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Database: UniProt
Entry: A5WHK7
LinkDB: A5WHK7
Original site: A5WHK7 
ID   PDXB_PSYWF              Reviewed;         374 AA.
AC   A5WHK7;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   16-JAN-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=PsycPRwf_2208;
OS   Psychrobacter sp. (strain PRwf-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Moraxellaceae; Psychrobacter.
OX   NCBI_TaxID=349106;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PRwf-1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Tiedje J.,
RA   Richardson P.;
RT   "Complete sequence of chromosome of Psychrobacter sp. PRwf-1.";
RL   Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000713; ABQ95148.1; -; Genomic_DNA.
DR   RefSeq; WP_011961420.1; NC_009524.1.
DR   ProteinModelPortal; A5WHK7; -.
DR   SMR; A5WHK7; -.
DR   STRING; 349106.PsycPRwf_2208; -.
DR   PRIDE; A5WHK7; -.
DR   EnsemblBacteria; ABQ95148; ABQ95148; PsycPRwf_2208.
DR   KEGG; prw:PsycPRwf_2208; -.
DR   eggNOG; COG0111; LUCA.
DR   HOGENOM; HOG000234432; -.
DR   KO; K03473; -.
DR   OMA; VCVMNTP; -.
DR   OrthoDB; 1638924at2; -.
DR   UniPathway; UPA00244; UER00310.
DR   Proteomes; UP000001993; 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.
FT   CHAIN         1    374       Erythronate-4-phosphate dehydrogenase.
FT                                /FTId=PRO_1000088424.
FT   ACT_SITE    222    222       {ECO:0000255|HAMAP-Rule:MF_01825}.
FT   ACT_SITE    251    251       {ECO:0000255|HAMAP-Rule:MF_01825}.
FT   ACT_SITE    268    268       Proton donor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01825}.
FT   BINDING      53     53       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01825}.
FT   BINDING      75     75       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01825}.
FT   BINDING     160    160       NAD. {ECO:0000255|HAMAP-Rule:MF_01825}.
FT   BINDING     246    246       NAD. {ECO:0000255|HAMAP-Rule:MF_01825}.
FT   BINDING     271    271       NAD; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01825}.
FT   BINDING     272    272       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01825}.
SQ   SEQUENCE   374 AA;  41340 MW;  F184A5D204BAB74E CRC64;
     MLTIIADSNI AHLHDYFNEQ TLNHPIQVIS MAGRDITADA LQQYQPDVLL IRSVTQIDAK
     LLDTNQSVKF IGSATIGTDH VNEGYVSLRG MRFVNAAGCS KHSVAQYVMS AILQLRPEYW
     ASNTSQSDKP VKLGIIGLGN IGSTLARYAL DLGWEVLGYD PFQSASVINN ASVEKVLAQS
     DVISLHVPLT LTGHSELPTY HMIDADALAK MPSTTMLINT SRGAVVSEAD LLADLNQNPE
     RQVVLDVFEN EPTVSAELLD KLTLATPHIA GYTLEGKLRG TQMIFDAFVR SYGEKGADIL
     SIKETDLMAD LLPDNPYQWQ QLKANPQKLA EFYDIKADDR QLRDSVNEQA GAVLGTDFDA
     LRKNYTLRRE WLFD
//
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