PDXB_PSYWF
ID PDXB_PSYWF Reviewed; 374 AA.
AC A5WHK7;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 90.
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=PsycPRwf_2208;
OS Psychrobacter sp. (strain PRwf-1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Psychrobacter.
OX NCBI_TaxID=349106;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PRwf-1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome of Psychrobacter sp. PRwf-1.";
RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000713; ABQ95148.1; -; Genomic_DNA.
DR RefSeq; WP_011961420.1; NC_009524.1.
DR AlphaFoldDB; A5WHK7; -.
DR SMR; A5WHK7; -.
DR STRING; 349106.PsycPRwf_2208; -.
DR PRIDE; A5WHK7; -.
DR EnsemblBacteria; ABQ95148; ABQ95148; PsycPRwf_2208.
DR KEGG; prw:PsycPRwf_2208; -.
DR eggNOG; COG0111; Bacteria.
DR HOGENOM; CLU_019796_4_0_6; -.
DR OMA; SAPGCNA; -.
DR OrthoDB; 1638924at2; -.
DR UniPathway; UPA00244; UER00310.
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.
FT CHAIN 1..374
FT /note="Erythronate-4-phosphate dehydrogenase"
FT /id="PRO_1000088424"
FT ACT_SITE 222
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01825"
FT ACT_SITE 251
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01825"
FT ACT_SITE 268
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01825"
FT BINDING 53
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01825"
FT BINDING 75
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01825"
FT BINDING 160
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01825"
FT BINDING 246
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01825"
FT BINDING 271
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01825"
FT BINDING 272
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01825"
SQ SEQUENCE 374 AA; 41340 MW; F184A5D204BAB74E CRC64;
MLTIIADSNI AHLHDYFNEQ TLNHPIQVIS MAGRDITADA LQQYQPDVLL IRSVTQIDAK
LLDTNQSVKF IGSATIGTDH VNEGYVSLRG MRFVNAAGCS KHSVAQYVMS AILQLRPEYW
ASNTSQSDKP VKLGIIGLGN IGSTLARYAL DLGWEVLGYD PFQSASVINN ASVEKVLAQS
DVISLHVPLT LTGHSELPTY HMIDADALAK MPSTTMLINT SRGAVVSEAD LLADLNQNPE
RQVVLDVFEN EPTVSAELLD KLTLATPHIA GYTLEGKLRG TQMIFDAFVR SYGEKGADIL
SIKETDLMAD LLPDNPYQWQ QLKANPQKLA EFYDIKADDR QLRDSVNEQA GAVLGTDFDA
LRKNYTLRRE WLFD
