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Database: UniProt
Entry: A0A0N1EHU3_9SPHN
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ID   A0A0N1EHU3_9SPHN        Unreviewed;       604 AA.
AC   A0A0N1EHU3;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 27.
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=ADT71_18865 {ECO:0000313|EMBL:KPH60854.1}, EDF59_108120
GN   {ECO:0000313|EMBL:TCM38430.1};
OS   Novosphingobium sp. ST904.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Novosphingobium.
OX   NCBI_TaxID=1684385 {ECO:0000313|EMBL:KPH60854.1, ECO:0000313|Proteomes:UP000037878};
RN   [1] {ECO:0000313|EMBL:KPH60854.1, ECO:0000313|Proteomes:UP000037878}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ST904 {ECO:0000313|EMBL:KPH60854.1,
RC   ECO:0000313|Proteomes:UP000037878};
RA   Thijs S., Bottos E.M., Van Hamme J.D., Gkorezis P., Rineau F.,
RA   Vangronsveld J.;
RT   "Novosphingobium nitrophenolicus strain ST904 degrades p-nitrophenol and
RT   stimulates plant growth.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:TCM38430.1, ECO:0000313|Proteomes:UP000295740}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ST904 {ECO:0000313|EMBL:TCM38430.1,
RC   ECO:0000313|Proteomes:UP000295740};
RA   Whitman W.;
RT   "Genomic Encyclopedia of Type Strains, Phase IV (KMG-V): Genome sequencing
RT   to study the core and pangenomes of soil and plant-associated
RT   prokaryotes.";
RL   Submitted (MAR-2019) 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:KPH60854.1}.
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DR   EMBL; LGJH01000155; KPH60854.1; -; Genomic_DNA.
DR   EMBL; SLVC01000008; TCM38430.1; -; Genomic_DNA.
DR   RefSeq; WP_054439318.1; NZ_SLVC01000008.1.
DR   AlphaFoldDB; A0A0N1EHU3; -.
DR   STRING; 1684385.ADT71_18865; -.
DR   PATRIC; fig|1684385.3.peg.1027; -.
DR   OrthoDB; 9807077at2; -.
DR   UniPathway; UPA00226; -.
DR   Proteomes; UP000037878; Unassembled WGS sequence.
DR   Proteomes; UP000295740; 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:UP000037878}.
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   604 AA;  64022 MW;  A07519FEA2A5C024 CRC64;
     MSNLSPVVAR VTDRIIERSK PSRERYLAMI EREAGRHSDR SFLSCSNLAH GFAASGEDKP
     AIATGKAINV GIVTAYNDML SAHQPYGRYP EQMKLYAREV GATAQVAGGV PAMCDGVTQG
     FDGMELSLFS RDTIALSTAV SLSHAMYDGM TLLGICDKIV PGLVMGALRF GHLPAVFIPS
     GPMPSGISNK EKQKVRQLYA EGKVGREELL ASESASYHSA GTCTFYGTAN SNQMMMEMMG
     LHMPGAAFVP PGTSLRQAVT RAAVHRVTEM TRKGDDFRPM GHVVDEKAIV NAIVGLLATG
     GSTNHAIHLP AMARCAGIHI DWQDFDELSG AVPLITRVYP NGSGDVNHFH AAGGMGWVVR
     ELLDAGLAHE DILTVSSGGM RAYATEPTLD DGELKWKPAP AVSGDDSMLS TVAKPFLPDG
     GMRLVSGNVG RATFKTSAVD QERWTIEAPC RVFETQEAVI NAFKAGELDR DVVVVVRHQG
     PRANGMPELH KLTPPLGVLQ DRGFKVALVT DGRMSGASGK VPAAIHVTPE ALADGPIAYL
     QDGDIVRLSA EDGTLSTTAD LSGRSPAPLP APAEGMGREL FAMFRMNAGG AEQGGSSMLE
     VAGL
//
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