EDD_HELPJ
ID EDD_HELPJ Reviewed; 608 AA.
AC Q9ZKB3;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 106.
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=jhp_1026;
OS Helicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J99 / ATCC 700824;
RX PubMed=9923682; DOI=10.1038/16495;
RA Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C.,
RA Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J.,
RA Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D.,
RA Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.;
RT "Genomic sequence comparison of two unrelated isolates of the human gastric
RT pathogen Helicobacter pylori.";
RL Nature 397:176-180(1999).
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; AE001439; AAD06597.1; -; Genomic_DNA.
DR PIR; E71859; E71859.
DR RefSeq; WP_001124101.1; NZ_CP011330.1.
DR AlphaFoldDB; Q9ZKB3; -.
DR SMR; Q9ZKB3; -.
DR STRING; 85963.jhp_1026; -.
DR EnsemblBacteria; AAD06597; AAD06597; jhp_1026.
DR KEGG; hpj:jhp_1026; -.
DR PATRIC; fig|85963.30.peg.1565; -.
DR eggNOG; COG0129; Bacteria.
DR OMA; CANIAHV; -.
DR UniPathway; UPA00226; -.
DR Proteomes; UP000000804; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
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.
FT CHAIN 1..608
FT /note="Phosphogluconate dehydratase"
FT /id="PRO_0000103556"
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; 66603 MW; 978A046F3AE15F98 CRC64;
MPKHSLEQIK EKITERSKKT RELYLENTFN PKNQPKIESL GCANIAHVTA SMPEHLKMPL
GSHKRKHFAI ITAYNDMLSA HQPFKNYPDL IKKELQEHNA YASVASGVPA MCDGITQGYE
GMELSLFSRD VIALSTAVGL SHNVFDGAFF LGVCDKIVPG LLIGALSFGN LASVFVPSGP
MVSGIENYKK AKARQDFAMG KINREELLKV EMQSYHDVGT CTFYGTANSN QMMMEFMGLH
VANSSFINPN NPLRKVLVEE SAKRLASGKV LPLAKLIDEK SILNALIGLM ATGGSTNHTL
HLIAIARSCG VILNWDDFDA ISNLIPLLAK VYPNGSADVN AFEACGGLAF VIKELLKEGL
LFEDTHTIMD TETQKGMQNY TKTPFLENDQ LVYKDAVSHS LNTDILRPVS EPFAANGGLK
ILKGNLGRAV IKISAIKDEH RKVKARAIVF KTQSEFLERF KNKELERDFV AVLPFQGPKS
NGMPELHKLT TNLGALQDMG YKVALVTDGR MSGASGKVPS AIHLSPEGAL NGAIIKIKDG
DLIELDAPNN ALNVLEKDFE KRGINPLFLE TLENLEKPTF GLGRELFTSL RLNANTAEEG
GMSFGIKV