ID E1VJJ2_9GAMM Unreviewed; 323 AA.
AC E1VJJ2;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=Glycerate dehydrogenase {ECO:0000313|EMBL:CBL44984.1};
GN ORFNames=HDN1F_14010 {ECO:0000313|EMBL:CBL44984.1};
OS gamma proteobacterium HdN1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria.
OX NCBI_TaxID=83406 {ECO:0000313|EMBL:CBL44984.1, ECO:0000313|Proteomes:UP000002677};
RN [1] {ECO:0000313|EMBL:CBL44984.1, ECO:0000313|Proteomes:UP000002677}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HdN1 {ECO:0000313|Proteomes:UP000002677};
RA Widdel F., Rabus R., Grundmann O., Werner I., Schreiber F., Ehrenreich P.,
RA Behrends A., Wilkes H., Kube M., Reinhardt R., Zedelius J.;
RT "Alkane degradation by a new type of denitrifying bacterium with possible
RT involvement of the electron acceptor in substrate activation.";
RL Environ. Microbiol. 0:0-0(2010).
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|RuleBase:RU003719}.
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DR EMBL; FP929140; CBL44984.1; -; Genomic_DNA.
DR AlphaFoldDB; E1VJJ2; -.
DR STRING; 83406.HDN1F_14010; -.
DR KEGG; gpb:HDN1F_14010; -.
DR eggNOG; COG1052; Bacteria.
DR HOGENOM; CLU_019796_1_3_6; -.
DR OrthoDB; 9805416at2; -.
DR Proteomes; UP000002677; 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 CDD; cd12162; 2-Hacid_dh_4; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
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 PANTHER; PTHR43761:SF1; 2-HACID_DH DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR43761; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_1G13630); 1.
DR Pfam; PF00389; 2-Hacid_dh; 1.
DR Pfam; PF02826; 2-Hacid_dh_C; 1.
DR SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719};
KW Reference proteome {ECO:0000313|Proteomes:UP000002677}.
FT DOMAIN 34..322
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 107..298
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 323 AA; 35240 MW; 53F8071CCD5B38FF CRC64;
MKSVFLDRAS MGDGIHLDRL RAAAPALTEY DYTAPEQVAE RIADHDIAIT NKSRICAETM
ARCKQLKLIA VTATGLNNID MEAAHRHGIQ VANVQHYATP SIVQHTFSLM LALTTRLVDY
HNDVRSGEWA RSSNFCLLHH PIRELSGKTL GIVGHGDLGQ GVARAASAFG MHVKIAARPG
AHYSTDTPAV LESTDSQVER IPLMQLLPQV DVLSLHCLLS PATERLIGAP QLRLMRRDSL
LINTARGGLI DEQALADALR ERRIGGAGLD VLSEEPPTHP NPLLSGDLPN LIITPHCAWG
SCEARQRLLD HTANNIRDFL AGR
//
