ID A0A0T6UWF2_9PSED Unreviewed; 608 AA.
AC A0A0T6UWF2;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=AO726_00110 {ECO:0000313|EMBL:KRW61880.1};
OS Pseudomonas sp. TTU2014-080ASC.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1729724 {ECO:0000313|EMBL:KRW61880.1, ECO:0000313|Proteomes:UP000051864};
RN [1] {ECO:0000313|EMBL:KRW61880.1, ECO:0000313|Proteomes:UP000051864}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TTU2014-080ASC {ECO:0000313|EMBL:KRW61880.1,
RC ECO:0000313|Proteomes:UP000051864};
RA Webb H.E., Bugarel M., Den Bakker H.C., Nightingale K., Granier S.A.,
RA Loneragan G.H.;
RT "Carbapenem-non-susceptible Bacteria Recovered from the Faeces of Dairy
RT Cattle.";
RL Submitted (SEP-2015) 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:KRW61880.1}.
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DR EMBL; LKKK01000001; KRW61880.1; -; Genomic_DNA.
DR RefSeq; WP_058066033.1; NZ_LKKK01000001.1.
DR AlphaFoldDB; A0A0T6UWF2; -.
DR STRING; 1729724.AO726_00110; -.
DR OrthoDB; 9807077at2; -.
DR UniPathway; UPA00226; -.
DR Proteomes; UP000051864; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000051864}.
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; 65147 MW; 6F2C22A788A8E7CB CRC64;
MHPRILEVTE RLIERSRETR SAYLRMIRAA ASEGPARGKL QCANFAHGVA GCGGSDKQRL
RLMDSANVAI VTAYNDMLSA HQPYETYPEQ IRQALRDIGS VGQVAGGVPA MCDGVTQGEP
GMEIGLASRE VIAMSTAVAL SHNMFDAAVF LGVCDKIIPG LLMGALRFGH LPSLFIPAGP
MPSGISNKEK ADVRERYSEG KASRDELLES EMKAYHAPGT CTFYGTANTN QMLMEMMGLH
LPGSSFVNPN TPLRDALTQE AARQVVRLTK QGGEFMPLGE LLDERVLINS IVALHATGGS
TNHTLHMPAI ALASGIQLTW QDMADLSEVV PTLAKVYPNG KADVNHFHAA GGVAYMVREL
LDAGLLHEDV NTVMGRGLRR YTQEPFLEDG KLVWREGGLA SLDPNILRPV SEPFSTEGGL
RLMSGNLGRG VMKVSAVAPE HQVVEAPAKV FHDQQALADA FKAGELECDF VAVMRFQGPR
FNGMPELHKM TPYLSVLQDR GFKVALVTDG RMSGASGKIP AAIHVCPEAS DGGPLAKVQE
GDRIRVDGTT GTLQLLVDSS ELASRSAAPS PSGQAVGCGR ELFAFMRAAM STAEQGASAF
TASLERLK
//
