ID Q6D054_PECAS Unreviewed; 308 AA.
AC Q6D054;
DT 16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT 16-AUG-2004, sequence version 1.
DT 27-MAR-2024, entry version 94.
DE SubName: Full=D-isomer specific 2-hydroxyacid dehydrogenase {ECO:0000313|EMBL:CAG76844.1};
GN OrderedLocusNames=ECA3947 {ECO:0000313|EMBL:CAG76844.1};
OS Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) (Erwinia
OS carotovora subsp. atroseptica).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Pectobacterium.
OX NCBI_TaxID=218491 {ECO:0000313|EMBL:CAG76844.1, ECO:0000313|Proteomes:UP000007966};
RN [1] {ECO:0000313|EMBL:CAG76844.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SCRI1043 {ECO:0000313|EMBL:CAG76844.1};
RA Bell K.S., Sebaihia M., Pritchard L., Holden M., Hyman L.J., Holeva M.C.,
RA Thomson N.R., Bentley S.D., Churcher C., Mungall K., Atkin R., Bason N.,
RA Brooks K., Chillingworth T., Clark K., Doggett J., Fraser A., Hance Z.,
RA Hauser H., Jagels K., Moule S., Norbertczak H., Ormond D., Price C.,
RA Quail M.A., Sanders M., Walker D., Whitehead S., Salmond G.P.C.,
RA Birch P.R.J., Barrell B.G., Parkhill J., Toth I.K.;
RT "The genome sequence of the enterobacterial phytopathogen Erwinia
RT carotovora subsp. atroseptica SCRI1043 and functional genomic
RT identification of novel virulence factors.";
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
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; BX950851; CAG76844.1; -; Genomic_DNA.
DR RefSeq; WP_011095441.1; NC_004547.2.
DR AlphaFoldDB; Q6D054; -.
DR STRING; 218491.ECA3947; -.
DR KEGG; eca:ECA3947; -.
DR PATRIC; fig|218491.5.peg.4010; -.
DR eggNOG; COG0111; Bacteria.
DR HOGENOM; CLU_019796_1_0_6; -.
DR OrthoDB; 9787219at2; -.
DR Proteomes; UP000007966; Chromosome.
DR GO; GO:0051287; F:NAD binding; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000007966}.
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; 33764 MW; 290A41404511699B CRC64;
MTAILLLDSR ADEIGSILNH GAPELELVLS NGTAEQAASC PIWLGEPDTA AALLAQGAKP
KWLQSTWAGF KPLLADGLPR DYRLSRAVGV FGQPIAEYVI AYMLRHELRL GERQVSQEER
RWDHRLPGSL ADKNVLIVGA GEIGCEVAGF LRPFGVELYG IVSTPRLRPD FKRIMSLAEL
PAAVPEADYV INLLPDTSAT TDIYDANLFA AMKPSALFIN VGRGSAVVDD DLRSALRDAQ
IAGAVLDVFR QEPLPYSHPF WKTPNLTLTA HIAGPMVPGL MGRLFLDNFS RFHADNTLRG
EVDFSREY
//