ID Q3YYJ7_SHISS Unreviewed; 444 AA.
AC Q3YYJ7;
DT 27-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2005, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE RecName: Full=L-2-hydroxyglutarate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00990};
DE Short=L2HG dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00990};
DE EC=1.1.5.13 {ECO:0000256|HAMAP-Rule:MF_00990};
DE AltName: Full=L2HG:quinone oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00990};
GN Name=ygaF {ECO:0000313|EMBL:AAZ89415.1};
GN Synonyms=lhgD {ECO:0000256|HAMAP-Rule:MF_00990};
GN OrderedLocusNames=SSON_2804 {ECO:0000313|EMBL:AAZ89415.1};
OS Shigella sonnei (strain Ss046).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=300269 {ECO:0000313|EMBL:AAZ89415.1, ECO:0000313|Proteomes:UP000002529};
RN [1] {ECO:0000313|EMBL:AAZ89415.1, ECO:0000313|Proteomes:UP000002529}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ss046 {ECO:0000313|EMBL:AAZ89415.1,
RC ECO:0000313|Proteomes:UP000002529};
RX PubMed=16275786; DOI=10.1093/nar/gki954;
RA Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA Jin Q.;
RT "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT bacillary dysentery.";
RL Nucleic Acids Res. 33:6445-6458(2005).
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:0000256|HAMAP-Rule:MF_00990}.
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:0000256|HAMAP-Rule:MF_00990};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|HAMAP-Rule:MF_00990};
CC -!- PATHWAY: Amino-acid degradation. {ECO:0000256|HAMAP-Rule:MF_00990}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC Rule:MF_00990}.
CC -!- SIMILARITY: Belongs to the L2HGDH family.
CC {ECO:0000256|ARBA:ARBA00037941, ECO:0000256|HAMAP-Rule:MF_00990}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000038; AAZ89415.1; -; Genomic_DNA.
DR AlphaFoldDB; Q3YYJ7; -.
DR KEGG; ssn:SSON_2804; -.
DR HOGENOM; CLU_024775_0_1_6; -.
DR Proteomes; UP000002529; 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; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 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_bact.
DR PANTHER; PTHR43104; L-2-HYDROXYGLUTARATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43104:SF2; L-2-HYDROXYGLUTARATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR Pfam; PF01266; DAO; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_00990};
KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_00990};
KW Electron transport {ECO:0000256|HAMAP-Rule:MF_00990};
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|HAMAP-Rule:MF_00990};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|HAMAP-
KW Rule:MF_00990};
KW Membrane {ECO:0000256|HAMAP-Rule:MF_00990, ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_00990}; Reference proteome {ECO:0000313|Proteomes:UP000002529};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Transport {ECO:0000256|HAMAP-Rule:MF_00990}.
FT TRANSMEM 23..43
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 25..412
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
SQ SEQUENCE 444 AA; 48590 MW; 445BCCDC8E56FED4 CRC64;
MAISLTPLTT TRRISKRKGI ERMYDFVIIG GGIIGMSTAM QLIDVYPDAR IALLEKESGP
ACHQTGHNSG VIHAGVYYTP GSLKAQFCLA GNRATKAFCD QNGIRYDNCG KMLVATSQLE
MERMRALWER TAANGIEREW INAVELRERE PNITGLGGIF VPSSGIVSYR EVTAAMAKIF
QARGGEIIYN AEVSALSKHK NGVVIRTRQG GEYEASTLIS CSGLMADRLV KMLGLEPGFI
ICPFRGEYFR LAPEHNQIVN HLIYPIPDPA MPFLGVHLTR MIDGSVTVGP NAVLAFKREG
YRKRDFSFSD TLEILSSSGI RRVLQNHLRS GLGEMKNSLC KSGYLRLVQK YCPRLSLSDL
QPWPAGVRAQ AVSPDGKLID DFLFVTTPRT IHTCNAPSPA ATSAIPIGAH IVSKVQTLLA
SQSNPGRTLR AARSVDALHA AFNQ
//
