ID U2TI09_9ACTN Unreviewed; 334 AA.
AC U2TI09;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Putative D-lactate dehydrogenase LdhA {ECO:0000313|EMBL:ERL12694.1};
GN ORFNames=HMPREF1248_1593 {ECO:0000313|EMBL:ERL12694.1};
OS Coriobacteriaceae bacterium BV3Ac1.
OC Bacteria; Actinomycetota; Coriobacteriia; Coriobacteriales;
OC Coriobacteriaceae.
OX NCBI_TaxID=1111135 {ECO:0000313|EMBL:ERL12694.1, ECO:0000313|Proteomes:UP000016652};
RN [1] {ECO:0000313|EMBL:ERL12694.1, ECO:0000313|Proteomes:UP000016652}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BV3AC1 {ECO:0000313|Proteomes:UP000016652};
RA Durkin A.S., Haft D.R., McCorrison J., Torralba M., Gillis M., Haft D.H.,
RA Methe B., Sutton G., Nelson K.E.;
RL Submitted (SEP-2013) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ERL12694.1}.
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; AWUP01000006; ERL12694.1; -; Genomic_DNA.
DR AlphaFoldDB; U2TI09; -.
DR PATRIC; fig|1111135.3.peg.707; -.
DR eggNOG; COG1052; Bacteria.
DR OrthoDB; 117809at2; -.
DR Proteomes; UP000016652; 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; 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; 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:UP000016652}.
FT DOMAIN 4..325
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 115..300
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 334 AA; 36717 MW; F5249F1836AA9828 CRC64;
MRILFYGTAS YDQESFEKEI ADFPDVKIDY TETNLTPMTA ALARGYDAVC AFVNADISAM
TLEILKGFGI GLVLMRCAGF DVVNVPMATE LGIKVTRVPA YSPEAIAEHA MALGQAANRR
IHKGYIRVRE NNFALNGLVG ETLYGKTAGI VGTGRIGAAL CRICKGYGMT VLGADLYPNQ
ALVDEEHVVD EYVDYDELYR RSDFISLHAF LNKDSYHLID DEAIDKMKPG VIFVNTGRGA
LVDTQALIRG IISGKIGAAG LDVYEEENAN VYQNRSGEIV DSVTARLCSF PNVVMTSHQA
FFTHEALSQI ARVTLENAQH YAREEEFIPR SVVC
//
