PDXB_BACTN
ID PDXB_BACTN Reviewed; 348 AA.
AC Q8A2E4;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Erythronate-4-phosphate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01825};
DE EC=1.1.1.290 {ECO:0000255|HAMAP-Rule:MF_01825};
GN Name=pdxB {ECO:0000255|HAMAP-Rule:MF_01825}; OrderedLocusNames=BT_3361;
OS Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 /
OS CCUG 10774 / NCTC 10582 / VPI-5482 / E50).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=226186;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC VPI-5482 / E50;
RX PubMed=12663928; DOI=10.1126/science.1080029;
RA Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C.,
RA Hooper L.V., Gordon J.I.;
RT "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis.";
RL Science 299:2074-2076(2003).
CC -!- FUNCTION: Catalyzes the oxidation of erythronate-4-phosphate to 3-
CC hydroxy-2-oxo-4-phosphonooxybutanoate. {ECO:0000255|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:0000255|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:0000255|HAMAP-Rule:MF_01825}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01825}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01825}.
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. PdxB subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_01825}.
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DR EMBL; AE015928; AAO78467.1; -; Genomic_DNA.
DR RefSeq; NP_812273.1; NC_004663.1.
DR RefSeq; WP_011108789.1; NC_004663.1.
DR AlphaFoldDB; Q8A2E4; -.
DR SMR; Q8A2E4; -.
DR STRING; 226186.BT_3361; -.
DR PaxDb; Q8A2E4; -.
DR PRIDE; Q8A2E4; -.
DR EnsemblBacteria; AAO78467; AAO78467; BT_3361.
DR GeneID; 60924540; -.
DR KEGG; bth:BT_3361; -.
DR PATRIC; fig|226186.12.peg.3429; -.
DR eggNOG; COG0111; Bacteria.
DR HOGENOM; CLU_019796_4_0_10; -.
DR InParanoid; Q8A2E4; -.
DR OMA; SAPGCNA; -.
DR UniPathway; UPA00244; UER00310.
DR Proteomes; UP000001414; Chromosome.
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:0004617; F:phosphoglycerate dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0006564; P:L-serine biosynthetic process; IBA:GO_Central.
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 HAMAP; MF_01825; PdxB; 1.
DR InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
DR InterPro; IPR029753; D-isomer_DH_CS.
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 Pfam; PF00389; 2-Hacid_dh; 1.
DR Pfam; PF02826; 2-Hacid_dh_C; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE 3: Inferred from homology;
KW Cytoplasm; NAD; Oxidoreductase; Pyridoxine biosynthesis;
KW Reference proteome.
FT CHAIN 1..348
FT /note="Erythronate-4-phosphate dehydrogenase"
FT /id="PRO_0000075972"
FT ACT_SITE 209
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01825"
FT ACT_SITE 238
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01825"
FT ACT_SITE 255
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01825"
FT BINDING 46
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01825"
FT BINDING 67
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01825"
FT BINDING 147
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01825"
FT BINDING 233
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01825"
FT BINDING 258
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01825"
FT BINDING 259
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01825"
SQ SEQUENCE 348 AA; 39077 MW; B6178E1AEA3C0E2A CRC64;
MKIIIDDKIP YIKEAAEKIA DEAIYAPGKD FTRELVQDAD ALIIRTRTHC NRELLEGSKV
KFIATATIGF DHIDTEYCKQ AGIEWANAPG CNSASVAQYI QSSLLIWKSL RNKKPDELTI
GIIGVGNVGS KVAKVAQDFG MRVLLNDLPR EEKEGNITFT SLEKIAEECD IITFHVPLYK
EGKYKTYHLA DGNFFRSLQR KPVVINTSRG EVIETNALLE AINNGIISDA VIDVWEHEPE
INRELLEKVL IGTPHIAGYS ADGKANATRM SLDSICRFFH LSATYEITPP APSSPLIEAK
DREEALLKMY NPIEDSNRLK SHPELFETLR GDYPLRREEK AYNIIGIK
