ID J6GQE3_9PORP Unreviewed; 376 AA.
AC J6GQE3;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=Erythronate-4-phosphate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01825};
DE EC=1.1.1.290 {ECO:0000256|HAMAP-Rule:MF_01825};
GN Name=pdxB {ECO:0000256|HAMAP-Rule:MF_01825,
GN ECO:0000313|EMBL:EJU16100.1};
GN ORFNames=HMPREF1323_0078 {ECO:0000313|EMBL:EJU16100.1};
OS Porphyromonas sp. oral taxon 279 str. F0450.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=1125723 {ECO:0000313|EMBL:EJU16100.1, ECO:0000313|Proteomes:UP000004156};
RN [1] {ECO:0000313|EMBL:EJU16100.1, ECO:0000313|Proteomes:UP000004156}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0450 {ECO:0000313|EMBL:EJU16100.1,
RC ECO:0000313|Proteomes:UP000004156};
RA Durkin A.S., McCorrison J., Torralba M., Gillis M., Methe B., Sutton G.,
RA Nelson K.E.;
RL Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the oxidation of erythronate-4-phosphate to 3-
CC hydroxy-2-oxo-4-phosphonooxybutanoate. {ECO:0000256|HAMAP-
CC Rule:MF_01825}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-phospho-D-erythronate + NAD(+) = (R)-3-hydroxy-2-oxo-4-
CC phosphooxybutanoate + H(+) + NADH; Xref=Rhea:RHEA:18829,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:58538, ChEBI:CHEBI:58766; EC=1.1.1.290;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01825};
CC -!- PATHWAY: Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis;
CC pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 2/5.
CC {ECO:0000256|HAMAP-Rule:MF_01825}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01825}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01825}.
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. PdxB subfamily. {ECO:0000256|HAMAP-
CC Rule:MF_01825}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01825}.
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:EJU16100.1}.
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DR EMBL; ALKJ01000032; EJU16100.1; -; Genomic_DNA.
DR RefSeq; WP_009433496.1; NZ_ALKJ01000032.1.
DR AlphaFoldDB; J6GQE3; -.
DR PATRIC; fig|1125723.3.peg.1412; -.
DR UniPathway; UPA00244; UER00310.
DR Proteomes; UP000004156; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0033711; F:4-phosphoerythronate dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0008615; P:pyridoxine biosynthetic process; IEA:UniProtKB-UniRule.
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; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR020921; Erythronate-4-P_DHase.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR038251; PdxB_dimer_sf.
DR PANTHER; PTHR10996; 2-HYDROXYACID DEHYDROGENASE-RELATED; 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.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01825};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_01825};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_01825};
KW Pyridoxine biosynthesis {ECO:0000256|ARBA:ARBA00023096, ECO:0000256|HAMAP-
KW Rule:MF_01825}; Reference proteome {ECO:0000313|Proteomes:UP000004156}.
FT DOMAIN 25..282
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 111..259
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
FT ACT_SITE 211
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01825"
FT ACT_SITE 240
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01825"
FT ACT_SITE 257
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01825"
FT BINDING 48
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01825"
FT BINDING 69
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01825"
FT BINDING 149
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01825"
FT BINDING 235
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01825"
FT BINDING 260
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01825"
SQ SEQUENCE 376 AA; 41061 MW; 865E7D4E8D01403A CRC64;
MDKPLFVLDS SLPYLEGLVE QVADVRRLPN RDFTPETIRG ARALLIRSVV HAGRELLEGS
GVEIVATATA GFDHIDADYC AAAGIHWESA PGCNAGGVVQ YVLSSLVRWS LERGVSLEGK
TIGIVGVGNV GGRLAKRVGA LGLRPLLCDP PRAEREGTEG FVSLETIQRE SDIITLHVPL
TRAGQYATEG MVDEAFLQGC ARRPLLINAC RGPVSPSAAL LKGLELRQIS DLIIDCWEGE
PVINKTLLER SFIATPHIAG WTADGKWRGS QMALEAVCRA LDLPLPEGLW DEGVLYTPDA
PCIDLSTFPE EERILRTQLH TCDLKATTQT LKSAPEDFEQ VRRAYRFPRE ASAYTVVGAY
PEEKPLLEQL GFTHIE
//
