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Database: UniProt
Entry: B3PK14
LinkDB: B3PK14
Original site: B3PK14 
ID   PDXB_CELJU              Reviewed;         378 AA.
AC   B3PK14;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   16-JAN-2019, entry version 74.
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=CJA_2376;
OS   Cellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp.
OS   cellulosa).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Cellvibrionales;
OC   Cellvibrionaceae; Cellvibrio.
OX   NCBI_TaxID=498211;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ueda107;
RX   PubMed=18556790; DOI=10.1128/JB.01701-07;
RA   DeBoy R.T., Mongodin E.F., Fouts D.E., Tailford L.E., Khouri H.,
RA   Emerson J.B., Mohamoud Y., Watkins K., Henrissat B., Gilbert H.J.,
RA   Nelson K.E.;
RT   "Insights into plant cell wall degradation from the genome sequence of
RT   the soil bacterium Cellvibrio japonicus.";
RL   J. Bacteriol. 190:5455-5463(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; CP000934; ACE83189.1; -; Genomic_DNA.
DR   RefSeq; WP_012487974.1; NC_010995.1.
DR   ProteinModelPortal; B3PK14; -.
DR   SMR; B3PK14; -.
DR   STRING; 498211.CJA_2376; -.
DR   PRIDE; B3PK14; -.
DR   EnsemblBacteria; ACE83189; ACE83189; CJA_2376.
DR   KEGG; cja:CJA_2376; -.
DR   eggNOG; ENOG4105CJ0; Bacteria.
DR   eggNOG; COG0111; LUCA.
DR   HOGENOM; HOG000234432; -.
DR   KO; K03473; -.
DR   OMA; SAPGCNA; -.
DR   OrthoDB; 1638924at2; -.
DR   BioCyc; CJAP498211:G1GB3-2355-MONOMER; -.
DR   UniPathway; UPA00244; UER00310.
DR   Proteomes; UP000001036; 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; 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    378       Erythronate-4-phosphate dehydrogenase.
FT                                /FTId=PRO_1000188257.
FT   ACT_SITE    202    202       {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     142    142       NAD. {ECO:0000255|HAMAP-Rule:MF_01825}.
FT   BINDING     169    169       NAD; via carbonyl oxygen.
FT                                {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}.
FT   BINDING     252    252       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01825}.
SQ   SEQUENCE   378 AA;  41551 MW;  551660759A2349DD CRC64;
     MKIVADENIP LVNEFFGHLG EITRLPGRSM TAEDVRAADV LIVRSVTPVN AALLEGSRVR
     FVGTCTIGVD HLDQAWLEQQ GIAWSSAPGC NANSVVEYVY AALCHLDIHW LHGRFGIIGC
     GNVGGLLYRR LKAQGVDVRC YDPNLTLAQN PDLTSLEDVL ACDFISMHTP LVTTGSYPSF
     HLVGERELAQ LRPGAILINA GRGAVVDNQA LLDCLRVRHD VRVVLDVWEP EPDISLELLN
     EVAIGSPHIA GYSYDGKLNG TAMIYQACCK HIGVAPQADL SELVPPLDDN LLDTAGLTQP
     WPLAKHLIKQ VYDIAADDAR LREQAQLACA GNSEFGAGFD HLRKHYPRRR EFHNYQVRLS
     AQAEAARHWL TVLGFRCV
//
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