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Database: UniProt
Entry: P05459
LinkDB: P05459
Original site: P05459 
ID   PDXB_ECOLI              Reviewed;         378 AA.
AC   P05459;
DT   01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 2.
DT   13-FEB-2019, entry version 162.
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=b2320, JW2317;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=2681152; DOI=10.1128/jb.171.11.6084-6092.1989;
RA   Schoenlein P.V., Roa B.B., Winkler M.E.;
RT   "Divergent transcription of pdxB and homology between the pdxB and
RT   serA gene products in Escherichia coli K-12.";
RL   J. Bacteriol. 171:6084-6092(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA   Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K.,
RA   Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N.,
RA   Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H.,
RA   Oshima T., Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S.,
RA   Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C.,
RA   Yamagata S., Horiuchi T.;
RT   "Construction of a contiguous 874-kb sequence of the Escherichia coli-
RT   K12 genome corresponding to 50.0-68.8 min on the linkage map and
RT   analysis of its sequence features.";
RL   DNA Res. 4:91-113(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
RA   Mau B., Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains
RT   MG1655 and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 273-378.
RC   STRAIN=K12;
RX   PubMed=2991861; DOI=10.1093/nar/13.14.5297;
RA   Arps P.J., Marvel C.C., Rubin B.C., Tolan D.A., Penhoet E.E.,
RA   Winkler M.E.;
RT   "Structural features of the hisT operon of Escherichia coli K-12.";
RL   Nucleic Acids Res. 13:5297-5315(1985).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 273-378.
RC   STRAIN=K12;
RX   PubMed=3029016; DOI=10.1128/jb.169.3.1061-1070.1987;
RA   Arps P.J., Winkler M.E.;
RT   "Structural analysis of the Escherichia coli K-12 hisT operon by using
RT   a kanamycin resistance cassette.";
RL   J. Bacteriol. 169:1061-1070(1987).
RN   [7]
RP   PATHWAY.
RX   PubMed=8595869; DOI=10.1111/j.1574-6968.1996.tb08001.x;
RA   Zhao G., Winkler M.E.;
RT   "4-phospho-hydroxy-L-threonine is an obligatory intermediate in
RT   pyridoxal 5'-phosphate coenzyme biosynthesis in Escherichia coli K-
RT   12.";
RL   FEMS Microbiol. Lett. 135:275-280(1996).
RN   [8]
RP   PYRIDOXAL PHOSPHATE PATHWAY.
RX   PubMed=9696782;
RA   Yang Y., Zhao G., Man T.-K., Winkler M.E.;
RT   "Involvement of the gapA- and epd (gapB)-encoded dehydrogenases in
RT   pyridoxal 5'-phosphate coenzyme biosynthesis in Escherichia coli K-
RT   12.";
RL   J. Bacteriol. 180:4294-4299(1998).
RN   [9]
RP   INDUCTION.
RX   PubMed=11844765; DOI=10.1128/JB.184.5.1359-1369.2002;
RA   Pease A.J., Roa B.R., Luo W., Winkler M.E.;
RT   "Positive growth rate-dependent regulation of the pdxA, ksgA, and pdxB
RT   genes of Escherichia coli K-12.";
RL   J. Bacteriol. 184:1359-1369(2002).
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       ECO:0000269|PubMed:8595869}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01825}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01825}.
CC   -!- INDUCTION: During growth rate. {ECO:0000269|PubMed:11844765}.
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. PdxB subfamily. {ECO:0000255|HAMAP-
CC       Rule:MF_01825}.
DR   EMBL; M29962; AAA24308.1; -; Genomic_DNA.
DR   EMBL; U76961; AAB36530.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC75380.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA16177.1; -; Genomic_DNA.
DR   EMBL; X02743; CAA26520.1; -; Genomic_DNA.
DR   EMBL; M15541; AAA24310.1; -; Genomic_DNA.
DR   PIR; JV0051; DEECPP.
DR   RefSeq; NP_416823.1; NC_000913.3.
DR   RefSeq; WP_000699148.1; NZ_LN832404.1.
DR   ProteinModelPortal; P05459; -.
DR   SMR; P05459; -.
DR   BioGrid; 4259616; 24.
DR   DIP; DIP-10449N; -.
DR   IntAct; P05459; 9.
DR   STRING; 316385.ECDH10B_2482; -.
DR   EPD; P05459; -.
DR   jPOST; P05459; -.
DR   PaxDb; P05459; -.
DR   PRIDE; P05459; -.
DR   EnsemblBacteria; AAC75380; AAC75380; b2320.
DR   EnsemblBacteria; BAA16177; BAA16177; BAA16177.
DR   GeneID; 946785; -.
DR   KEGG; ecj:JW2317; -.
DR   KEGG; eco:b2320; -.
DR   PATRIC; fig|1411691.4.peg.4413; -.
DR   EchoBASE; EB0686; -.
DR   EcoGene; EG10692; pdxB.
DR   eggNOG; ENOG4105CJ0; Bacteria.
DR   eggNOG; COG0111; LUCA.
DR   HOGENOM; HOG000234432; -.
DR   InParanoid; P05459; -.
DR   KO; K03473; -.
DR   PhylomeDB; P05459; -.
DR   BioCyc; EcoCyc:ERYTHRON4PDEHYDROG-MONOMER; -.
DR   BioCyc; ECOL316407:JW2317-MONOMER; -.
DR   BioCyc; MetaCyc:ERYTHRON4PDEHYDROG-MONOMER; -.
DR   BRENDA; 1.1.1.290; 2026.
DR   UniPathway; UPA00244; UER00310.
DR   PRO; PR:P05459; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR   GO; GO:0033711; F:4-phosphoerythronate dehydrogenase activity; IDA:EcoCyc.
DR   GO; GO:0051287; F:NAD binding; IDA:EcoCyc.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0036001; P:'de novo' pyridoxal 5'-phosphate biosynthetic process; IMP:EcoCyc.
DR   GO; GO:0008615; P:pyridoxine biosynthetic process; IMP:EcoCyc.
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   2: Evidence at transcript level;
KW   Complete proteome; Cytoplasm; NAD; Oxidoreductase;
KW   Pyridoxine biosynthesis; Reference proteome.
FT   CHAIN         1    378       Erythronate-4-phosphate dehydrogenase.
FT                                /FTId=PRO_0000075975.
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   378 AA;  41368 MW;  6CEF17691CF2C14A CRC64;
     MKILVDENMP YARDLFSRLG EVTAVPGRPI PVAQLADADA LMVRSVTKVN ESLLAGKPIK
     FVGTATAGTD HVDEAWLKQA GIGFSAAPGC NAIAVVEYVF SSLLMLAERD GFSLYDRTVG
     IVGVGNVGRR LQARLEALGI KTLLCDPPRA DRGDEGDFRS LDELVQRADI LTFHTPLFKD
     GPYKTLHLAD EKLIRSLKPG AILINACRGA VVDNTALLTC LNEGQKLSVV LDVWEGEPEL
     NVELLKKVDI GTSHIAGYTL EGKARGTTQV FEAYSKFIGH EQHVALDTLL PAPEFGRITL
     HGPLDQPTLK RLVHLVYDVR RDDAPLRKVA GIPGEFDKLR KNYLERREWS SLYVICDDAS
     AASLLCKLGF NAVHHPAR
//
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