ID A0A2U1AWK0_9BACT Unreviewed; 368 AA.
AC A0A2U1AWK0;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=4-phosphoerythronate dehydrogenase {ECO:0000313|EMBL:NMD87041.1, ECO:0000313|EMBL:PVY40617.1};
GN Name=pdxB {ECO:0000313|EMBL:NMD87041.1};
GN ORFNames=C8D82_11669 {ECO:0000313|EMBL:PVY40617.1}, HF882_10635
GN {ECO:0000313|EMBL:NMD87041.1};
OS Victivallis vadensis.
OC Bacteria; Lentisphaerota; Lentisphaeria; Victivallales; Victivallaceae;
OC Victivallis.
OX NCBI_TaxID=172901 {ECO:0000313|EMBL:PVY40617.1, ECO:0000313|Proteomes:UP000245959};
RN [1] {ECO:0000313|EMBL:PVY40617.1, ECO:0000313|Proteomes:UP000245959}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14823 {ECO:0000313|EMBL:PVY40617.1,
RC ECO:0000313|Proteomes:UP000245959};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:NMD87041.1, ECO:0000313|Proteomes:UP000576225}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COR2-253-APC-1A {ECO:0000313|EMBL:NMD87041.1,
RC ECO:0000313|Proteomes:UP000576225};
RA Hitch T.C.A., Wylensek D., Clavel T.;
RL Submitted (APR-2020) 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:PVY40617.1}.
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DR EMBL; JABAEW010000018; NMD87041.1; -; Genomic_DNA.
DR EMBL; QEKH01000016; PVY40617.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U1AWK0; -.
DR OrthoDB; 1522997at2; -.
DR Proteomes; UP000245959; Unassembled WGS sequence.
DR Proteomes; UP000576225; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0033711; F:4-phosphoerythronate dehydrogenase activity; IEA:InterPro.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0008615; P:pyridoxine biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd12158; ErythrP_dh; 1.
DR Gene3D; 3.30.1370.170; -; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR HAMAP; MF_01825; PdxB; 1.
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; IPR020921; Erythronate-4-P_DHase.
DR InterPro; IPR024531; Erythronate-4-P_DHase_dimer.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR038251; PdxB_dimer_sf.
DR PANTHER; PTHR42789; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_6G10090); 1.
DR PANTHER; PTHR42789:SF1; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_6G10090); 1.
DR Pfam; PF00389; 2-Hacid_dh; 1.
DR Pfam; PF02826; 2-Hacid_dh_C; 1.
DR Pfam; PF11890; DUF3410; 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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719};
KW Pyridoxine biosynthesis {ECO:0000256|ARBA:ARBA00023096};
KW Reference proteome {ECO:0000313|Proteomes:UP000245959}.
FT DOMAIN 34..108
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 109..252
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
FT DOMAIN 287..364
FT /note="Erythronate-4-phosphate dehydrogenase dimerisation"
FT /evidence="ECO:0000259|Pfam:PF11890"
SQ SEQUENCE 368 AA; 39362 MW; B7A3CEDF4AA64B9D CRC64;
MKIVADDKIP FLKGVLEPFF EMVYLPGGKI GPADVRDADA LITRTRTRCD RALLAGSKVG
FIATATIGFD HIDTAALREL GIDWTNAPGC NAASVAQYLA CVLADFRIPL AGKTLGVVGV
GNVGSRVVRV GEAFGMRVLQ CDPPRAEREG GSRFRPLDEL VAEADFLTFH VPLERGGGHP
TFHLADAALL AAMKPGAVLI NTSRGEVVDG SALKAALQAG SIGGAVLDVW EHEPEIDLEL
LELVRLGTPH IAGYSTDGKA NGTAMSVQAV GRHFGVIEYT GWTPYSLPVP EQPLIRLDAA
LPESEQLSAA CRASYDIRFD DAQLRADPAG FERQRGNYRI RREPPAYRIE GGAPVVRTAL
AKLGFQLA
//
