ID   EDD_HELPY               Reviewed;         608 AA.
AC   P56111;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Phosphogluconate dehydratase {ECO:0000255|HAMAP-Rule:MF_02094};
DE            EC=4.2.1.12 {ECO:0000255|HAMAP-Rule:MF_02094};
GN   Name=edd {ECO:0000255|HAMAP-Rule:MF_02094}; OrderedLocusNames=HP_1100;
OS   Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=85962;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700392 / 26695;
RX   PubMed=9252185; DOI=10.1038/41483;
RA   Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA   Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA   Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA   Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA   McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA   Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA   Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA   Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT   "The complete genome sequence of the gastric pathogen Helicobacter
RT   pylori.";
RL   Nature 388:539-547(1997).
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}.
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   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_02094};
CC       Note=Binds 1 [4Fe-4S] cluster. {ECO:0000255|HAMAP-Rule:MF_02094};
CC   -!- PATHWAY: Carbohydrate metabolism; Entner-Doudoroff pathway.
CC       {ECO:0000255|HAMAP-Rule:MF_02094}.
CC   -!- SIMILARITY: Belongs to the IlvD/Edd family. {ECO:0000255|HAMAP-
CC       Rule:MF_02094, ECO:0000305}.
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DR   EMBL; AE000511; AAD08143.1; -; Genomic_DNA.
DR   PIR; D64657; D64657.
DR   RefSeq; NP_207891.1; NC_000915.1.
DR   RefSeq; WP_001124018.1; NC_018939.1.
DR   AlphaFoldDB; P56111; -.
DR   SMR; P56111; -.
DR   STRING; 85962.C694_05675; -.
DR   PaxDb; P56111; -.
DR   EnsemblBacteria; AAD08143; AAD08143; HP_1100.
DR   KEGG; hpy:HP_1100; -.
DR   PATRIC; fig|85962.47.peg.1180; -.
DR   eggNOG; COG0129; Bacteria.
DR   OMA; CANIAHV; -.
DR   PhylomeDB; P56111; -.
DR   UniPathway; UPA00226; -.
DR   Proteomes; UP000000429; 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; IEA:UniProtKB-UniRule.
DR   GO; GO:0046177; P:D-gluconate catabolic process; IEA:UniProtKB-UniRule.
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   3: Inferred from homology;
KW   4Fe-4S; Carbohydrate metabolism; Gluconate utilization; Iron; Iron-sulfur;
KW   Lyase; Metal-binding; Reference proteome.
FT   CHAIN           1..608
FT                   /note="Phosphogluconate dehydratase"
FT                   /id="PRO_0000103555"
FT   BINDING         154
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02094"
FT   BINDING         221
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02094"
SQ   SEQUENCE   608 AA;  66655 MW;  47EF7E62E3371F59 CRC64;
     MPKHSLEQIK EKITERSKKT RELYLENIFN PKNQPKIESL GCANIAHVTA SMPEHLKMPL
     GSHKRKHFAI ITAYNDMLSA HQPFKNYPDL IKKELQEHNA YASVASGVPA MCDGITQGYD
     GMELSLFSRD VIALSTAVGL SHNVFDGAFF LGVCDKIVPG LLIGALSFGN LASVFVPSGP
     MVSGIENYKK AKARQDFAMG KINREELLKV EMQSYHDVGT CTFYGTANSN QMMMEFMGLH
     VANSSFINPN NPLRKVLVEE SAKRLASGKV LPLAKLIDEK SILNALIGLM ATGGSTNHTL
     HLIAIARSCG VILNWDDFDA VSNLIPLLAK VYPNGSADVN AFEACGGLVF VIKELLKEGL
     LFEDTHTIMD TETQKGMQNY TKTPFLENNQ LVYKDAINHS LNTDILRPVS DPFAANGGLK
     ILKGNLGRAV IKISAIKDEH RKVKARAIVF KTQSEFLERF KNKELERDFV AVLPFQGPKS
     NGMPELHKLT TNLGALQDMG YKVALVTDGR MSGASGKVPS AIHLSPEGAL NGAIIKIKDG
     DLIELDAPNN ALNVLEKDFE KRGINPLFLE TLENLEKPSF GLGRELFTSL RLNVNTAEEG
     GMSFGIKV