ID L0EBX7_THECK Unreviewed; 318 AA.
AC L0EBX7;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Phosphoglycerate dehydrogenase-like oxidoreductase {ECO:0000313|EMBL:AGA57129.1};
GN OrderedLocusNames=Theco_0942 {ECO:0000313|EMBL:AGA57129.1};
OS Thermobacillus composti (strain DSM 18247 / JCM 13945 / KWC4).
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Thermobacillus.
OX NCBI_TaxID=717605 {ECO:0000313|EMBL:AGA57129.1, ECO:0000313|Proteomes:UP000010795};
RN [1] {ECO:0000313|Proteomes:UP000010795}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18247 / JCM 13945 / KWC4
RC {ECO:0000313|Proteomes:UP000010795};
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Teshima H., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Anderson I.,
RA Woyke T.;
RT "Complete sequence of chromosome of Thermobacillus composti KWC4.";
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|RuleBase:RU003719}.
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DR EMBL; CP003255; AGA57129.1; -; Genomic_DNA.
DR RefSeq; WP_015253887.1; NC_019897.1.
DR AlphaFoldDB; L0EBX7; -.
DR STRING; 717605.Theco_0942; -.
DR KEGG; tco:Theco_0942; -.
DR eggNOG; COG0111; Bacteria.
DR HOGENOM; CLU_019796_1_0_9; -.
DR OrthoDB; 9805416at2; -.
DR Proteomes; UP000010795; 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; cd05300; 2-Hacid_dh_1; 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; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43333; 2-HACID_DH_C DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43333:SF1; 2-HACID_DH_C DOMAIN-CONTAINING PROTEIN; 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.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719};
KW Reference proteome {ECO:0000313|Proteomes:UP000010795}.
FT DOMAIN 40..310
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 105..279
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 318 AA; 34870 MW; E8F9981D79393F03 CRC64;
MGTILCLHGF GPEEQEKIRR AAPGATIVFG RSAEIGPDVY RDAEAVCGWN DRVAEICLQE
GAKLRWVQTW SAGIDSLPLE KLRQRGVLLT DAAGVHSVAV AETALAHMLG LTRGIHIAVR
SQMAGEWHRP SELSELYGRT ALIVGAGAIG TRIAELARAF GMRTIGIRRT PAPQPAYDRV
DGMDKLDEAI AESDYIVNVL PDTPETRGIF DEARFRLMKP TAFFINVGRG ASVKTEALVE
ALRERRIAGA GLDVFEEEPL PSGHPLWALD NVILTPHTAG HTNRLKERVA DLFAANLEIY
LRGETDRLIN LVNYDKGY
//
