ID D1PIB3_9FIRM Unreviewed; 316 AA.
AC D1PIB3;
DT 09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT 09-FEB-2010, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=4-phosphoerythronate dehydrogenase {ECO:0000313|EMBL:EFB77581.1};
DE EC=1.1.1.290 {ECO:0000313|EMBL:EFB77581.1};
GN Name=pdxB {ECO:0000313|EMBL:EFB77581.1};
GN ORFNames=SUBVAR_04078 {ECO:0000313|EMBL:EFB77581.1};
OS Subdoligranulum variabile DSM 15176.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Subdoligranulum.
OX NCBI_TaxID=411471 {ECO:0000313|EMBL:EFB77581.1, ECO:0000313|Proteomes:UP000003438};
RN [1] {ECO:0000313|EMBL:EFB77581.1, ECO:0000313|Proteomes:UP000003438}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15176 {ECO:0000313|EMBL:EFB77581.1,
RC ECO:0000313|Proteomes:UP000003438};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (DEC-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 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:EFB77581.1}.
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DR EMBL; ACBY02000009; EFB77581.1; -; Genomic_DNA.
DR RefSeq; WP_007045525.1; NZ_GG704769.1.
DR AlphaFoldDB; D1PIB3; -.
DR STRING; 411471.SUBVAR_04078; -.
DR GeneID; 78307455; -.
DR eggNOG; COG0111; Bacteria.
DR HOGENOM; CLU_019796_1_3_9; -.
DR OrthoDB; 9805416at2; -.
DR Proteomes; UP000003438; 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; cd12161; GDH_like_1; 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; 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; PS00065; D_2_HYDROXYACID_DH_1; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000003438}.
FT DOMAIN 22..315
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 112..285
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 316 AA; 33188 MW; 9016E43E7A041432 CRC64;
MSKIVILESL GISAEELAAR KAPFEAQGHT FAEFARSTDP AVLADEAKDA DALILANMPL
PGAVIEGCDK LKFIDVAFTG VDHIGLDAAR AKGITVSNAS GYSNEAVAEL VLGMALSLSR
NLTAVEQRCR DGKTKDGLVG FELAGKTVGI VGLGKIGSRT AELFHALGCP ILAHSRTVHA
DAPDYVRQVS LEDLLAQSDL VVLHCPLNDS TRGMINAEKL AMMKSTALLI NVARGPVVVA
GDLADALDQG VIAGAGIDVF DKEPPLDAGE PLLHCKNCLV TPHVAFATRE SMTLRAEIVF
DNLAAWLAGH PKNVVL
//
