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Database: UniProt
Entry: D1PJ92_9FIRM
LinkDB: D1PJ92_9FIRM
Original site: D1PJ92_9FIRM 
ID   D1PJ92_9FIRM            Unreviewed;       331 AA.
AC   D1PJ92;
DT   09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT   09-FEB-2010, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   SubName: Full=4-phosphoerythronate dehydrogenase {ECO:0000313|EMBL:EFB77252.1};
DE            EC=1.1.1.290 {ECO:0000313|EMBL:EFB77252.1};
GN   Name=pdxB {ECO:0000313|EMBL:EFB77252.1};
GN   ORFNames=SUBVAR_04412 {ECO:0000313|EMBL:EFB77252.1};
OS   Subdoligranulum variabile DSM 15176.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Subdoligranulum.
OX   NCBI_TaxID=411471 {ECO:0000313|EMBL:EFB77252.1, ECO:0000313|Proteomes:UP000003438};
RN   [1] {ECO:0000313|EMBL:EFB77252.1, ECO:0000313|Proteomes:UP000003438}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15176 {ECO:0000313|EMBL:EFB77252.1,
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   -!- 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:EFB77252.1}.
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DR   EMBL; ACBY02000013; EFB77252.1; -; Genomic_DNA.
DR   RefSeq; WP_007045851.1; NZ_GG704769.1.
DR   AlphaFoldDB; D1PJ92; -.
DR   STRING; 411471.SUBVAR_04412; -.
DR   GeneID; 78307757; -.
DR   eggNOG; COG0111; Bacteria.
DR   HOGENOM; CLU_019796_1_0_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; 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; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   4: Predicted;
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Oxidoreductase {ECO:0000313|EMBL:EFB77252.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003438}.
FT   DOMAIN          103..279
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   331 AA;  36407 MW;  E7086AAD7CAA6DA0 CRC64;
     MEKHILVALP LTEAQRETIR QAAPRFAYRF TTQETVTREE ILWADAILGN VPVDLIRQND
     HLAWFQSNFA GPDPYLEPGV LPADCLVTNA TGAYGLAISE WMLGMWLALA KDLVLYRDRQ
     HRHEWNAIER PVRSIAGARV LCVGMGDIGA SFARRAHLLG AEVVGVRRHA GECPDYCLRV
     VDTAHLDEEL PAADLVALSL PGTPQTYRMF DAARLARCKQ GAILLNVGRG STVDCDALAA
     AVQSGALYGA AIDVTDPEPL PPDHPLWGLD TVLITPHISG RFSLPRTLEN IVGIFAHNLQ
     RFAAGQTLDN QMSRTTRYVS EDTPGRRLTC E
//
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