PDXB_ECOSM
ID PDXB_ECOSM Reviewed; 378 AA.
AC B1LLS6;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 82.
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=EcSMS35_2476;
OS Escherichia coli (strain SMS-3-5 / SECEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=439855;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SMS-3-5 / SECEC;
RX PubMed=18708504; DOI=10.1128/jb.00661-08;
RA Fricke W.F., Wright M.S., Lindell A.H., Harkins D.M., Baker-Austin C.,
RA Ravel J., Stepanauskas R.;
RT "Insights into the environmental resistance gene pool from the genome
RT sequence of the multidrug-resistant environmental isolate Escherichia coli
RT SMS-3-5.";
RL J. Bacteriol. 190:6779-6794(2008).
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; CP000970; ACB17370.1; -; Genomic_DNA.
DR RefSeq; WP_000699135.1; NC_010498.1.
DR AlphaFoldDB; B1LLS6; -.
DR SMR; B1LLS6; -.
DR EnsemblBacteria; ACB17370; ACB17370; EcSMS35_2476.
DR KEGG; ecm:EcSMS35_2476; -.
DR HOGENOM; CLU_019796_4_0_6; -.
DR OMA; SAPGCNA; -.
DR UniPathway; UPA00244; UER00310.
DR Proteomes; UP000007011; 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; 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 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.
DR PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE 3: Inferred from homology;
KW Cytoplasm; NAD; Oxidoreductase; Pyridoxine biosynthesis.
FT CHAIN 1..378
FT /note="Erythronate-4-phosphate dehydrogenase"
FT /id="PRO_1000188268"
FT ACT_SITE 208
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01825"
FT ACT_SITE 237
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01825"
FT ACT_SITE 254
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 232
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01825"
FT BINDING 257
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01825"
FT BINDING 258
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01825"
SQ SEQUENCE 378 AA; 41347 MW; 275E565614881154 CRC64;
MKILVDENMP YARDLFSRLG EVTAVPGRPI PVAQLADADA LMVRSVTKVN ESLLAGKPIK
FVGTATAGTD HVDEAWLKQA GIGFSAAPGC NAIAVVEYVF SSLLMLAERD GFSLHERTVG
IVGVGNVGRR LQARLEALGI KTLLCDPPRA DRGDEGDFRS LDELVQHADI LTFHTPLFKD
GPYKTLHLAD EKLIRSLKPG AILINACRGA VVDNTALLTC LNEGQKLSVV LDVWEGEPEL
NVELLKKVDI GTPHIAGYTL EGKARGTTQV FEAYSKFIGH EQHVALDTLL PAPEFGRITL
HGPLDQPTLK RLVHLVYDVR RDDAPLRKVA GIPGEFDKLR KNYLERREWS SLYVICDDAS
AASLLCKLGF NAVHHPAR
