EDD_ECOLI
ID EDD_ECOLI Reviewed; 603 AA.
AC P0ADF6; P25530;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Phosphogluconate dehydratase {ECO:0000255|HAMAP-Rule:MF_02094, ECO:0000305};
DE EC=4.2.1.12 {ECO:0000255|HAMAP-Rule:MF_02094, ECO:0000269|PubMed:17102132, ECO:0000269|PubMed:1846355};
DE AltName: Full=6-phosphogluconate dehydratase {ECO:0000303|PubMed:1846355};
DE AltName: Full=Entner-Doudoroff dehydrase {ECO:0000303|PubMed:5337844};
GN Name=edd {ECO:0000255|HAMAP-Rule:MF_02094, ECO:0000303|PubMed:5337844};
GN OrderedLocusNames=b1851, JW1840;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RX PubMed=1624451; DOI=10.1128/jb.174.14.4638-4646.1992;
RA Egan S.E., Fliege R., Tong S., Shibata A., Wolf R.E. Jr., Conway T.;
RT "Molecular characterization of the Entner-Doudoroff pathway in Escherichia
RT coli: sequence analysis and localization of promoters for the edd-eda
RT operon.";
RL J. Bacteriol. 174:4638-4646(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=8344525; DOI=10.1016/0378-1119(93)90362-7;
RA Carter A.T., Pearson B.M., Dickinson J.R., Lancashire W.E.;
RT "Sequence of the Escherichia coli K-12 edd and eda genes of the Entner-
RT Doudoroff pathway.";
RL Gene 130:155-156(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA Horiuchi T.;
RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 40.1-50.0 min region on the linkage map.";
RL DNA Res. 3:379-392(1996).
RN [4]
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., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
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 MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 238-603.
RC STRAIN=K12;
RA Smith J.M., Nygaard P.;
RT "Purine and one-carbon metabolism in Escherichia coli K12: DNA sequence of
RT a second GAR transformylase.";
RL Submitted (JUL-1993) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP DISRUPTION PHENOTYPE, AND PATHWAY.
RX PubMed=5337844; DOI=10.1128/jb.93.5.1579-1581.1967;
RA Zablotny R., Fraenkel D.G.;
RT "Glucose and gluconate metabolism in a mutant of Escherichia coli lacking
RT gluconate-6-phosphate dehydrase.";
RL J. Bacteriol. 93:1579-1581(1967).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=1846355; DOI=10.1016/s0021-9258(18)52319-x;
RA Gardner P.R., Fridovich I.;
RT "Superoxide sensitivity of the Escherichia coli 6-phosphogluconate
RT dehydratase.";
RL J. Biol. Chem. 266:1478-1483(1991).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=17102132; DOI=10.1074/jbc.m607646200;
RA Jang S., Imlay J.A.;
RT "Micromolar intracellular hydrogen peroxide disrupts metabolism by damaging
RT iron-sulfur enzymes.";
RL J. Biol. Chem. 282:929-937(2007).
CC -!- FUNCTION: Catalyzes the dehydration of 6-phospho-D-gluconate to 2-
CC dehydro-3-deoxy-6-phospho-D-gluconate. {ECO:0000255|HAMAP-
CC Rule:MF_02094, ECO:0000269|PubMed:17102132,
CC ECO:0000269|PubMed:1846355}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=6-phospho-D-gluconate = 2-dehydro-3-deoxy-6-phospho-D-
CC gluconate + H2O; Xref=Rhea:RHEA:17277, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:57569, ChEBI:CHEBI:58759; EC=4.2.1.12;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02094,
CC ECO:0000269|PubMed:17102132, ECO:0000269|PubMed:1846355};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000250|UniProtKB:P05791,
CC ECO:0000255|HAMAP-Rule:MF_02094, ECO:0000305|PubMed:17102132};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250|UniProtKB:P05791,
CC ECO:0000255|HAMAP-Rule:MF_02094};
CC -!- ACTIVITY REGULATION: Sensitive to oxidants such as superoxide or
CC hydrogen peroxide. {ECO:0000269|PubMed:17102132,
CC ECO:0000269|PubMed:1846355}.
CC -!- PATHWAY: Carbohydrate metabolism; Entner-Doudoroff pathway.
CC {ECO:0000255|HAMAP-Rule:MF_02094, ECO:0000269|PubMed:5337844}.
CC -!- INDUCTION: By growth on gluconate. {ECO:0000269|PubMed:1624451}.
CC -!- DISRUPTION PHENOTYPE: The mutant grows at normal rates on glucose and
CC fructose, whereas on gluconate it grows about one-third as fast as the
CC wild-type. {ECO:0000269|PubMed:5337844}.
CC -!- SIMILARITY: Belongs to the IlvD/Edd family. {ECO:0000255|HAMAP-
CC Rule:MF_02094, ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M87458; AAA23722.1; -; Genomic_DNA.
DR EMBL; X63694; CAA45221.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74921.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15659.1; -; Genomic_DNA.
