ID R0DTC8_RALPI Unreviewed; 609 AA.
AC R0DTC8;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 38.
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=OR214_03472 {ECO:0000313|EMBL:ENZ76733.1};
OS Ralstonia pickettii OR214.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Ralstonia.
OX NCBI_TaxID=1264675 {ECO:0000313|EMBL:ENZ76733.1, ECO:0000313|Proteomes:UP000013280};
RN [1] {ECO:0000313|EMBL:ENZ76733.1, ECO:0000313|Proteomes:UP000013280}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OR214 {ECO:0000313|EMBL:ENZ76733.1,
RC ECO:0000313|Proteomes:UP000013280};
RX PubMed=23792748;
RA Utturkar S.M., Bollmann A., Brzoska R.M., Klingeman D.M., Epstein S.E.,
RA Palumbo A.V., Brown S.D.;
RT "Draft Genome Sequence for Ralstonia sp. Strain OR214, a Bacterium with
RT Potential for Bioremediation.";
RL Genome Announc. 1:0-0(2013).
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:ENZ76733.1}.
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DR EMBL; APMQ01000009; ENZ76733.1; -; Genomic_DNA.
DR RefSeq; WP_004632649.1; NZ_APMQ01000009.1.
DR AlphaFoldDB; R0DTC8; -.
DR PATRIC; fig|1264675.3.peg.3405; -.
DR UniPathway; UPA00226; -.
DR Proteomes; UP000013280; 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 609 AA; 64865 MW; ADA0947BED3A5633 CRC64;
MALHRTLAAV TQRIIDRSRG PRQAYLDVTR KNAGRRVERT LLSCTNLAHG FAAMPGEAKI
RLKALERPNL GIVSAYNDML SAHQPLEAFP AWLKQAALDA GGTAQFAGGV PAMCDGVTQG
QDGMELSLFS RDTIALSTAV ALSHQMFDAA LYLGVCDKIV PGLVIGALSF GHLPAVFVPA
GPMTTGISND EKARTRQLYA EGKLSRADLL EAESKSYHGA GTCTFYGTAN SNQMLMEVMG
LHLPGTAFIN PNTPLREALT RESARQALKL VFSGDQYTPI ADVLDERAFV NGIVGLLATG
GSTNHTLHLV AMARAAGILL TWDDFNDLSG VIPLLARVYP NGKADVNEFQ AAGGLSIVIR
ELIDAGLLHD DVTTIMGKGL RRHAQEPFLD GEKLVWRDGA AASLDTNIVR GVAEPFSPDG
GLRVLDGNIG RSVIKVSAVK PEHRFVEAPA RVFLAQDDLI NAFKAGELER DFVAVLPYQG
PAANGMPELH KLTPTLSVLQ ERGFKVALVT DGRMSGASGK VPAAIHITPE ALNGGPLARV
RDGDIVVLDA EAGTLQVRVP EAEWNARQVT APDLSHYHAG VGRDLFSGFR RNVSPAEEGA
CTLFVSAGA
//
