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Database: UniProt
Entry: A0A073J1E9_9RHOB
LinkDB: A0A073J1E9_9RHOB
Original site: A0A073J1E9_9RHOB 
ID   A0A073J1E9_9RHOB        Unreviewed;       601 AA.
AC   A0A073J1E9;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 34.
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=SUH3_19325 {ECO:0000313|EMBL:KEJ95665.1};
OS   Pseudosulfitobacter pseudonitzschiae.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Pseudosulfitobacter.
OX   NCBI_TaxID=1402135 {ECO:0000313|EMBL:KEJ95665.1, ECO:0000313|Proteomes:UP000027746};
RN   [1] {ECO:0000313|EMBL:KEJ95665.1, ECO:0000313|Proteomes:UP000027746}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H3 {ECO:0000313|EMBL:KEJ95665.1,
RC   ECO:0000313|Proteomes:UP000027746};
RA   Lai Q., Hong Z.;
RT   "Sulfitobacter sp. H3 (MCCC 1A00686) Genome Sequencing.";
RL   Submitted (JAN-2014) 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:KEJ95665.1}.
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DR   EMBL; JAMD01000005; KEJ95665.1; -; Genomic_DNA.
DR   RefSeq; WP_037925778.1; NZ_WKFG01000017.1.
DR   AlphaFoldDB; A0A073J1E9; -.
DR   GeneID; 68869594; -.
DR   OrthoDB; 9807077at2; -.
DR   UniPathway; UPA00226; -.
DR   Proteomes; UP000027746; 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:0004792; F:thiosulfate sulfurtransferase activity; IEA:InterPro.
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   InterPro; IPR001307; Thiosulphate_STrfase_CS.
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.
DR   PROSITE; PS00380; RHODANESE_1; 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:UP000027746}.
FT   BINDING         155
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02094"
FT   BINDING         222
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02094"
SQ   SEQUENCE   601 AA;  63346 MW;  4DA0AECC22972D43 CRC64;
     MALAPKIQDV TARIVKRSAD SRAQYLDRMR RAAEDGPRRA HLTCGNQAHA FAAMGAEKAS
     LVEGISPNIG IVTAYNDMLS AHQPFQRFPD LIKQTALANG GTAQVAGGVP AMCDGVTQGQ
     TGMELSLFSR DVIALAAGVA LSHNTFDSAV YLGVCDKIVP GLIIAAATFG YIPSIFLPAG
     PMPSGLPNEE KSKVRQLHAS GQVGRDKLME AEMASYHGPG TCTFYGTANS NQMLMEFMGL
     HLPGASFVNP DTDLRDALTH AGAKRALEIT NLGNDYRPVC DILDERTFVN GLVGLMATGG
     STNLVIHIIA MARAAGVQLD LQDLADISDA TPLMARVYPN GLADVNHFHA AGGLTYMIGE
     LLDAGLLHPD TVTVMGNGLQ DYTQEPKLID GEVRWQDAPR QSQNDRILRP ASDPFAPQGG
     LKQLNGNLGR GVIKISAVAD EHQLVEAPAR VFHDQEEVKA AFKAGTLTDD CVIVVRFQGP
     KANGMPELHA LNPLMAVMQG RGQKVALVTD GRMSGASGKT PAAIHVSPEA LDGGLIAKVR
     DGDMIRLDAK AGTLQVLAEG IEDRAPATAD LSGNTNGVGR ELFAMFRANV GGADTGAAVV
     V
//
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