GenomeNet

Database: UniProt
Entry: Q8D0U3
LinkDB: Q8D0U3
Original site: Q8D0U3 
ID   PDXB_YERPE              Reviewed;         375 AA.
AC   Q8D0U3; Q0WDC8; Q8ZD29;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   13-APR-2004, sequence version 2.
DT   16-JAN-2019, entry version 116.
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=YPO2763, y1597, YP_2400;
OS   Yersinia pestis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=632;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CO-92 / Biovar Orientalis;
RX   PubMed=11586360; DOI=10.1038/35097083;
RA   Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G.,
RA   Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L.,
RA   Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M.,
RA   Chillingworth T., Cronin A., Davies R.M., Davis P., Dougan G.,
RA   Feltwell T., Hamlin N., Holroyd S., Jagels K., Karlyshev A.V.,
RA   Leather S., Moule S., Oyston P.C.F., Quail M.A., Rutherford K.M.,
RA   Simmonds M., Skelton J., Stevens K., Whitehead S., Barrell B.G.;
RT   "Genome sequence of Yersinia pestis, the causative agent of plague.";
RL   Nature 413:523-527(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KIM10+ / Biovar Mediaevalis;
RX   PubMed=12142430; DOI=10.1128/JB.184.16.4601-4611.2002;
RA   Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P.,
RA   Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C.,
RA   Fetherston J.D., Lindler L.E., Brubaker R.R., Plano G.V.,
RA   Straley S.C., McDonough K.A., Nilles M.L., Matson J.S., Blattner F.R.,
RA   Perry R.D.;
RT   "Genome sequence of Yersinia pestis KIM.";
RL   J. Bacteriol. 184:4601-4611(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=91001 / Biovar Mediaevalis;
RX   PubMed=15368893; DOI=10.1093/dnares/11.3.179;
RA   Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D.,
RA   Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z.,
RA   Jin L., Dai R., Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J.,
RA   Yang H., Wang J., Huang P., Yang R.;
RT   "Complete genome sequence of Yersinia pestis strain 91001, an isolate
RT   avirulent to humans.";
RL   DNA Res. 11:179-197(2004).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAM85166.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=AAS62605.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; AL590842; CAL21382.1; -; Genomic_DNA.
DR   EMBL; AE009952; AAM85166.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AE017042; AAS62605.1; ALT_INIT; Genomic_DNA.
DR   PIR; AC0337; AC0337.
DR   RefSeq; WP_002209725.1; NZ_UHIZ01000001.1.
DR   RefSeq; YP_002347710.1; NC_003143.1.
DR   ProteinModelPortal; Q8D0U3; -.
DR   SMR; Q8D0U3; -.
DR   IntAct; Q8D0U3; 3.
DR   STRING; 187410.y1597; -.
DR   PaxDb; Q8D0U3; -.
DR   DNASU; 1146544; -.
DR   EnsemblBacteria; AAM85166; AAM85166; y1597.
DR   EnsemblBacteria; AAS62605; AAS62605; YP_2400.
DR   GeneID; 1175594; -.
DR   KEGG; ype:YPO2763; -.
DR   KEGG; ypk:y1597; -.
DR   KEGG; ypm:YP_2400; -.
DR   PATRIC; fig|1028802.3.peg.1132; -.
DR   eggNOG; ENOG4105CJ0; Bacteria.
DR   eggNOG; COG0111; LUCA.
DR   HOGENOM; HOG000234432; -.
DR   KO; K03473; -.
DR   UniPathway; UPA00244; UER00310.
DR   Proteomes; UP000000815; Chromosome.
DR   Proteomes; UP000001019; Chromosome.
DR   Proteomes; UP000002490; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0033711; F:4-phosphoerythronate dehydrogenase activity; IBA:GO_Central.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0036001; P:'de novo' pyridoxal 5'-phosphate biosynthetic process; IBA:GO_Central.
DR   GO; GO:0008615; P:pyridoxine biosynthetic process; IBA:GO_Central.
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; 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.
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    375       Erythronate-4-phosphate dehydrogenase.
FT                                /FTId=PRO_0000075996.
FT   ACT_SITE    208    208       {ECO:0000255|HAMAP-Rule:MF_01825}.
FT   ACT_SITE    237    237       {ECO:0000255|HAMAP-Rule:MF_01825}.
FT   ACT_SITE    254    254       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     146    146       NAD. {ECO:0000255|HAMAP-Rule:MF_01825}.
FT   BINDING     175    175       NAD; via carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01825}.
FT   BINDING     232    232       NAD. {ECO:0000255|HAMAP-Rule:MF_01825}.
FT   BINDING     257    257       NAD; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01825}.
FT   BINDING     258    258       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01825}.
SQ   SEQUENCE   375 AA;  41167 MW;  C0C228B01B22F262 CRC64;
     MKILVDENMP YAEELFRRLG DVQAVPGRPI PRDALVDADA LMVRSVTKVN EALLHGTSIG
     FVGTATAGTD HVDDTWLRQQ GIGFSAAPGC NAIAVVEYVF SALMMMAERD GFQLRDKTVG
     IIGVGNVGSR LNARLQALGV RTLLCDPPRA DRGDNEAFWP LEKLVREADV LTFHTPLNKT
     GAYQSLHMAD DELLAALPDG RILINACRGA VVDNAALLRA LEKGKKLSVV LDVWEPEPDL
     SLPLLARVDI GTPHIAGYTL EGKARGTTQV FEAFSQHLGQ PQSVELASLL PVPEFSHLRL
     NGELDEGKLK RLMHLVYDVR RDDAPLRHVA GLPGEFDRLR KHYQERREWS SLCVQCDDAT
     SAGLLQQLGF TTQLL
//
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