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Database: UniProt
Entry: E9SE70_RUMAL
LinkDB: E9SE70_RUMAL
Original site: E9SE70_RUMAL 
ID   E9SE70_RUMAL            Unreviewed;       379 AA.
AC   E9SE70;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   SubName: Full=4-phosphoerythronate dehydrogenase {ECO:0000313|EMBL:EGC02433.1};
DE            EC=1.1.1.290 {ECO:0000313|EMBL:EGC02433.1};
GN   Name=pdxB {ECO:0000313|EMBL:EGC02433.1};
GN   ORFNames=CUS_5226 {ECO:0000313|EMBL:EGC02433.1};
OS   Ruminococcus albus 8.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Ruminococcus.
OX   NCBI_TaxID=246199 {ECO:0000313|EMBL:EGC02433.1, ECO:0000313|Proteomes:UP000004259};
RN   [1] {ECO:0000313|EMBL:EGC02433.1, ECO:0000313|Proteomes:UP000004259}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=8 {ECO:0000313|EMBL:EGC02433.1,
RC   ECO:0000313|Proteomes:UP000004259};
RA   Nelson K.E., Sutton G., Torralba M., Durkin S., Harkins D., Montgomery R.,
RA   Ziemer C., Klaassens E., Ocuiv P., Morrison M.;
RL   Submitted (FEB-2011) 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:EGC02433.1}.
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DR   EMBL; ADKM02000094; EGC02433.1; -; Genomic_DNA.
DR   RefSeq; WP_002850925.1; NZ_JAJFOM010000001.1.
DR   AlphaFoldDB; E9SE70; -.
DR   STRING; 246199.CUS_5226; -.
DR   eggNOG; COG0111; Bacteria.
DR   OrthoDB; 9805416at2; -.
DR   Proteomes; UP000004259; 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; cd12174; PGDH_like_3; 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; PTHR42938; FORMATE DEHYDROGENASE 1; 1.
DR   PANTHER; PTHR42938:SF9; FORMATE DEHYDROGENASE 1; 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|RuleBase:RU003719,
KW   ECO:0000313|EMBL:EGC02433.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004259}.
FT   DOMAIN          27..304
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          100..273
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   379 AA;  39572 MW;  173443EA80045623 CRC64;
     MYNILTMNKI AACGTDKFDK AAYTITDECA EPTAIMVRSA KLHDYEMPAS LLAIARAGAG
     VNNIPVDKCA EQGIVVFNTP GANANAVKEL VICALLLSSR RITEAAAWAN SLKGTEDAPK
     TVEGGKAKFA GPEIFGKTLG VIGLGAIGGK VANAAVALGM NVIGFDPFLS EAAAKALDSS
     VKVVDSKDEI YKNSDYITLH VPFTPDAKNS ISKEQIAMMK DGVRIINAAR GELVDTAAVV
     EAIKAGKVAK YVTDFADDIG LGEENVITLP HLGASTPESE DNCAIMAADE LMDYIERGKI
     RNSVTFPNLE LAKTADQLVC VLHKAEVTED AVKAAVGADV VASASATKKA WGYTLLDVKG
     SANVDAVKAV AGVVGVRVI
//
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