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Database: UniProt
Entry: Q6LNU2
LinkDB: Q6LNU2
Original site: Q6LNU2 
ID   PDXB_PHOPR              Reviewed;         391 AA.
AC   Q6LNU2;
DT   21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   16-JAN-2019, entry version 93.
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=PBPRA2656;
OS   Photobacterium profundum (strain SS9).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
OC   Vibrionaceae; Photobacterium.
OX   NCBI_TaxID=298386;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1253 / SS9;
RX   PubMed=15746425; DOI=10.1126/science.1103341;
RA   Vezzi A., Campanaro S., D'Angelo M., Simonato F., Vitulo N.,
RA   Lauro F.M., Cestaro A., Malacrida G., Simionati B., Cannata N.,
RA   Romualdi C., Bartlett D.H., Valle G.;
RT   "Life at depth: Photobacterium profundum genome sequence and
RT   expression analysis.";
RL   Science 307:1459-1461(2005).
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; CR378671; CAG21034.1; -; Genomic_DNA.
DR   RefSeq; WP_011219313.1; NC_006370.1.
DR   ProteinModelPortal; Q6LNU2; -.
DR   SMR; Q6LNU2; -.
DR   STRING; 298386.PBPRA2656; -.
DR   EnsemblBacteria; CAG21034; CAG21034; PBPRA2656.
DR   KEGG; ppr:PBPRA2656; -.
DR   eggNOG; ENOG4105CJ0; Bacteria.
DR   eggNOG; COG0111; LUCA.
DR   HOGENOM; HOG000234432; -.
DR   KO; K03473; -.
DR   OMA; SAPGCNA; -.
DR   OrthoDB; 1638924at2; -.
DR   UniPathway; UPA00244; UER00310.
DR   Proteomes; UP000000593; Chromosome 1.
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; 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; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; NAD; Oxidoreductase;
KW   Pyridoxine biosynthesis; Reference proteome.
FT   CHAIN         1    391       Erythronate-4-phosphate dehydrogenase.
FT                                /FTId=PRO_0000075980.
FT   ACT_SITE    209    209       {ECO:0000255|HAMAP-Rule:MF_01825}.
FT   ACT_SITE    243    243       {ECO:0000255|HAMAP-Rule:MF_01825}.
FT   ACT_SITE    260    260       Proton donor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01825}.
FT   BINDING      45     45       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01825}.
FT   BINDING      67     67       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01825}.
FT   BINDING     147    147       NAD. {ECO:0000255|HAMAP-Rule:MF_01825}.
FT   BINDING     176    176       NAD; via carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01825}.
FT   BINDING     238    238       NAD. {ECO:0000255|HAMAP-Rule:MF_01825}.
FT   BINDING     263    263       NAD; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01825}.
FT   BINDING     264    264       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01825}.
SQ   SEQUENCE   391 AA;  42695 MW;  5078085C65B1C36F CRC64;
     MKILIDENMP YAAELFGQLG EVVTKPGRTL SADDLIDIDA LMIRSVTKVN HNLISKANKL
     QFVGTATAGQ DHVDQALLAE RGITFTSAPG CNKVGVAEYV LSALMVIGQQ QGFSIFDKTI
     GIIGAGNVGS YLAQCLDALG IPYLLNDPIK EQEGDTRQFH SLEAIKAQCD VITVHTPITK
     DGEYPTHHLI NEAFIDALQP DAILINAARG PVTDNQALKK ALQLSQSGLG KKLTAVLDVF
     EFEPHVDLEL LPLLAFATPH IAGYGLEGKA RGTTMVFNRY CAFLNIDQAV EASSLLPIAP
     VPNVSLSRKW DDATLFSLIQ LIYDIRKDDA LFRRNMVVTK GNEAQMATAF DQMRKNYWDR
     REYSAITVTG KVGFGVESLA KLGFTVVEDI Q
//
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