ID E0SHX1_DICD3 Unreviewed; 308 AA.
AC E0SHX1;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=D-3-phosphoglycerate dehydrogenase {ECO:0000313|EMBL:ADN00180.1};
DE EC=1.1.1.95 {ECO:0000313|EMBL:ADN00180.1};
GN OrderedLocusNames=Dda3937_00450 {ECO:0000313|EMBL:ADN00180.1};
OS Dickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937)).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Dickeya.
OX NCBI_TaxID=198628 {ECO:0000313|EMBL:ADN00180.1, ECO:0000313|Proteomes:UP000006859};
RN [1] {ECO:0000313|EMBL:ADN00180.1, ECO:0000313|Proteomes:UP000006859}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3937 {ECO:0000313|EMBL:ADN00180.1,
RC ECO:0000313|Proteomes:UP000006859};
RX PubMed=21217001; DOI=10.1128/JB.01513-10;
RA Glasner J.D., Yang C.H., Reverchon S., Hugouvieux-Cotte-Pattat N.,
RA Condemine G., Bohin J.P., Van Gijsegem F., Yang S., Franza T., Expert D.,
RA Plunkett G. III, San Francisco M.J., Charkowski A.O., Py B., Bell K.,
RA Rauscher L., Rodriguez-Palenzuela P., Toussaint A., Holeva M.C., He S.Y.,
RA Douet V., Boccara M., Blanco C., Toth I., Anderson B.D., Biehl B.S.,
RA Mau B., Flynn S.M., Barras F., Lindeberg M., Birch P.R., Tsuyumu S.,
RA Shi X., Hibbing M., Yap M.N., Carpentier M., Dassa E., Umehara M.,
RA Kim J.F., Rusch M., Soni P., Mayhew G.F., Fouts D.E., Gill S.R.,
RA Blattner F.R., Keen N.T., Perna N.T.;
RT "Genome sequence of the plant-pathogenic bacterium Dickeya dadantii 3937.";
RL J. Bacteriol. 193:2076-2077(2011).
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DR EMBL; CP002038; ADN00180.1; -; Genomic_DNA.
DR AlphaFoldDB; E0SHX1; -.
DR STRING; 198628.Dda3937_00450; -.
DR KEGG; ddd:Dda3937_00450; -.
DR PATRIC; fig|198628.6.peg.3921; -.
DR eggNOG; COG0111; Bacteria.
DR HOGENOM; CLU_019796_1_0_6; -.
DR OrthoDB; 9787219at2; -.
DR Proteomes; UP000006859; Chromosome.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0004617; F:phosphoglycerate dehydrogenase activity; IEA:UniProtKB-EC.
DR CDD; cd05300; 2-Hacid_dh_1; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
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; PF02826; 2-Hacid_dh_C; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 4: Predicted;
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:ADN00180.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006859}.
FT DOMAIN 101..273
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 308 AA; 33487 MW; 61EF4D1DDD356363 CRC64;
MTSILLLDSR ADELRDVLHE AAPDLPLVIG SGEAAQAQAC EIWVGEPDKA AQLLAQGVKP
RWLQSTWAGY KPLLAKGLPR DYRLSRAVGV FGQPIAEYVL AYLLQHELHL SQRLWSQQRG
EWKKILPGSL FGRRVLIVGA GDIGREVAAF LQPFGVELYG VAYSPREMPM FARVEGLSSL
TSAVASADYV INILPDTPAT TDIYHAGVFA AMKPSALFIN VGRGTAVVDT DLCTALHEGQ
IAGAVLDVFR KEPLPGDHPF WRTPNLTITA HVAGPLVPAR LGKLFLDNLP RFRQGLALAG
EVGFDKSY
//
