ID Q97FN7_CLOAB Unreviewed; 326 AA.
AC Q97FN7;
DT 01-OCT-2001, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2001, sequence version 1.
DT 27-MAR-2024, entry version 120.
DE SubName: Full=D-lactate dehydrogenase {ECO:0000313|EMBL:AAK80638.1};
GN OrderedLocusNames=CA_C2691 {ECO:0000313|EMBL:AAK80638.1};
OS Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS / VKM B-1787).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=272562 {ECO:0000313|EMBL:AAK80638.1, ECO:0000313|Proteomes:UP000000814};
RN [1] {ECO:0000313|EMBL:AAK80638.1, ECO:0000313|Proteomes:UP000000814}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787
RC {ECO:0000313|Proteomes:UP000000814};
RX PubMed=11466286; DOI=10.1128/JB.183.16.4823-4838.2001;
RA Nolling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA Doucette-Stamm L., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA Smith D.R.;
RT "Genome sequence and comparative analysis of the solvent-producing
RT bacterium Clostridium acetobutylicum.";
RL J. Bacteriol. 183:4823-4838(2001).
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; AE001437; AAK80638.1; -; Genomic_DNA.
DR PIR; C97231; C97231.
DR RefSeq; NP_349298.1; NC_003030.1.
DR RefSeq; WP_010965979.1; NC_003030.1.
DR AlphaFoldDB; Q97FN7; -.
DR STRING; 272562.CA_C2691; -.
DR GeneID; 44999182; -.
DR KEGG; cac:CA_C2691; -.
DR PATRIC; fig|272562.8.peg.2883; -.
DR eggNOG; COG1052; Bacteria.
DR HOGENOM; CLU_019796_1_1_9; -.
DR OrthoDB; 9805416at2; -.
DR Proteomes; UP000000814; Chromosome.
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; cd12185; HGDH_LDH_like; 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:UP000000814}.
FT DOMAIN 4..324
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 109..295
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 326 AA; 36770 MW; 1968211551786BBE CRC64;
MKILAFEVRE DEKLYFEKYA AQYNCEITCI EDPLTFNNLK IVEGYDGISI LGKSHITCDL
EDSLKSLNVN FCSTRTVGFD HIDITHAHEI GFKIANTNYP PTGVAEHTVM LMLMSLRHYK
QAMWRGHVND YSLGGLQGRE LNTLTVGIVG TGKIGQCVIK YLSNFGCKIL AYDMHENTDV
TKYAKYTDLD TIITSSDIIS LHTPLLEGTY HLINDEKINR MKDNVVLINC ARGELMDIDA
LIRGVEAKKI GALGLDVIEG EKDLYHQDKR TDIISNQKIA YLRQFPNVIL TQHMAFYTDI
AVESMVKCSI EAIHDFIKTG NSKTSI
//
