ID C0CXU2_9FIRM Unreviewed; 321 AA.
AC C0CXU2;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=4-phosphoerythronate dehydrogenase {ECO:0000313|EMBL:EEG56091.1};
DE EC=1.1.1.290 {ECO:0000313|EMBL:EEG56091.1};
GN Name=pdxB {ECO:0000313|EMBL:EEG56091.1};
GN ORFNames=CLOSTASPAR_01817 {ECO:0000313|EMBL:EEG56091.1};
OS [Clostridium] asparagiforme DSM 15981.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Enterocloster.
OX NCBI_TaxID=518636 {ECO:0000313|EMBL:EEG56091.1, ECO:0000313|Proteomes:UP000004756};
RN [1] {ECO:0000313|EMBL:EEG56091.1, ECO:0000313|Proteomes:UP000004756}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15981 {ECO:0000313|EMBL:EEG56091.1,
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:EEG56091.1, ECO:0000313|Proteomes:UP000004756}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15981 {ECO:0000313|EMBL:EEG56091.1,
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {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:EEG56091.1}.
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DR EMBL; ACCJ01000095; EEG56091.1; -; Genomic_DNA.
DR RefSeq; WP_007709209.1; NZ_GG657591.1.
DR AlphaFoldDB; C0CXU2; -.
DR HOGENOM; CLU_019796_1_3_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 GO; GO:0003714; F:transcription corepressor activity; IEA:InterPro.
DR CDD; cd05299; CtBP_dh; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR InterPro; IPR043322; CtBP.
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; PTHR43761:SF1; 2-HACID_DH DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR43761; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_1G13630); 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; PS00670; D_2_HYDROXYACID_DH_2; 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}.
FT DOMAIN 14..315
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 107..283
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 321 AA; 35831 MW; 2CBB187F9A428261 CRC64;
MLVVITDYQY DNIDAERRII GEAGFELRDY QVKETKEMIP LVKEADAIVT QYSDVSREVI
GQLEHCKMII KYGIGVNNID TKAATEKGIY VCNVPDYGVE EVSDHAVTMM LALGKKMQIL
EKAFREGDWG YSSTMPLYRL RDCTLGLVGF GRIPQLVAKK MAGFGLRILA YDPFVDEEKA
RAMGVRPVDL ETILRESDFI SVHVPLNEGT RHLIGRESFK KMKQTAFVVN TARGGVIDEK
ALVEALNAGE IAGAGVDVYE EEPVSPDNPL LHMDNVIATP HCAWYSETAI TTLQRKVAEE
VVNVLQGNEP FNCVNRGELN R
//
