ID PDXB_COXBU Reviewed; 366 AA. AC Q83AR8; DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot. DT 13-APR-2004, sequence version 2. DT 27-MAR-2024, entry version 114. 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}; GN OrderedLocusNames=CBU_1812; OS Coxiella burnetii (strain RSA 493 / Nine Mile phase I). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales; Coxiellaceae; OC Coxiella. OX NCBI_TaxID=227377; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RSA 493 / Nine Mile phase I; RX PubMed=12704232; DOI=10.1073/pnas.0931379100; RA Seshadri R., Paulsen I.T., Eisen J.A., Read T.D., Nelson K.E., Nelson W.C., RA Ward N.L., Tettelin H., Davidsen T.M., Beanan M.J., DeBoy R.T., RA Daugherty S.C., Brinkac L.M., Madupu R., Dodson R.J., Khouri H.M., RA Lee K.H., Carty H.A., Scanlan D., Heinzen R.A., Thompson H.A., Samuel J.E., RA Fraser C.M., Heidelberg J.F.; RT "Complete genome sequence of the Q-fever pathogen, Coxiella burnetii."; RL Proc. Natl. Acad. Sci. U.S.A. 100:5455-5460(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}. CC -!- SEQUENCE CAUTION: CC Sequence=AAO91305.1; Type=Erroneous initiation; Evidence={ECO:0000305}; 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; AE016828; AAO91305.1; ALT_INIT; Genomic_DNA. DR RefSeq; NP_820791.1; NC_002971.3. DR RefSeq; WP_010958459.1; NC_002971.4. DR AlphaFoldDB; Q83AR8; -. DR SMR; Q83AR8; -. DR STRING; 227377.CBU_1812; -. DR EnsemblBacteria; AAO91305; AAO91305; CBU_1812. DR GeneID; 1209723; -. DR KEGG; cbu:CBU_1812; -. DR PATRIC; fig|227377.7.peg.1798; -. DR eggNOG; COG0111; Bacteria. DR HOGENOM; CLU_019796_4_0_6; -. DR OrthoDB; 9770208at2; -. DR UniPathway; UPA00244; UER00310. DR Proteomes; UP000002671; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0033711; F:4-phosphoerythronate dehydrogenase activity; IBA:GO_Central. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro. DR GO; GO:0036001; P:'de novo' pyridoxal 5'-phosphate biosynthetic process; IBA:GO_Central. DR GO; GO:0008615; P:pyridoxine biosynthetic process; IBA:GO_Central. 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; 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; PTHR10996; 2-HYDROXYACID DEHYDROGENASE-RELATED; 1. DR PANTHER; PTHR10996:SF286; D-3-PHOSPHOGLYCERATE DEHYDROGENASE 1-RELATED; 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; PS00671; D_2_HYDROXYACID_DH_3; 1. PE 3: Inferred from homology; KW Cytoplasm; NAD; Oxidoreductase; Pyridoxine biosynthesis; KW Reference proteome. FT CHAIN 1..366 FT /note="Erythronate-4-phosphate dehydrogenase" FT /id="PRO_0000075974" FT ACT_SITE 208 FT /evidence="ECO:0000255|HAMAP-Rule:MF_01825" FT ACT_SITE 233 FT /evidence="ECO:0000255|HAMAP-Rule:MF_01825" FT ACT_SITE 250 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 175 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01825" FT BINDING 228 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01825" FT BINDING 253 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01825" FT BINDING 254 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01825" SQ SEQUENCE 366 AA; 40969 MW; FC5F34670DCF8C1F CRC64; MIKILADDRI PFVSELFGDF GELILKPGAH IQNRDLLAVN ALLTRSITSV DSALLEGTAV EFVGSATAGF DHIDSTWLKK QSIHWAYAPG ANATAVAEYV LHCVAYLHKK NLLPRKSATA AIIGVGHVGC VVSDRLRKIG FTVFHNDPPR AQLEKDFISV PLASLANVDL VCLHTPLVKT GNFPTYHLID NRFLKMLKPG SVLLNAGRGA VIDNNALLQC DHVITCLDVW ENEPTVNLQL LEKTTIATPH IAGYSKQAKL RATLMIYDAF LKYFHLSDTR RFSELQQLQE TMTLNIQDGR NAEDILLTLF DPGRESQRMR ETLAENPDQF EYLRRHFPLR NEFSAIQLTP TPSALLRKEL DDWGFK //