ID E4N658_KITSK Unreviewed; 330 AA.
AC E4N658;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=Putative D-lactate dehydrogenase {ECO:0000313|EMBL:BAJ26689.1};
DE EC=1.1.1.28 {ECO:0000313|EMBL:BAJ26689.1};
GN Name=ldhA {ECO:0000313|EMBL:BAJ26689.1};
GN OrderedLocusNames=KSE_08500 {ECO:0000313|EMBL:BAJ26689.1};
OS Kitasatospora setae (strain ATCC 33774 / DSM 43861 / JCM 3304 / KCC A-0304
OS / NBRC 14216 / KM-6054) (Streptomyces setae).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Kitasatospora.
OX NCBI_TaxID=452652 {ECO:0000313|EMBL:BAJ26689.1, ECO:0000313|Proteomes:UP000007076};
RN [1] {ECO:0000313|EMBL:BAJ26689.1, ECO:0000313|Proteomes:UP000007076}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33774 / DSM 43861 / JCM 3304 / KCC A-0304 / NBRC 14216 /
RC KM-6054 {ECO:0000313|Proteomes:UP000007076};
RX PubMed=21059706; DOI=10.1093/dnares/dsq026;
RA Ichikawa N., Oguchi A., Ikeda H., Ishikawa J., Kitani S., Watanabe Y.,
RA Nakamura S., Katano Y., Kishi E., Sasagawa M., Ankai A., Fukui S.,
RA Hashimoto Y., Kamata S., Otoguro M., Tanikawa S., Nihira T., Horinouchi S.,
RA Ohnishi Y., Hayakawa M., Kuzuyama T., Arisawa A., Nomoto F., Miura H.,
RA Takahashi Y., Fujita N.;
RT "Genome sequence of Kitasatospora setae NBRC 14216T: an evolutionary
RT snapshot of the family Streptomycetaceae.";
RL DNA Res. 17:393-406(2010).
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; AP010968; BAJ26689.1; -; Genomic_DNA.
DR RefSeq; WP_014134008.1; NC_016109.1.
DR AlphaFoldDB; E4N658; -.
DR STRING; 452652.KSE_08500; -.
DR KEGG; ksk:KSE_08500; -.
DR PATRIC; fig|452652.3.peg.839; -.
DR eggNOG; COG1052; Bacteria.
DR HOGENOM; CLU_019796_1_1_11; -.
DR Proteomes; UP000007076; Chromosome.
DR GO; GO:0008720; F:D-lactate dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0051287; F:NAD binding; 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; 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:UP000007076}.
FT DOMAIN 9..325
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 330 AA; 35350 MW; B24EEFDAEDC83492 CRC64;
MEILAYGVLS DERPLLQDAL EQHRLRMLDV FLTADTAPLA AGFPVVSSSV NDTLDAGVLS
LLAAGGTKLI AQRSTGFNNI DLTAAAELGL TVARVSYYSP YAVAEHAWTL ALAVNRRLTR
ATTRSREFDF RLDGLMGRDI HGMTVGVIGT GKIGECFARI AAGFGTELLG WDVAENPACL
ELGMTYTELP ELLSRADLVS LHVPLLPATH HLIDAAALAR MKDDAILVNS SRGGLVDSTA
LVETLRAGRL SGVGLDVYEE ETGVFFTDQS IQGVTDDTLA RLVTFPQVLV TSHQAYYTRT
AVGQIIDATA RNIDDFAAGR TSENTLVPKS
//
