ID A0A292YKX8_9BACL Unreviewed; 335 AA.
AC A0A292YKX8;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE SubName: Full=D-glycerate dehydrogenase {ECO:0000313|EMBL:GAX89826.1};
GN ORFNames=EFBL_1451 {ECO:0000313|EMBL:GAX89826.1};
OS Effusibacillus lacus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Alicyclobacillaceae;
OC Effusibacillus.
OX NCBI_TaxID=1348429 {ECO:0000313|EMBL:GAX89826.1, ECO:0000313|Proteomes:UP000217785};
RN [1] {ECO:0000313|Proteomes:UP000217785}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=skLN1 {ECO:0000313|Proteomes:UP000217785};
RA Watanabe M., Kojima H., Fukui M.;
RT "Draft genome sequence of Effusibacillus lacus strain skLN1.";
RL Submitted (JUL-2017) 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:GAX89826.1}.
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DR EMBL; BDUF01000032; GAX89826.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A292YKX8; -.
DR OrthoDB; 9805416at2; -.
DR Proteomes; UP000217785; 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:UP000217785}.
FT DOMAIN 5..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 335 AA; 37304 MW; 99547856EA01DC93 CRC64;
MKPKVYITRK LPEEVVSRIR EVCEIRMWEE EEVPVPRFVL ENEIAKIDGL YCLLTETIDR
TLLEKAPKLK VVSNMAVGYN NIEVSAATDR GILVTNTPGV LTETTADLTF ALLMATARRI
VESSGFLRSG QWKTWSPMLL TGQDIHGATL GIIGLGRIGE ALARRAKGFD MRLLYHNRSR
KPDAENRLGL EYTDMETLLR ESDFVCVMTP YTPETHNLIG KAQLALMKKN AVLINTARGG
IVNEDDLYEA LKKGTIWAAG LDVFEQEPIP LNHPLLTLPN VVTLPHIGSA SVKTRLKMAH
LAADNLLQAL SGQRPAHPVN PEVLKQNRSL ALRQN
//
