ID   B8CM78_SHEPW            Unreviewed;       608 AA.
AC   B8CM78;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 77.
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   OrderedLocusNames=swp_2392 {ECO:0000313|EMBL:ACJ29135.1};
OS   Shewanella piezotolerans (strain WP3 / JCM 13877).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=225849 {ECO:0000313|EMBL:ACJ29135.1, ECO:0000313|Proteomes:UP000000753};
RN   [1] {ECO:0000313|EMBL:ACJ29135.1, ECO:0000313|Proteomes:UP000000753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WP3 / JCM 13877 {ECO:0000313|Proteomes:UP000000753};
RX   PubMed=18398463; DOI=10.1371/journal.pone.0001937;
RA   Wang F., Wang J., Jian H., Zhang B., Li S., Wang F., Zeng X., Gao L.,
RA   Bartlett D.H., Yu J., Hu S., Xiao X.;
RT   "Environmental adaptation: genomic analysis of the piezotolerant and
RT   psychrotolerant deep-sea iron reducing bacterium Shewanella piezotolerans
RT   WP3.";
RL   PLoS ONE 3:E1937-E1937(2008).
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; CP000472; ACJ29135.1; -; Genomic_DNA.
DR   RefSeq; WP_020912495.1; NC_011566.1.
DR   AlphaFoldDB; B8CM78; -.
DR   STRING; 225849.swp_2392; -.
DR   KEGG; swp:swp_2392; -.
DR   eggNOG; COG0129; Bacteria.
DR   HOGENOM; CLU_014271_1_2_6; -.
DR   OrthoDB; 9807077at2; -.
DR   UniPathway; UPA00226; -.
DR   Proteomes; UP000000753; 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}.
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;  64639 MW;  96CB43DC52590779 CRC64;
     MHTVVQSVTD RIIERSKDSR AKYLAALEDA KNRGVHRSAL SCGNLAHGFA ACNPADKSSI
     KQLTKANIGI VTSFNDMLSA HQPYGEYPDL LKQACNEVGS VAQVAGGVPA MCDGVTQGQP
     GMELSLLSRE VIAMGTAVGL SHNMFDGALL LGICDKIVPG LLIGALSFGH LPMLFVPAGP
     MKSGIPNKEK ARIRQKYAQG EVDREALLDA ESKSYHSAGT CTFYGTANSN QLMLEVMGLQ
     LPGSSFVNPD DPLREVLSKT AAKQVCRLTE MGTQYTPIGH IVSEKSIVNG IVALLATGGS
     TNLTMHIVAA ARAAGVIINW DDFSELSDAV PLLARVYPNG HADINHFHAA GGMAFLIKEL
     LDGGLLHEDV ETVAGFGLKR YTQEPQIRDG ELTWVDGQKT SLDSEVLTSL NSPFQANGGL
     KLLKGNLGRA VIKVSAVQEQ HRIVEAPAVV IDDQNKLEAI FKAGELDKDC VVVVKGQGPK
     AIGMPELHKL TPILGTLQDR GFKVALLTDG RMSGASGKVP AAIHLTPEAL DGGMIAKIHN
     GDLVRVNATT GELTLLVDEA ELQARMPEKV DLQKTSYGMG RELFGALRAS LSSPETGARS
     TSAIDEIY
//