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Database: UniProt
Entry: B7GY62
LinkDB: B7GY62
Original site: B7GY62 
ID   PDXB_ACIB3              Reviewed;         355 AA.
AC   B7GY62;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   05-DEC-2018, entry version 62.
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=ABBFA_000839;
OS   Acinetobacter baumannii (strain AB307-0294).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Moraxellaceae; Acinetobacter;
OC   Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=557600;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AB307-0294;
RX   PubMed=18931120; DOI=10.1128/JB.00834-08;
RA   Adams M.D., Goglin K., Molyneaux N., Hujer K.M., Lavender H.,
RA   Jamison J.J., MacDonald I.J., Martin K.M., Russo T., Campagnari A.A.,
RA   Hujer A.M., Bonomo R.A., Gill S.R.;
RT   "Comparative genome sequence analysis of multidrug-resistant
RT   Acinetobacter baumannii.";
RL   J. Bacteriol. 190:8053-8064(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; CP001172; ACJ56961.1; -; Genomic_DNA.
DR   RefSeq; WP_000706080.1; NC_011595.1.
DR   ProteinModelPortal; B7GY62; -.
DR   SMR; B7GY62; -.
DR   EnsemblBacteria; ACJ56961; ACJ56961; ABBFA_000839.
DR   KEGG; abb:ABBFA_000839; -.
DR   HOGENOM; HOG000234432; -.
DR   KO; K03473; -.
DR   OMA; SAPGCNA; -.
DR   BioCyc; ABAU557600:ABBFA_RS04205-MONOMER; -.
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   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   Cytoplasm; NAD; Oxidoreductase; Pyridoxine biosynthesis.
FT   CHAIN         1    355       Erythronate-4-phosphate dehydrogenase.
FT                                /FTId=PRO_1000188251.
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;  39426 MW;  338126F627169A5E CRC64;
     MKIVADENLA FTDYFFSEFG DIQHKAGRTL THTDVQDAEA LLVRSVTAVN ESLIQNTALK
     YVGSATIGTD HLDIQALEKH GITWANAAGC NAQAVAEYVI TALLHLDASL LEQQEKFTLG
     IVGLGNVGKR LVYMAQLLGW KVIGFDPYVQ LDSIENVSFQ ALLQQANAVS IHVPLTKKGE
     HATYHLFDEK AFAALQPNTI LINSARGPVV KEAALIEDIQ RTQRKVVLDV FEHEPVISEE
     LLNMLALATP HIAGYSLEGK ARGTQMIYEA FCQKFGYEIN KRFETQLPAC EDYFSGHDLK
     AVLKQKLSQI YDIAQDDANI RACVKEGKVE QKAFDLLRKN YPLRREWAAH GGPQA
//
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