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Database: UniProt
Entry: A0A0P0P0E0_9CAUL
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Original site: A0A0P0P0E0_9CAUL 
ID   A0A0P0P0E0_9CAUL        Unreviewed;       603 AA.
AC   A0A0P0P0E0;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
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=AQ619_11585 {ECO:0000313|EMBL:ALL13927.1};
OS   Caulobacter henricii.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Caulobacter.
OX   NCBI_TaxID=69395 {ECO:0000313|EMBL:ALL13927.1, ECO:0000313|Proteomes:UP000056905};
RN   [1] {ECO:0000313|EMBL:ALL13927.1, ECO:0000313|Proteomes:UP000056905}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CB4 {ECO:0000313|EMBL:ALL13927.1,
RC   ECO:0000313|Proteomes:UP000056905};
RA   Scott D., Ely B.;
RT   "Conservation of the essential genome among Caulobacter and Brevundimonas
RT   species.";
RL   Submitted (OCT-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}.
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DR   EMBL; CP013002; ALL13927.1; -; Genomic_DNA.
DR   RefSeq; WP_062147548.1; NZ_CP013002.1.
DR   AlphaFoldDB; A0A0P0P0E0; -.
DR   STRING; 69395.AQ619_11585; -.
DR   KEGG; chq:AQ619_11585; -.
DR   eggNOG; COG0129; Bacteria.
DR   OrthoDB; 9807077at2; -.
DR   UniPathway; UPA00226; -.
DR   Proteomes; UP000056905; Chromosome.
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:UP000056905}.
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   603 AA;  63096 MW;  E786F2F3EB598D81 CRC64;
     MSLNPVIARV TDRIIARSRD SRSAYLAHMD AAIASNPGRA KLSCANWAHA FAASPSVDKV
     RALDPNAPNI GIVSAYNDML SAHQPLEAYP ALIKEAAREA GATAQFAGGV PAMCDGVTQG
     RPGMELSLFS RDVIAMATAV ALTHDAFDSA LYLGVCDKIV PGLVIGALTF SHLPALFVPA
     GPMTSGLPNN EKARIRALYA EGKVGRDELL AAESASYHGP GTCTFYGTAN TNQMLMELMG
     FHLPGSAFVH PNTPLREALV KEAARRAAAV TAKGNEYIPV GRMIDEKSVV NGVVGLMATG
     GSTNLALHLV AMAHAAGVIL TLEDLDEISR ATPLLARVYP NGSADVNHFQ AAGGMAFVIR
     ELLKAGLAHE DVLTIAGPGL SRYTQEPALV DGQLTWRDGA AESLDTAIVR PVSDAFSPEG
     GLRMLGGNIG RGVMKISAVK AEHHAITAPA AVFQEQEDFI AAFKRGELDR DVVVVMRFQG
     PAANGMPELH NLSPSISVLL DRGFKVALVT DGRMSGASGK TPAAIHVTPE AAKGGLLAYV
     QDGDLITVDA TNGDLKVLVD EATLRARTPA NVPASKPGFG REMFGWMRAG VGPADHGASV
     LFA
//
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