ID D4G858_RIEPU Unreviewed; 330 AA.
AC D4G858;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=D-lactate dehydrogenase {ECO:0000313|EMBL:ADD79527.1};
DE EC=1.1.1.28 {ECO:0000313|EMBL:ADD79527.1};
GN OrderedLocusNames=RIEPE_0262 {ECO:0000313|EMBL:ADD79527.1};
OS Riesia pediculicola (strain USDA).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Riesia.
OX NCBI_TaxID=515618 {ECO:0000313|EMBL:ADD79527.1, ECO:0000313|Proteomes:UP000001700};
RN [1] {ECO:0000313|EMBL:ADD79527.1, ECO:0000313|Proteomes:UP000001700}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=USDA {ECO:0000313|EMBL:ADD79527.1,
RC ECO:0000313|Proteomes:UP000001700};
RA Kirkness E.F.;
RT "Genome sequence of Riesia pediculicola USDA.";
RL Submitted (MAY-2008) 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; CP001085; ADD79527.1; -; Genomic_DNA.
DR RefSeq; WP_013087517.1; NC_014109.1.
DR AlphaFoldDB; D4G858; -.
DR STRING; 515618.RIEPE_0262; -.
DR KEGG; rip:RIEPE_0262; -.
DR eggNOG; COG1052; Bacteria.
DR HOGENOM; CLU_019796_1_1_6; -.
DR OrthoDB; 9805416at2; -.
DR Proteomes; UP000001700; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0008720; F:D-lactate dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
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 NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719}.
FT DOMAIN 5..323
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 133..277
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 330 AA; 37880 MW; 2B22B6D26CC7B447 CRC64;
MKIVLYSVRS YEKIFFEKLN RKNGFNLDIQ YLSCRLNKNT IEKSNGSKVI CTFVHDMIDE
EILQFLFISG VRLIALRCTG FDHVDLESAK KIGIKVVHVP GYSPESIAEY AVSLILYASR
GLYLSSNEEI EEVRDTLKDQ VIGVIGTGRI GSITLKILKG FGSKLLAYDP IPNREIVSET
GINYVSMDDL LSYSHIISLH CPLNQENYHL INKDSCQRMK DGVILINTSR GELIDSESVL
LAMKSGKIRF FCSDVFEKEY FLENENNCPL KEEHQVYKDI FRSFKKQRNF FFTRHRAFLT
KSSLRKIAKI TLSNINDFRN GSSSLKYELT
//
