07563-6;
RA Knorr S., Sinn M., Galetskiy D., Williams R.M., Wang C., Mueller N.,
RA Mayans O., Schleheck D., Hartig J.S.;
RT "Widespread bacterial lysine degradation proceeding via glutarate and L-2-
RT hydroxyglutarate.";
RL Nat. Commun. 9:5071-5071(2018).
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. {ECO:0000269|PubMed:30498244}.
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:0000269|PubMed:30498244};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58665;
CC Evidence={ECO:0000305|PubMed:30498244};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00990,
CC ECO:0000269|PubMed:18390652, ECO:0000269|PubMed:30498244};
CC -!- PATHWAY: Amino-acid degradation. {ECO:0000305|PubMed:30498244}.
CC -!- INTERACTION:
CC P37339; P0A9L5: ppiC; NbExp=3; IntAct=EBI-555990, EBI-555953;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:30498244}.
CC -!- INDUCTION: Expression is induced by RpoS during carbon starvation and
CC at stationary phase. Is also regulated by cAMP-CRP. Repressed by CsiR.
CC Makes part of the operon glaH-lhgD-gabDTP.
CC {ECO:0000269|PubMed:14731280}.
CC -!- SIMILARITY: Belongs to the L2HGDH family. {ECO:0000255|HAMAP-
CC Rule:MF_00990}.
CC -!- CAUTION: Was originally thought to be an oxidase, i.e. using molecular
CC oxygen for oxidation of L-2-hydroxyglutarate and producing hydrogen
CC peroxide. However, no O2 consumption could be detected with L2HG using
CC the purified recombinant and active enzyme (PubMed:30498244).
CC {ECO:0000269|PubMed:30498244, ECO:0000305|PubMed:18390652}.
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DR EMBL; U00096; AAC75707.2; -; Genomic_DNA.
DR EMBL; AP009048; BAA16521.1; -; Genomic_DNA.
DR EMBL; M88334; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; E65045; E65045.
DR RefSeq; NP_417146.2; NC_000913.3.
DR RefSeq; WP_000271909.1; NZ_LN832404.1.
DR AlphaFoldDB; P37339; -.
DR SMR; P37339; -.
DR BioGRID; 4263106; 11.
DR BioGRID; 852377; 1.
DR DIP; DIP-12096N; -.
DR IntAct; P37339; 4.
DR STRING; 511145.b2660; -.
DR jPOST; P37339; -.
DR PaxDb; P37339; -.
DR PRIDE; P37339; -.
DR DNASU; 948069; -.
DR EnsemblBacteria; AAC75707; AAC75707; b2660.
DR EnsemblBacteria; BAA16521; BAA16521; BAA16521.
DR GeneID; 948069; -.
DR KEGG; ecj:JW2635; -.
DR KEGG; eco:b2660; -.
DR PATRIC; fig|1411691.4.peg.4081; -.
DR EchoBASE; EB2288; -.
DR eggNOG; COG0579; Bacteria.
DR HOGENOM; CLU_024775_0_1_6; -.
DR InParanoid; P37339; -.
DR OMA; GVHFTRM; -.
DR PhylomeDB; P37339; -.
DR BioCyc; EcoCyc:EG12387-MON; -.
DR BioCyc; MetaCyc:EG12387-MON; -.
DR SABIO-RK; P37339; -.
DR PRO; PR:P37339; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IDA:EcoliWiki.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0003973; F:(S)-2-hydroxy-acid oxidase activity; IBA:GO_Central.
DR GO; GO:0140696; F:(S)-2-hydroxyglutarate dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0047545; F:2-hydroxyglutarate dehydrogenase activity; IDA:EcoCyc.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IDA:EcoCyc.
DR GO; GO:0019477; P:L-lysine catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006554; P:lysine catabolic process; EXP:EcoCyc.
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 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Electron transport; FAD; Flavoprotein;
KW Membrane; Oxidoreductase; Reference proteome; Transport.
FT CHAIN 1..422
FT /note="L-2-hydroxyglutarate dehydrogenase"
FT /id="PRO_0000169295"
SQ SEQUENCE 422 AA; 46082 MW; 8E13E890B0A7365C CRC64;
MYDFVIIGGG IIGMSTAMQL IDVYPDARIA LLEKESAPAC HQTGHNSGVI HAGVYYTPGS
LKAQFCLAGN RATKAFCDQN GIRYDNCGKM LVATSDLEME RMRALWERTA ANGIEREWLN
ADELREREPN ITGLGGIFVP SSGIVSYRDV TAAMAKIFQS RGGEIIYNAE VSGLNEHKNG
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
