ID F8JB99_HYPSM Unreviewed; 322 AA.
AC F8JB99;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=Glycerate dehydrogenase {ECO:0000313|EMBL:CCB67082.1};
DE EC=1.1.1.29 {ECO:0000313|EMBL:CCB67082.1};
GN OrderedLocusNames=HYPMC_3872 {ECO:0000313|EMBL:CCB67082.1};
OS Hyphomicrobium sp. (strain MC1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Hyphomicrobiaceae; Hyphomicrobium.
OX NCBI_TaxID=717785 {ECO:0000313|EMBL:CCB67082.1, ECO:0000313|Proteomes:UP000000494};
RN [1] {ECO:0000313|Proteomes:UP000000494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MC1 {ECO:0000313|Proteomes:UP000000494};
RA Genoscope.;
RT "The complete genome of Hyphomicrobium sp. MC1.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00005854,
CC ECO:0000256|RuleBase:RU003719}.
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DR EMBL; FQ859181; CCB67082.1; -; Genomic_DNA.
DR RefSeq; WP_013949475.1; NC_015717.1.
DR AlphaFoldDB; F8JB99; -.
DR STRING; 717785.HYPMC_3872; -.
DR KEGG; hmc:HYPMC_3872; -.
DR eggNOG; COG1052; Bacteria.
DR HOGENOM; CLU_019796_1_2_5; -.
DR Proteomes; UP000000494; Chromosome.
DR GO; GO:0008465; F:glycerate dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR CDD; cd05301; GDH; 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; IPR029752; D-isomer_DH_CS1.
DR InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR10996:SF178; 2-HYDROXYACID DEHYDROGENASE YGL185C-RELATED; 1.
DR PANTHER; PTHR10996; 2-HYDROXYACID DEHYDROGENASE-RELATED; 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; PS00065; D_2_HYDROXYACID_DH_1; 1.
DR PROSITE; PS00670; D_2_HYDROXYACID_DH_2; 1.
DR PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719};
KW Reference proteome {ECO:0000313|Proteomes:UP000000494}.
FT DOMAIN 6..318
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 112..290
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 322 AA; 35511 MW; FF59BB1D3DA63B46 CRC64;
MSKKKILITW PLPEAAMARA RETYDVIAHG DNPKITVDEM LETAKSVDAI LLTLNEKCPA
AVIEKIPENI KCISTFSIGF DHIDLEACKK RGIKVGNAPH GVTVATAEIA MLLLLGSARR
ASEGEKMIRT RSWPGWQPLQ LVGQRLDNKK LGIYGFGKIG QALAQRARGF DMEIHYYDIY
RAKPEVEAKY NATYHDSLDS LLKISQFFSI NAPSTPETRG FFNKATIEKL PQGAIVVNTA
RGDLVNDEDT IAALKSGRLA YAGLDVFAGE PKINEGYYDL PNTFLFPHLG SAAIEARNQM
GFEALDNIDA FFAGKDMPFK LA
//
