PDXB_BAUCH
ID PDXB_BAUCH Reviewed; 376 AA.
AC Q1LTA7;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 89.
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=BCI_0363;
OS Baumannia cicadellinicola subsp. Homalodisca coagulata.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Candidatus Baumannia.
OX NCBI_TaxID=374463;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16729848; DOI=10.1371/journal.pbio.0040188;
RA Wu D., Daugherty S.C., Van Aken S.E., Pai G.H., Watkins K.L., Khouri H.,
RA Tallon L.J., Zaborsky J.M., Dunbar H.E., Tran P.L., Moran N.A., Eisen J.A.;
RT "Metabolic complementarity and genomics of the dual bacterial symbiosis of
RT sharpshooters.";
RL PLoS Biol. 4:1079-1092(2006).
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; CP000238; ABF14137.1; -; Genomic_DNA.
DR RefSeq; WP_011520540.1; NC_007984.1.
DR AlphaFoldDB; Q1LTA7; -.
DR SMR; Q1LTA7; -.
DR STRING; 374463.BCI_0363; -.
DR EnsemblBacteria; ABF14137; ABF14137; BCI_0363.
DR KEGG; bci:BCI_0363; -.
DR HOGENOM; CLU_019796_4_0_6; -.
DR OMA; SAPGCNA; -.
DR OrthoDB; 1638924at2; -.
DR UniPathway; UPA00244; UER00310.
DR Proteomes; UP000002427; 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:0046983; F:protein dimerization activity; 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 HAMAP; MF_01825; PdxB; 1.
DR InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
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 Pfam; PF00389; 2-Hacid_dh; 1.
DR Pfam; PF02826; 2-Hacid_dh_C; 1.
DR Pfam; PF11890; DUF3410; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 1.
PE 3: Inferred from homology;
KW Cytoplasm; NAD; Oxidoreductase; Pyridoxine biosynthesis;
KW Reference proteome.
FT CHAIN 1..376
FT /note="Erythronate-4-phosphate dehydrogenase"
FT /id="PRO_0000297435"
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 45
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01825"
FT BINDING 66
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01825"
FT BINDING 146
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 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 376 AA; 42151 MW; C2E486EEDF8C1963 CRC64;
MKILVDENIP YAHKIFSRLG DVQIIHGRKI TAQIVSSYDA LIVRSVTNVN QSLLEGSKVR
FVGSTTSGID HIDDHWLEKS GIKFSYAAGC NAIAVVEYVF TALLLLSQRY GFHLRDKTVG
IIGVGNIGRL LYQRLNAFGV PTLLCDPPQA EISTIGEWQL LEKLVTEADV LTLHTPLTYH
GRHATWHLIN EDLLSALPST KRILINTCRG AVVDNVALLH ALKKGKLLSV ILDVWEKEPN
LSLSLLNNVD IGTAHIAGYS LEGKVRGAIK IFNDYSKFLG AIQSLNVSAF LPAPMIEYVR
WHGVINEEEL RKLAYLIYDL QFDDILLRRN IHKPHGFDQL RTNYCERREW SSLSVGTDNN
ISTNMLNQLG FKSILI
