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Database: UniProt
Entry: J0H5E3_HELPX
LinkDB: J0H5E3_HELPX
Original site: J0H5E3_HELPX 
ID   J0H5E3_HELPX            Unreviewed;       608 AA.
AC   J0H5E3;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   RecName: Full=Phosphogluconate dehydratase {ECO:0000256|HAMAP-Rule:MF_02094};
DE            EC=4.2.1.12 {ECO:0000256|HAMAP-Rule:MF_02094};
GN   Name=edd {ECO:0000256|HAMAP-Rule:MF_02094,
GN   ECO:0000313|EMBL:EJC32904.1};
GN   ORFNames=HPHPP13B_0640 {ECO:0000313|EMBL:EJC32904.1};
OS   Helicobacter pylori Hp P-13b.
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=992107 {ECO:0000313|EMBL:EJC32904.1, ECO:0000313|Proteomes:UP000003392};
RN   [1] {ECO:0000313|EMBL:EJC32904.1, ECO:0000313|Proteomes:UP000003392}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hp P-13b {ECO:0000313|EMBL:EJC32904.1,
RC   ECO:0000313|Proteomes:UP000003392};
RA   Blanchard T.G., Czinn S.J., McCracken C., Abolude K., Maroo A.,
RA   Santana-Cruz I., Tallon L.J., Ficke F.W.F.;
RT   "Genome sequence of Helicobacter pylori Hp P-13b.";
RL   Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the dehydration of 6-phospho-D-gluconate to 2-
CC       dehydro-3-deoxy-6-phospho-D-gluconate. {ECO:0000256|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:0000256|HAMAP-Rule:MF_02094};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_02094};
CC       Note=Binds 1 [4Fe-4S] cluster. {ECO:0000256|HAMAP-Rule:MF_02094};
CC   -!- PATHWAY: Carbohydrate metabolism; Entner-Doudoroff pathway.
CC       {ECO:0000256|HAMAP-Rule:MF_02094}.
CC   -!- SIMILARITY: Belongs to the IlvD/Edd family.
CC       {ECO:0000256|ARBA:ARBA00006486, ECO:0000256|HAMAP-Rule:MF_02094}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EJC32904.1}.
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DR   EMBL; AKQI01000004; EJC32904.1; -; Genomic_DNA.
DR   RefSeq; WP_001123999.1; NZ_AKQI01000004.1.
DR   AlphaFoldDB; J0H5E3; -.
DR   PATRIC; fig|992107.3.peg.619; -.
DR   UniPathway; UPA00226; -.
DR   Proteomes; UP000003392; Unassembled WGS sequence.
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; IlvD/EDD C-terminal domain-like; 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   NCBIfam; TIGR01196; edd; 1.
DR   PANTHER; PTHR43661; D-XYLONATE DEHYDRATASE; 1.
DR   PANTHER; PTHR43661:SF1; PHOSPHOGLUCONATE DEHYDRATASE; 1.
DR   Pfam; PF00920; ILVD_EDD; 1.
DR   SUPFAM; SSF143975; IlvD/EDD N-terminal domain-like; 1.
DR   SUPFAM; SSF52016; LeuD/IlvD-like; 1.
DR   PROSITE; PS00886; ILVD_EDD_1; 1.
DR   PROSITE; PS00887; ILVD_EDD_2; 1.
PE   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|HAMAP-Rule:MF_02094};
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277, ECO:0000256|HAMAP-
KW   Rule:MF_02094};
KW   Gluconate utilization {ECO:0000256|ARBA:ARBA00023064, ECO:0000256|HAMAP-
KW   Rule:MF_02094}; Iron {ECO:0000256|HAMAP-Rule:MF_02094};
KW   Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_02094};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_02094};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_02094}.
FT   BINDING         154
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02094"
FT   BINDING         221
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02094"
SQ   SEQUENCE   608 AA;  66691 MW;  CB3BCA4681594896 CRC64;
     MPKHSLEQIK EKITERSKKT REFYLENIFN 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 AFEACGGLAF VIKELLKEGL
     LFEDTHTIMD TETQKGMQNY TKTPFLENDQ LVYKDAVSHS LNTDILRPVS EPFAVNGGLK
     ILKGNLGRAV IKISAIKDEH RKVKARAIVF KTQSEFLERF KNKELERDFV AVLPFQGPKS
     NGMPELHKLT TNLGALQDMG YKVALVTDGR MSGASGKVPS AIHLSPEGAL NGAIIKIKDG
     DLIELDAPNN ALNVLEKDFE KRGINPLFLE TLENLEKPTF GLGRELFTSL RLNVNTAEEG
     GMSFGIKI
//
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