ID C0CSX8_9FIRM Unreviewed; 317 AA.
AC C0CSX8;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=4-phosphoerythronate dehydrogenase {ECO:0000313|EMBL:EEG57854.1};
DE EC=1.1.1.290 {ECO:0000313|EMBL:EEG57854.1};
GN Name=pdxB {ECO:0000313|EMBL:EEG57854.1};
GN ORFNames=CLOSTASPAR_00072 {ECO:0000313|EMBL:EEG57854.1};
OS [Clostridium] asparagiforme DSM 15981.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Enterocloster.
OX NCBI_TaxID=518636 {ECO:0000313|EMBL:EEG57854.1, ECO:0000313|Proteomes:UP000004756};
RN [1] {ECO:0000313|EMBL:EEG57854.1, ECO:0000313|Proteomes:UP000004756}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15981 {ECO:0000313|EMBL:EEG57854.1,
RC ECO:0000313|Proteomes:UP000004756};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EEG57854.1, ECO:0000313|Proteomes:UP000004756}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15981 {ECO:0000313|EMBL:EEG57854.1,
RC ECO:0000313|Proteomes:UP000004756};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Clostridium asparagiforme (DSM 15981).";
RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00005854}.
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:EEG57854.1}.
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DR EMBL; ACCJ01000005; EEG57854.1; -; Genomic_DNA.
DR RefSeq; WP_007705061.1; NZ_GG657587.1.
DR AlphaFoldDB; C0CSX8; -.
DR HOGENOM; CLU_876330_0_0_9; -.
DR Proteomes; UP000004756; Unassembled WGS sequence.
DR GO; GO:0033711; F:4-phosphoerythronate dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
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; PTHR42789; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_6G10090); 1.
DR PANTHER; PTHR42789:SF1; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_6G10090); 1.
DR Pfam; PF02826; 2-Hacid_dh_C; 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:0000313|EMBL:EEG57854.1}.
FT DOMAIN 115..285
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 317 AA; 34268 MW; 4181E877AB812E79 CRC64;
MEHREIRSIA GEDNPDTRAV QEQVRRFAEG LGCRYIWTPG AVGGGSIDLA GVDALIVDGD
EMNVLLEDCS EAGVKVVVRR TGSWQEGDLL RALNLGIRLA AVPEDGGTEM GEMALSLILA
LRRKVIRHHQ QVMEGQWVRH AASSVMGSTI GILGLENGGR ELAQMMGAMG CRVQVWRPDP
EKAGAAPYPE AELETLCREA DIVSVHLSYG QAGNCIVGGD LIGWMKRTAV LISMGDGRLV
DTEALYTALK EKRIEAAALD TLERTVIEGE NPLRTLRNVI LTPGIGRFTR EELVRTGCEA
ARIAAELLSE SDGSVTK
//
