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
//