ID A0A366XVW3_9BACI Unreviewed; 330 AA.
AC A0A366XVW3;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=D-glycerate dehydrogenase {ECO:0000313|EMBL:RBW68274.1};
GN ORFNames=DS031_17275 {ECO:0000313|EMBL:RBW68274.1};
OS Bacillus taeanensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=273032 {ECO:0000313|EMBL:RBW68274.1, ECO:0000313|Proteomes:UP000253314};
RN [1] {ECO:0000313|EMBL:RBW68274.1, ECO:0000313|Proteomes:UP000253314}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BH030017 {ECO:0000313|EMBL:RBW68274.1,
RC ECO:0000313|Proteomes:UP000253314};
RA Liu R., Huang Z.;
RT "Lottiidibacillus patelloidae gen. nov., sp. nov., isolated from the
RT intestinal tract of a marine limpet and the reclassification of B.
RT taeanensis BH030017T, B. algicola KMM 3737T and B. hwajinpoensis SW-72T as
RT genus Lottiidibacillus.";
RL Submitted (JUL-2018) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RBW68274.1}.
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DR EMBL; QOCW01000022; RBW68274.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A366XVW3; -.
DR OrthoDB; 9805416at2; -.
DR Proteomes; UP000253314; Unassembled WGS sequence.
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; 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; 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:UP000253314}.
FT DOMAIN 7..320
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 110..288
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 330 AA; 36504 MW; 04D137CE26886C4F CRC64;
MKPNVYITRK LPLPVVEKIK EVCEVRMWDE EDIPVPKEVL EKEIENVDGL YCLLTESIDK
ELLSKANNLK VISNMAVGYN NIDVDAASGK GILVTNTPGV LTETTADLTF ALMMAAGRRL
VEASDYLKAG KWKTWSPMML TGQDMYGATL GIIGLGRIGE SVAKRAKGFD MDVLYYNRSR
KKEAEEELGI HYRDLETLLK ESDFVCVLTP YTPETENLIG KEQLALMKSS AVLVNTARGG
IVNEGDLYHA LKSGEIFAAG LDVFKEEPIS LDHPLLTLPN VVVLPHIGSA SKKTRMNMAN
LAADNLLQGV ERKTPKHLVN KHVIEEGLSY
//
