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
//