ID   HGDH_ACIFV              Reviewed;         331 AA.
AC   D2RJU7;
DT   07-NOV-2018, integrated into UniProtKB/Swiss-Prot.
DT   02-MAR-2010, sequence version 1.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=(R)-2-hydroxyglutarate dehydrogenase {ECO:0000303|PubMed:23000002};
DE            Short=HGDH {ECO:0000303|PubMed:23000002};
DE            EC=1.1.1.399 {ECO:0000269|PubMed:23000002};
GN   Name=hgdH {ECO:0000303|PubMed:23000002};
GN   OrderedLocusNames=Acfer_0976 {ECO:0000312|EMBL:ADB47349.1};
OS   Acidaminococcus fermentans (strain ATCC 25085 / DSM 20731 / CCUG 9996 / CIP
OS   106432 / VR4).
OC   Bacteria; Firmicutes; Negativicutes; Acidaminococcales; Acidaminococcaceae;
OC   Acidaminococcus.
OX   NCBI_TaxID=591001;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25085 / DSM 20731 / CCUG 9996 / CIP 106432 / VR4;
RX   PubMed=21304687; DOI=10.4056/sigs.1002553;
RA   Chang Y.J., Pukall R., Saunders E., Lapidus A., Copeland A., Nolan M.,
RA   Glavina Del Rio T., Lucas S., Chen F., Tice H., Cheng J.F., Han C.,
RA   Detter J.C., Bruce D., Goodwin L., Pitluck S., Mikhailova N., Liolios K.,
RA   Pati A., Ivanova N., Mavromatis K., Chen A., Palaniappan K., Land M.,
RA   Hauser L., Jeffries C.D., Brettin T., Rohde M., Goker M., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Acidaminococcus fermentans type strain
RT   (VR4).";
RL   Stand. Genomic Sci. 3:1-14(2010).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=23000002; DOI=10.1016/j.ab.2012.09.009;
RA   Yu X., Bresser J., Schall I., Djurdjevic I., Buckel W., Wang X.,
RA   Engel P.C.;
RT   "Development of a satisfactory and general continuous assay for
RT   aminotransferases by coupling with (R)-2-hydroxyglutarate dehydrogenase.";
RL   Anal. Biochem. 431:127-131(2012).
CC   -!- FUNCTION: Catalyzes the reduction of 2-oxoglutarate to 2-
CC       hydroxyglutarate. {ECO:0000269|PubMed:23000002}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-2-hydroxyglutarate + NAD(+) = 2-oxoglutarate + H(+) +
CC         NADH; Xref=Rhea:RHEA:49612, ChEBI:CHEBI:15378, ChEBI:CHEBI:15801,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC         EC=1.1.1.399; Evidence={ECO:0000269|PubMed:23000002};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=210 uM for 2-oxoglutarate {ECO:0000269|PubMed:23000002};
CC         Note=kcat is 290000 sec(-1). {ECO:0000269|PubMed:23000002};
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000305}.
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DR   EMBL; CP001859; ADB47349.1; -; Genomic_DNA.
DR   RefSeq; WP_012938338.1; NC_013740.1.
DR   AlphaFoldDB; D2RJU7; -.
DR   SMR; D2RJU7; -.
DR   STRING; 591001.Acfer_0976; -.
DR   EnsemblBacteria; ADB47349; ADB47349; Acfer_0976.
DR   KEGG; afn:Acfer_0976; -.
DR   eggNOG; COG1052; Bacteria.
DR   HOGENOM; CLU_019796_1_1_9; -.
DR   OMA; MRIACYG; -.
DR   OrthoDB; 1638924at2; -.
DR   Proteomes; UP000001902; Chromosome.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
DR   InterPro; IPR029753; D-isomer_DH_CS.
DR   InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF00389; 2-Hacid_dh; 1.
DR   Pfam; PF02826; 2-Hacid_dh_C; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE   1: Evidence at protein level;
KW   NAD; Oxidoreductase; Reference proteome.
FT   CHAIN           1..331
FT                   /note="(R)-2-hydroxyglutarate dehydrogenase"
FT                   /id="PRO_0000445607"
FT   ACT_SITE        235
FT                   /evidence="ECO:0000250|UniProtKB:P26297"
FT   ACT_SITE        264
FT                   /evidence="ECO:0000250|UniProtKB:P26297"
FT   ACT_SITE        297
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P26297"
FT   BINDING         156..157
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P26297"
FT   BINDING         176
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P26297"
FT   BINDING         206..207
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P26297"
FT   BINDING         212
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P26297"
FT   BINDING         233..235
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P26297"
FT   BINDING         259
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P26297"
SQ   SEQUENCE   331 AA;  36586 MW;  7574F226A4DBE60F CRC64;
     MKVLCYGVRD VELPIFEACN KEFGYDIKCV PDYLNTKETA EMAAGFDAVI LRGNCFANKQ
     NLDIYKKLGV KYILTRTAGT DHIDKEYAKE LGFPMAFVPR YSPNAIAELA VTQAMMLLRH
     TAYTTSRTAK KNFKVDAFMF SKEVRNCTVG VVGLGRIGRV AAQIFHGMGA TVIGEDVFEI
     KGIEDYCTQV SLDEVLEKSD IITIHAPYIK ENGAVVTRDF LKKMKDGAIL VNCARGQLVD
     TEAVIEAVES GKLGGYGCDV LDGEASVFGK DLEGQKLENP LFEKLVDLYP RVLITPHLGS
     YTDEAVKNMV EVSYQNLKDL AETGDCPNKI K