ID E4LN17_9FIRM Unreviewed; 343 AA.
AC E4LN17;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=4-phosphoerythronate dehydrogenase {ECO:0000313|EMBL:EFR39760.1};
DE EC=1.1.1.290 {ECO:0000313|EMBL:EFR39760.1};
GN Name=pdxB {ECO:0000313|EMBL:EFR39760.1};
GN ORFNames=HMPREF9162_0455 {ECO:0000313|EMBL:EFR39760.1};
OS Selenomonas sp. oral taxon 137 str. F0430.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Selenomonadaceae;
OC Selenomonas.
OX NCBI_TaxID=879310 {ECO:0000313|EMBL:EFR39760.1, ECO:0000313|Proteomes:UP000005418};
RN [1] {ECO:0000313|EMBL:EFR39760.1, ECO:0000313|Proteomes:UP000005418}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0430 {ECO:0000313|EMBL:EFR39760.1,
RC ECO:0000313|Proteomes:UP000005418};
RA Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G.,
RA Nelson K.E.;
RL Submitted (NOV-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:EFR39760.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AENV01000015; EFR39760.1; -; Genomic_DNA.
DR AlphaFoldDB; E4LN17; -.
DR eggNOG; COG1052; Bacteria.
DR Proteomes; UP000005418; 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; cd12162; 2-Hacid_dh_4; 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; PS00670; D_2_HYDROXYACID_DH_2; 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}.
FT DOMAIN 48..342
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 132..311
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 343 AA; 37177 MW; 5B314602725461F8 CRC64;
MWAPSNPIEK EYDRNNLIGG LRMKIVVLDG YTENPGDISW SPLAALGDLT VYDRTSYDES
PLIPERIGDA EIIVINKTPI SPATMDACPN LRAVAVLATG YNTVDAAYAR KKNIDVMNVP
GYGTDNVSQN AIALLLEACS QVGHHDRSVH AGEWTSSIDF CYWQRPLIEV SGKTAGIIGL
GRIGRATARV LCALNVNVIA YSRTETDEGR AVADYVPLDT LFARSDFIFL HCPLTPATEG
IVDAAAIARM KDGVIIVNNG RGQLIVEEDL AAALRSGKVA WAAVDVVSAE PIAADNPLLH
APHCIINPHI AWATKEARER IMQITADNVR TFIEGRPQNV VNL
//
