ID D7GTD0_9FIRM Unreviewed; 322 AA.
AC D7GTD0;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=Lactate dehydrogenase and related dehydrogenases {ECO:0000313|EMBL:CBL41072.1};
DE EC=1.1.1.29 {ECO:0000313|EMBL:CBL41072.1};
GN ORFNames=CK3_13570 {ECO:0000313|EMBL:CBL41072.1};
OS butyrate-producing bacterium SS3/4.
OC Bacteria; Bacillota; Clostridia; Eubacteriales.
OX NCBI_TaxID=245014 {ECO:0000313|EMBL:CBL41072.1, ECO:0000313|Proteomes:UP000008961};
RN [1] {ECO:0000313|EMBL:CBL41072.1, ECO:0000313|Proteomes:UP000008961}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SS3/4 {ECO:0000313|EMBL:CBL41072.1,
RC ECO:0000313|Proteomes:UP000008961};
RG metaHIT consortium -- http://www.metahit.eu/;
RA Pajon A., Turner K., Parkhill J., Duncan S., Flint H.;
RT "The genome sequence of Clostridiales sp. SS3/4.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CBL41072.1, ECO:0000313|Proteomes:UP000008961}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SS3/4 {ECO:0000313|EMBL:CBL41072.1,
RC ECO:0000313|Proteomes:UP000008961};
RA Pajon A.;
RL Submitted (MAR-2010) 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; FP929062; CBL41072.1; -; Genomic_DNA.
DR AlphaFoldDB; D7GTD0; -.
DR KEGG; bprs:CK3_13570; -.
DR PATRIC; fig|245014.3.peg.3068; -.
DR HOGENOM; CLU_019796_1_3_9; -.
DR BioCyc; BBAC245014:G1314-1158-MONOMER; -.
DR Proteomes; UP000008961; Chromosome.
DR GO; GO:0008465; F:glycerate dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0051287; F:NAD binding; 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; IPR029752; D-isomer_DH_CS1.
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; 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}.
FT DOMAIN 19..320
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 110..289
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 322 AA; 35426 MW; 1ED27561B217C423 CRC64;
MKLVVLDGYT ENPGDLSWDA LKEFGDLTVY DRTSFTESPL IAERIGDAEI IITNKTPISR
ETIDKCPRIK LIAALATGYN VIDYNYAAEK GIPVVNVPTY GTASVSQFSI ALLLEICHHI
GHHDKTVHEG KWAENIDWCY WDYPLIELEG KTMGIIGFGR IGQAEGRIAK ALGMNVIAYD
LYPNESGRAI ADYVTQDELF AKADVISLHC NLTPENAGLI NRENIAKMKD GVILLNNARG
QLVNEVDLVE ALASGKVAAA GLDVVSTEPI KADNPLLKAP NCIITPHISW APKESRRRIM
DCTVENIRAF LNGKPVHVVN MK
//
