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Database: UniProt
Entry: A0A1C3JWY2_9BURK
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ID   A0A1C3JWY2_9BURK        Unreviewed;       602 AA.
AC   A0A1C3JWY2;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 31.
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=ODI_01145 {ECO:0000313|EMBL:SBT23763.1}, ODI_R2299
GN   {ECO:0000313|EMBL:SOE49775.1};
OS   Orrella dioscoreae.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Orrella.
OX   NCBI_TaxID=1851544 {ECO:0000313|EMBL:SBT23763.1, ECO:0000313|Proteomes:UP000078558};
RN   [1] {ECO:0000313|EMBL:SBT23763.1, ECO:0000313|Proteomes:UP000078558}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Orrdi1 {ECO:0000313|EMBL:SBT23763.1};
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:SOE49775.1, ECO:0000313|Proteomes:UP000078558}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Orrdi1 {ECO:0000313|EMBL:SOE49775.1};
RA   de Groot N.N.;
RL   Submitted (AUG-2017) 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; FLRC01000003; SBT23763.1; -; Genomic_DNA.
DR   EMBL; LT907988; SOE49775.1; -; Genomic_DNA.
DR   RefSeq; WP_067749246.1; NZ_LT907988.1.
DR   AlphaFoldDB; A0A1C3JWY2; -.
DR   STRING; 1851544.ODI_01145; -.
DR   KEGG; odi:ODI_R2299; -.
DR   OrthoDB; 9807077at2; -.
DR   UniPathway; UPA00226; -.
DR   Proteomes; UP000078558; Chromosome i.
DR   Proteomes; UP000078558; 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:UP000078558}.
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   602 AA;  63245 MW;  8887ADDDAF919DA4 CRC64;
     MALHATLDAV TARIRARSAE PRAAYLARLD AQSRRDRGAD RLGCANVAHA FAGMPGNDKL
     RVVAERARNI GIVTAYNDML SAHAPLQHYP DVLKDEARRH GATAQVAGGV PAMCDGVTQG
     TPGMELSLFS RDVIAMATAV SLSHDVFDAA LMLGVCDKIV PGLLIGALHF GHLPTVFVPA
     GPMTSGLSNS AKARVRERAA QGLVGRAELL QAESAAYHGQ GTCTFYGTAN SNQMLLEAMG
     LHVPGTAFIN PGEGLREALT RDAARRVLAQ GCPAIGRVVD ERAIVNAMVA LLATGGSTNH
     LIHWVAVARA AGLVIDWDDF AALSAVVPLL ARVYPNGAAD VNQFQAAGGP GYVLRELLDA
     GLMHEDVLTI SADGIRAYTR LPVAAADERL SWDPIGDSTD LDVLRPAAAP FSATGGLRLL
     QGNLGRGVIK VSAVPEDRHV VEAPARVFDT QADLQAAFQA GELDRDVVCV VRWQGPRANG
     MPELHKLTPP LAVLQGKGFR VALVTDGRMS GASGKVPAAI HVTPEALADG PLARVQDGDV
     IRLDAVQGTL DALVDAQTWA ARVPARPPVS MDEANGVGWG RELFAGFRRN APGAEEGACT
     WL
//
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