ID A0A1H0Q0Y3_9RALS Unreviewed; 608 AA.
AC A0A1H0Q0Y3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
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 ORFNames=SAMN04488595_104361 {ECO:0000313|EMBL:SDP11052.1};
OS Ralstonia sp. 25mfcol4.1.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Ralstonia.
OX NCBI_TaxID=1761899 {ECO:0000313|EMBL:SDP11052.1, ECO:0000313|Proteomes:UP000199332};
RN [1] {ECO:0000313|EMBL:SDP11052.1, ECO:0000313|Proteomes:UP000199332}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=25MFCol4.1 {ECO:0000313|EMBL:SDP11052.1,
RC ECO:0000313|Proteomes:UP000199332};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FNJO01000004; SDP11052.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H0Q0Y3; -.
DR STRING; 1761899.SAMN04488595_104361; -.
DR OrthoDB; 9807077at2; -.
DR UniPathway; UPA00226; -.
DR Proteomes; UP000199332; 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 156
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02094"
FT BINDING 223
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02094"
SQ SEQUENCE 608 AA; 64695 MW; 6CD6D41B1F9F897D CRC64;
MPRHPVLEKV TARIVARSAP TRQAYLDRTR AMAGQRVERA NISCTNLAHG VAAMPDEAKI
RLKAQERPNL AIVSAYNDML SAHQPLQAYP QWLKEAALEA GGTAQFAGGT PAMCDGVTQG
QDGMDLSLFS RDVIAMATAV ALSHQMFDGV LCLGVCDKIV PGLVMGALSF GHLPAVFVPG
GPMTTGMSND EKARIRQLYA EGKIDRAGLL EAETRSYHGP GTCTFYGTAN SNQMLMEIMG
LHLPGTAFIN PNTPLREALT RESARQALRL VHGGERYTPI AEVLDERAFV NGIVGLVATG
GSTNHTLHLI AMARVAGIQL TWDDFHELSA SVPLLARVYP NGKADVNQFQ AAGGLSLVIR
GLLSLGLLHD DVNTVAGPGL AHYMREPALR DGKLTWVDGP EASLDDTIVR TADAPFAPDG
GIKLLDGKLG RCVIKTSAVK PEHQVVEAPA IVFHHQDDVL DAFKRGELER DFVAVLPWQG
PAACGMPELH KLTPTLTLLQ DRGFHVALVT DGRMSGASGK VPAAIHVCPE ALSGGAIGRV
RTGDIVRVDA PAGVLTVKVS DADWAARTHD VPDLTANRHG VGRDLFAGFR KHVGTAETGA
CSLFADEG
//