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Database: UniProt
Entry: Q5WXZ0
LinkDB: Q5WXZ0
Original site: Q5WXZ0 
ID   PDXB_LEGPL              Reviewed;         350 AA.
AC   Q5WXZ0;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   05-DEC-2018, entry version 94.
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=lpl0949;
OS   Legionella pneumophila (strain Lens).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=297245;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Lens;
RX   PubMed=15467720; DOI=10.1038/ng1447;
RA   Cazalet C., Rusniok C., Brueggemann H., Zidane N., Magnier A., Ma L.,
RA   Tichit M., Jarraud S., Bouchier C., Vandenesch F., Kunst F.,
RA   Etienne J., Glaser P., Buchrieser C.;
RT   "Evidence in the Legionella pneumophila genome for exploitation of
RT   host cell functions and high genome plasticity.";
RL   Nat. Genet. 36:1165-1173(2004).
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
CC       biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-
CC       phosphate: step 2/5. {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}.
DR   EMBL; CR628337; CAH15183.1; -; Genomic_DNA.
DR   RefSeq; WP_011215087.1; NC_006369.1.
DR   ProteinModelPortal; Q5WXZ0; -.
DR   SMR; Q5WXZ0; -.
DR   EnsemblBacteria; CAH15183; CAH15183; lpl0949.
DR   KEGG; lpf:lpl0949; -.
DR   LegioList; lpl0949; -.
DR   HOGENOM; HOG000278825; -.
DR   KO; K03473; -.
DR   OMA; SAPGCNA; -.
DR   UniPathway; UPA00244; UER00310.
DR   Proteomes; UP000002517; 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:0008615; P:pyridoxine biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd12158; ErythrP_dh; 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; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR42938:SF3; PTHR42938:SF3; 1.
DR   Pfam; PF00389; 2-Hacid_dh; 1.
DR   Pfam; PF02826; 2-Hacid_dh_C; 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   Complete proteome; Cytoplasm; NAD; Oxidoreductase;
KW   Pyridoxine biosynthesis.
FT   CHAIN         1    350       Erythronate-4-phosphate dehydrogenase.
FT                                /FTId=PRO_0000297444.
FT   NP_BIND     124    125       NAD. {ECO:0000255|HAMAP-Rule:MF_01825}.
FT   NP_BIND     203    205       NAD. {ECO:0000255|HAMAP-Rule:MF_01825}.
FT   ACT_SITE    205    205       {ECO:0000255|HAMAP-Rule:MF_01825}.
FT   ACT_SITE    231    231       {ECO:0000255|HAMAP-Rule:MF_01825}.
FT   ACT_SITE    248    248       Proton donor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01825}.
FT   BINDING      45     45       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01825}.
FT   BINDING      66     66       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01825}.
FT   BINDING     144    144       NAD. {ECO:0000255|HAMAP-Rule:MF_01825}.
FT   BINDING     226    226       NAD. {ECO:0000255|HAMAP-Rule:MF_01825}.
FT   BINDING     251    251       NAD; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01825}.
SQ   SEQUENCE   350 AA;  38943 MW;  B68F096E84FF59EE CRC64;
     MNILADALLP GLDSAFPPPF TVTLYHKADE IPELLHHKDV LLCRSTLKIN GDLLKHHQIK
     VVATATSGTD HIDFPFLESQ NISIIDAKGC NATSVADYVV ACLAYLDKQQ LIQGKTAGII
     GLGQVGTKVY ERLNAAEFQL CLYDPPKATR DTSFQSCSLE DLLECDFLCV HAELHSNAPY
     PSLNLINRDF LKELKPGCII INASRGGIIN EEALLHLGSA ILYCTDVYNN EPHIDNRIVS
     RATLCTPHIA GHSLEAKFAA VAIVSRKLHQ MLGLPYPQFA TPEKPYRLND DSNWRELALS
     IYNPIHETLE LKHAGNLSSA FLTLRKNHHH RHDFTTYFDS DSIKKYPLLG
//
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