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Database: UniProt
Entry: Q2S0U3
LinkDB: Q2S0U3
Original site: Q2S0U3 
ID   PDXB_SALRD              Reviewed;         392 AA.
AC   Q2S0U3;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   16-JAN-2019, entry version 91.
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=SRU_2082;
OS   Salinibacter ruber (strain DSM 13855 / M31).
OC   Bacteria; Bacteroidetes; Bacteroidetes Order II. Incertae sedis;
OC   Rhodothermaceae; Salinibacter.
OX   NCBI_TaxID=309807;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13855 / M31;
RX   PubMed=16330755; DOI=10.1073/pnas.0509073102;
RA   Mongodin E.F., Nelson K.E., Daugherty S., DeBoy R.T., Wister J.,
RA   Khouri H., Weidman J., Walsh D.A., Papke R.T., Sanchez Perez G.,
RA   Sharma A.K., Nesbo C.L., MacLeod D., Bapteste E., Doolittle W.F.,
RA   Charlebois R.L., Legault B., Rodriguez-Valera F.;
RT   "The genome of Salinibacter ruber: convergence and gene exchange among
RT   hyperhalophilic bacteria and archaea.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:18147-18152(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; CP000159; ABC44154.1; -; Genomic_DNA.
DR   RefSeq; WP_011404810.1; NC_007677.1.
DR   RefSeq; YP_446188.1; NC_007677.1.
DR   ProteinModelPortal; Q2S0U3; -.
DR   SMR; Q2S0U3; -.
DR   STRING; 309807.SRU_2082; -.
DR   EnsemblBacteria; ABC44154; ABC44154; SRU_2082.
DR   GeneID; 3851421; -.
DR   KEGG; sru:SRU_2082; -.
DR   PATRIC; fig|309807.25.peg.2167; -.
DR   eggNOG; ENOG4105CJ0; Bacteria.
DR   eggNOG; COG0111; LUCA.
DR   HOGENOM; HOG000234432; -.
DR   KO; K03473; -.
DR   OMA; SAPGCNA; -.
DR   BioCyc; SRUB309807:G1G5H-2079-MONOMER; -.
DR   UniPathway; UPA00244; UER00310.
DR   Proteomes; UP000008674; 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   Gene3D; 3.30.1370.170; -; 1.
DR   HAMAP; MF_01825; PdxB; 1.
DR   InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
DR   InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR   InterPro; IPR020921; Erythronate-4-P_DHase.
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   SUPFAM; SSF51735; SSF51735; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; NAD; Oxidoreductase;
KW   Pyridoxine biosynthesis; Reference proteome.
FT   CHAIN         1    392       Erythronate-4-phosphate dehydrogenase.
FT                                /FTId=PRO_0000297462.
FT   ACT_SITE    215    215       {ECO:0000255|HAMAP-Rule:MF_01825}.
FT   ACT_SITE    244    244       {ECO:0000255|HAMAP-Rule:MF_01825}.
FT   ACT_SITE    261    261       Proton donor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01825}.
FT   BINDING      48     48       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01825}.
FT   BINDING      69     69       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01825}.
FT   BINDING     149    149       NAD. {ECO:0000255|HAMAP-Rule:MF_01825}.
FT   BINDING     239    239       NAD. {ECO:0000255|HAMAP-Rule:MF_01825}.
FT   BINDING     264    264       NAD; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01825}.
FT   BINDING     265    265       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01825}.
SQ   SEQUENCE   392 AA;  41521 MW;  9A6136289A834715 CRC64;
     MTSLQILADA NIPRVEDAFG QFGTVRRMPG REMTTSDVAA ADVLLVRSVT PVGPALLDGT
     PLRFVGSATI GTDHVDRDYL RAQGIPFAHA PGSNADSVAD YVVAALLGLA RRRGGALEER
     TVGIVGCGNI GGRLARRLSA LGMEVLRNDP PRARAADADG TGHGFVPLDT VLGAADVVTL
     HVPLKASGPD PTHHLVDAAF LDRLGDGAWL LNTSRGAVVD GDALLAARRR GDVAAAVLDV
     WENEPSPDPA LIEAVDLATP HIAGYAYDGK VRGTEMLYEA LCDALGGEAR WAGTDAIRPA
     SADALRGRAP DPRLSATEWR FELARQAYDP AVDDASLRDL VKLGPDARGE AFAHLRAGYR
     RRREMQQHTV PGTAVPAEHE QAVTEGLKMK LD
//
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