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Database: UniProt
Entry: D2RJU7
LinkDB: D2RJU7
Original site: D2RJU7 
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   16-JAN-2019, entry version 50.
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 / VR4).
OC   Bacteria; Firmicutes; Negativicutes; Acidaminococcales;
OC   Acidaminococcaceae; Acidaminococcus.
OX   NCBI_TaxID=591001;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25085 / DSM 20731 / 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.,
RA   Liolios K., Pati A., Ivanova N., Mavromatis K., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Jeffries C.D., Brettin T.,
RA   Rohde M., Goker M., Bristow J., Eisen J.A., Markowitz V.,
RA   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
RT   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,
CC         ChEBI:CHEBI:15801, ChEBI:CHEBI:16810, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945; EC=1.1.1.399;
CC         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}.
DR   EMBL; CP001859; ADB47349.1; -; Genomic_DNA.
DR   RefSeq; WP_012938338.1; NC_013740.1.
DR   ProteinModelPortal; D2RJU7; -.
DR   STRING; 591001.Acfer_0976; -.
DR   EnsemblBacteria; ADB47349; ADB47349; Acfer_0976.
DR   KEGG; afn:Acfer_0976; -.
DR   eggNOG; ENOG4105C5I; Bacteria.
DR   eggNOG; COG1052; LUCA.
DR   HOGENOM; HOG000136695; -.
DR   KO; K03778; -.
DR   OMA; MRIACYG; -.
DR   OrthoDB; 1638924at2; -.
DR   BioCyc; AFER591001:G1GH7-1028-MONOMER; -.
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   Complete proteome; NAD; Oxidoreductase; Reference proteome.
FT   CHAIN         1    331       (R)-2-hydroxyglutarate dehydrogenase.
FT                                /FTId=PRO_0000445607.
FT   NP_BIND     156    157       NAD. {ECO:0000250|UniProtKB:P26297}.
FT   NP_BIND     206    207       NAD. {ECO:0000250|UniProtKB:P26297}.
FT   NP_BIND     233    235       NAD. {ECO:0000250|UniProtKB:P26297}.
FT   ACT_SITE    235    235       {ECO:0000250|UniProtKB:P26297}.
FT   ACT_SITE    264    264       {ECO:0000250|UniProtKB:P26297}.
FT   ACT_SITE    297    297       Proton donor.
FT                                {ECO:0000250|UniProtKB:P26297}.
FT   BINDING     176    176       NAD. {ECO:0000250|UniProtKB:P26297}.
FT   BINDING     212    212       NAD. {ECO:0000250|UniProtKB:P26297}.
FT   BINDING     259    259       NAD. {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
//
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