DR EMBL; L20897; AAA23863.1; -; Genomic_DNA.
DR PIR; A42986; A42986.
DR RefSeq; NP_416365.1; NC_000913.3.
DR RefSeq; WP_001069467.1; NZ_SSZK01000001.1.
DR AlphaFoldDB; P0ADF6; -.
DR SMR; P0ADF6; -.
DR BioGRID; 4261382; 12.
DR DIP; DIP-47906N; -.
DR IntAct; P0ADF6; 12.
DR STRING; 511145.b1851; -.
DR PaxDb; P0ADF6; -.
DR PRIDE; P0ADF6; -.
DR DNASU; 946362; -.
DR EnsemblBacteria; AAC74921; AAC74921; b1851.
DR EnsemblBacteria; BAA15659; BAA15659; BAA15659.
DR GeneID; 67415450; -.
DR GeneID; 946362; -.
DR KEGG; ecj:JW1840; -.
DR KEGG; eco:b1851; -.
DR PATRIC; fig|511145.12.peg.1929; -.
DR EchoBASE; EB0253; -.
DR eggNOG; COG0129; Bacteria.
DR HOGENOM; CLU_014271_1_2_6; -.
DR InParanoid; P0ADF6; -.
DR OMA; CANIAHV; -.
DR PhylomeDB; P0ADF6; -.
DR BioCyc; EcoCyc:PGLUCONDEHYDRAT-MON; -.
DR BioCyc; MetaCyc:PGLUCONDEHYDRAT-MON; -.
DR UniPathway; UPA00226; -.
DR PRO; PR:P0ADF6; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016836; F:hydro-lyase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004456; F:phosphogluconate dehydratase activity; IDA:EcoCyc.
DR GO; GO:0046177; P:D-gluconate catabolic process; IMP:EcoCyc.
DR GO; GO:0009255; P:Entner-Doudoroff pathway through 6-phosphogluconate; IEA:UniProtKB-UniRule.
DR Gene3D; 3.50.30.80; -; 1.
DR HAMAP; MF_02094; Edd; 1.
DR InterPro; IPR004786; 6-phosphgluc_deHydtase.
DR InterPro; IPR042096; Dihydro-acid_dehy_C.
DR InterPro; IPR000581; DiOHA_6PGluconate_deHydtase.
DR InterPro; IPR020558; DiOHA_6PGluconate_deHydtase_CS.
DR InterPro; IPR037237; IlvD/EDD_N.
DR PANTHER; PTHR43661:SF1; PTHR43661:SF1; 1.
DR Pfam; PF00920; ILVD_EDD; 1.
DR SUPFAM; SSF143975; SSF143975; 1.
DR TIGRFAMs; TIGR01196; edd; 1.
DR PROSITE; PS00886; ILVD_EDD_1; 1.
DR PROSITE; PS00887; ILVD_EDD_2; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Carbohydrate metabolism; Gluconate utilization; Iron; Iron-sulfur;
KW Lyase; Metal-binding; Reference proteome.
FT CHAIN 1..603
FT /note="Phosphogluconate dehydratase"
FT /id="PRO_0000103553"
FT BINDING 154
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P05791, ECO:0000255|HAMAP-
FT Rule:MF_02094"
FT BINDING 221
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P05791, ECO:0000255|HAMAP-
FT Rule:MF_02094"
FT CONFLICT 252..254
FT /note="PLR -> AC (in Ref. 1; AAA23722)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 603 AA; 64639 MW; D046405193BFC185 CRC64;
MNPQLLRVTN RIIERSRETR SAYLARIEQA KTSTVHRSQL ACGNLAHGFA ACQPEDKASL
KSMLRNNIAI ITSYNDMLSA HQPYEHYPEI IRKALHEANA VGQVAGGVPA MCDGVTQGQD
GMELSLLSRE VIAMSAAVGL SHNMFDGALF LGVCDKIVPG LTMAALSFGH LPAVFVPSGP
MASGLPNKEK VRIRQLYAEG KVDRMALLES EAASYHAPGT CTFYGTANTN QMVVEFMGMQ
LPGSSFVHPD SPLRDALTAA AARQVTRMTG NGNEWMPIGK MIDEKVVVNG IVALLATGGS
TNHTMHLVAM ARAAGIQINW DDFSDLSDVV PLMARLYPNG PADINHFQAA GGVPVLVREL
LKAGLLHEDV NTVAGFGLSR YTLEPWLNNG ELDWREGAEK SLDSNVIASF EQPFSHHGGT
KVLSGNLGRA VMKTSAVPVE NQVIEAPAVV FESQHDVMPA FEAGLLDRDC VVVVRHQGPK
ANGMPELHKL MPPLGVLLDR CFKIALVTDG RLSGASGKVP SAIHVTPEAY DGGLLAKVRD
GDIIRVNGQT GELTLLVDEA ELAAREPHIP DLSASRVGTG RELFSALREK LSGAEQGATC
ITF
