ID A0A1I6INQ1_9FIRM Unreviewed; 328 AA.
AC A0A1I6INQ1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=D-lactate dehydrogenase {ECO:0000313|EMBL:SFR68354.1};
GN ORFNames=SAMN05661086_00954 {ECO:0000313|EMBL:SFR68354.1};
OS Anaeromicropila populeti.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Anaeromicropila.
OX NCBI_TaxID=37658 {ECO:0000313|EMBL:SFR68354.1, ECO:0000313|Proteomes:UP000199659};
RN [1] {ECO:0000313|EMBL:SFR68354.1, ECO:0000313|Proteomes:UP000199659}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=743A {ECO:0000313|EMBL:SFR68354.1,
RC ECO:0000313|Proteomes:UP000199659};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FOYZ01000003; SFR68354.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I6INQ1; -.
DR STRING; 37658.SAMN05661086_00954; -.
DR OrthoDB; 9805416at2; -.
DR Proteomes; UP000199659; 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; cd12183; LDH_like_2; 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; PTHR43026; 2-HYDROXYACID DEHYDROGENASE HOMOLOG 1-RELATED; 1.
DR PANTHER; PTHR43026:SF1; 2-HYDROXYACID DEHYDROGENASE HOMOLOG 1-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:UP000199659}.
FT DOMAIN 7..325
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 110..294
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 328 AA; 36979 MW; 77BAED948D2340A5 CRC64;
MKTISFFDTK PYDKVYFDAY KAKYHIDIIY HETKLNKGSA ILAKNSQGVC AFVNDTLDRE
TLETLCESGI EIVAMRCAGY NNVDLKFAKG KIHIVRVPAY SPHAVAEATM GMLLTLNRKF
HRAYNRTREY NFSINGLNGF DLYGKTIGVV GTGQIGRIFI KICKGFGMNI LAYDPYPAQD
ADFQYVDFNE LCEKSDIISL HCPLTKESHY IINQKSIEKM KQGVYIINTS RGALIDSDDL
LENIKSGKIG GAALDVYEEE SDFFFEDLSN TIVHDDVLSR LISMPNVLVT SHQAFFTNEA
IENIAKTTLG NFQEFFDVGT LTNEVCYK
//
