GenomeNet

Database: UniProt
Entry: B0VT23
LinkDB: B0VT23
Original site: B0VT23 
ID   PDXB_ACIBS              Reviewed;         355 AA.
AC   B0VT23;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   13-FEB-2019, entry version 78.
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=ABSDF0843;
OS   Acinetobacter baumannii (strain SDF).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Moraxellaceae; Acinetobacter;
OC   Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=509170;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SDF;
RX   PubMed=18350144; DOI=10.1371/journal.pone.0001805;
RA   Vallenet D., Nordmann P., Barbe V., Poirel L., Mangenot S.,
RA   Bataille E., Dossat C., Gas S., Kreimeyer A., Lenoble P., Oztas S.,
RA   Poulain J., Segurens B., Robert C., Abergel C., Claverie J.-M.,
RA   Raoult D., Medigue C., Weissenbach J., Cruveiller S.;
RT   "Comparative analysis of Acinetobacters: three genomes for three
RT   lifestyles.";
RL   PLoS ONE 3:E1805-E1805(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
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; CU468230; CAP00210.1; -; Genomic_DNA.
DR   ProteinModelPortal; B0VT23; -.
DR   SMR; B0VT23; -.
DR   EnsemblBacteria; CAP00210; CAP00210; ABSDF0843.
DR   KEGG; abm:ABSDF0843; -.
DR   HOGENOM; HOG000234432; -.
DR   KO; K03473; -.
DR   OMA; SAPGCNA; -.
DR   UniPathway; UPA00244; UER00310.
DR   Proteomes; UP000001741; 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   PANTHER; PTHR42938:SF3; PTHR42938:SF3; 1.
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   Complete proteome; Cytoplasm; NAD; Oxidoreductase;
KW   Pyridoxine biosynthesis; Reference proteome.
FT   CHAIN         1    355       Erythronate-4-phosphate dehydrogenase.
FT                                /FTId=PRO_1000188254.
FT   ACT_SITE    206    206       {ECO:0000255|HAMAP-Rule:MF_01825}.
FT   ACT_SITE    234    234       {ECO:0000255|HAMAP-Rule:MF_01825}.
FT   ACT_SITE    251    251       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     146    146       NAD. {ECO:0000255|HAMAP-Rule:MF_01825}.
FT   BINDING     229    229       NAD. {ECO:0000255|HAMAP-Rule:MF_01825}.
FT   BINDING     254    254       NAD; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01825}.
FT   BINDING     255    255       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01825}.
SQ   SEQUENCE   355 AA;  39312 MW;  2D70CEF3AC209CE5 CRC64;
     MKIVADENLA FTDYFFSEFG DIQHKAGRTL THTDVQDAEA LLVRSVTAVN ESLIQNTALK
     YVGSATIGTD HLDIQALEKQ GITWANAAGC NAQAVAEYVI TALLHLDASL LEQQEKFTLG
     IVGLGNVGKR LAYMAQLLGW KVIGFDPFVQ LDSIENVSFQ TLLQQANAVS IHVPLTKKGE
     HATYHLFDEK AFAALQPNTI LINSARGPVV KEAALIEDIQ CTQRKVVLDV FEHEPVISEG
     LLNMLALATP HIAGYSLEGK ARGTQMIYEA FCQKFGYDIN KRFETQLPAC EDYFSGHDLK
     AVLKQKLSQI YDIAQYDANI RACVKEGKVE QKAFDLLRKN YPLRREWAAH GGPQA
//
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