ID E0E256_9FIRM Unreviewed; 332 AA.
AC E0E256;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=4-phosphoerythronate dehydrogenase {ECO:0000313|EMBL:EFM64995.1};
DE EC=1.1.1.290 {ECO:0000313|EMBL:EFM64995.1};
GN Name=pdxB {ECO:0000313|EMBL:EFM64995.1};
GN ORFNames=HMPREF0634_1387 {ECO:0000313|EMBL:EFM64995.1};
OS Peptostreptococcus stomatis DSM 17678.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC Peptostreptococcus.
OX NCBI_TaxID=596315 {ECO:0000313|EMBL:EFM64995.1, ECO:0000313|Proteomes:UP000003244};
RN [1] {ECO:0000313|EMBL:EFM64995.1, ECO:0000313|Proteomes:UP000003244}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17678 {ECO:0000313|EMBL:EFM64995.1,
RC ECO:0000313|Proteomes:UP000003244};
RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Nelson K.E.;
RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00005854,
CC 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:EFM64995.1}.
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DR EMBL; ADGQ01000032; EFM64995.1; -; Genomic_DNA.
DR RefSeq; WP_007788835.1; NZ_ADGQ01000032.1.
DR AlphaFoldDB; E0E256; -.
DR STRING; 596315.HMPREF0634_1387; -.
DR GeneID; 84800303; -.
DR eggNOG; COG1052; Bacteria.
DR OrthoDB; 9805416at2; -.
DR Proteomes; UP000003244; 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 CDD; cd12186; LDH; 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; IPR029753; D-isomer_DH_CS.
DR InterPro; IPR029752; D-isomer_DH_CS1.
DR InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43026; 2-HYDROXYACID DEHYDROGENASE HOMOLOG 1-RELATED; 1.
DR PANTHER; PTHR43026:SF1; 2-HYDROXYACID DEHYDROGENASE HOMOLOG 1-RELATED; 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; PS00065; D_2_HYDROXYACID_DH_1; 1.
DR PROSITE; PS00670; D_2_HYDROXYACID_DH_2; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719};
KW Reference proteome {ECO:0000313|Proteomes:UP000003244}.
FT DOMAIN 8..331
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 112..299
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 332 AA; 36575 MW; 0CFDF1B19F5BE08C CRC64;
MKILAYHVQG YEEKAFKKWS EENGVQVDLE YGLITPESIE KAKGYDGITT QQVIPVKDEE
IFKKMKEYGL TQVASRTAGV DMFDLKTARK YGISVTNVPR YSPNAIAELA VTHAMTLLRN
IGHIRAAQFK GDFTWNKDLI SKEIRSCTVG IIGTGRIGLT AATLFKGLGA KVIGFDEFKN
PGADGILEYR DTVEALLEEA DVVSLHLPLT DGTYHMINKD RIKHMKDHAI LVNTGRGGLV
NIDDVVEALE SGKIKGAALD VLECETLYVN QKIDPKKIEG TVVETLMGMD NVVLTGHFAF
FTETAVDNMV STALDNLKVE IETGKVQNCM NA
//
