GenomeNet

Database: UniProt
Entry: Q31IH6
LinkDB: Q31IH6
Original site: Q31IH6 
ID   PDXB_HYDCU              Reviewed;         375 AA.
AC   Q31IH6;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, 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=Tcr_0451;
OS   Hydrogenovibrio crunogenus (strain XCL-2) (Thiomicrospira crunogena).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC   Piscirickettsiaceae; Hydrogenovibrio.
OX   NCBI_TaxID=317025;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=XCL-2;
RX   PubMed=17105352; DOI=10.1371/journal.pbio.0040383;
RA   Scott K.M., Sievert S.M., Abril F.N., Ball L.A., Barrett C.J.,
RA   Blake R.A., Boller A.J., Chain P.S.G., Clark J.A., Davis C.R.,
RA   Detter C., Do K.F., Dobrinski K.P., Faza B.I., Fitzpatrick K.A.,
RA   Freyermuth S.K., Harmer T.L., Hauser L.J., Huegler M., Kerfeld C.A.,
RA   Klotz M.G., Kong W.W., Land M., Lapidus A., Larimer F.W., Longo D.L.,
RA   Lucas S., Malfatti S.A., Massey S.E., Martin D.D., McCuddin Z.,
RA   Meyer F., Moore J.L., Ocampo L.H. Jr., Paul J.H., Paulsen I.T.,
RA   Reep D.K., Ren Q., Ross R.L., Sato P.Y., Thomas P., Tinkham L.E.,
RA   Zeruth G.T.;
RT   "The genome of deep-sea vent chemolithoautotroph Thiomicrospira
RT   crunogena XCL-2.";
RL   PLoS Biol. 4:1-17(2006).
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; CP000109; ABB41047.1; -; Genomic_DNA.
DR   RefSeq; WP_011369872.1; NC_007520.2.
DR   ProteinModelPortal; Q31IH6; -.
DR   SMR; Q31IH6; -.
DR   STRING; 317025.Tcr_0451; -.
DR   PRIDE; Q31IH6; -.
DR   EnsemblBacteria; ABB41047; ABB41047; Tcr_0451.
DR   KEGG; tcx:Tcr_0451; -.
DR   eggNOG; ENOG4105CJ0; Bacteria.
DR   eggNOG; COG0111; LUCA.
DR   HOGENOM; HOG000234432; -.
DR   KO; K03473; -.
DR   OMA; SAPGCNA; -.
DR   OrthoDB; 1638924at2; -.
DR   BioCyc; TCRU317025:G1G4Z-463-MONOMER; -.
DR   UniPathway; UPA00244; UER00310.
DR   Proteomes; UP000002713; 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; 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.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; NAD; Oxidoreductase;
KW   Pyridoxine biosynthesis; Reference proteome.
FT   CHAIN         1    375       Erythronate-4-phosphate dehydrogenase.
FT                                /FTId=PRO_0000297478.
FT   ACT_SITE    211    211       {ECO:0000255|HAMAP-Rule:MF_01825}.
FT   ACT_SITE    236    236       {ECO:0000255|HAMAP-Rule:MF_01825}.
FT   ACT_SITE    253    253       Proton donor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01825}.
FT   BINDING      49     49       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01825}.
FT   BINDING     150    150       NAD. {ECO:0000255|HAMAP-Rule:MF_01825}.
FT   BINDING     178    178       NAD; via carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01825}.
FT   BINDING     231    231       NAD. {ECO:0000255|HAMAP-Rule:MF_01825}.
FT   BINDING     256    256       NAD; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01825}.
SQ   SEQUENCE   375 AA;  42174 MW;  ED0347A3E75E37B6 CRC64;
     MTPSRTLVID DAVPYAKELF SHLGNVISLP GKEINTEHLQ NADALIVRSR TQVNSALLEH
     TNVSFVGSTV VGLDHVDQPY LKENAIEFYS AQGCNANSVS EYVITNLVNL AIEKKFTLSE
     KSLAIIGVGH VGKLVEKKAR ALGMTVLLND PPRARQEMSD EFIDLDNALK SDIITVHTPL
     TKTGQDATFH LLSTDKLKKI QPHQILINAA RGGIIDEQAW INTPTESNII DCWENEPNIN
     PDLYNQADIA TPHIAGHALD AKIAGSEMVY RALCQHWQIS PDDSWRRFLP PPPPPISLSL
     TGNHQEDIHN VLQQCYRPEE DDAAIRANNI VVTHKKYEYY RRHYPIHREW PQHRVIKTPD
     PTFNNLLYSL GFQLI
//
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