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Database: UniProt
Entry: I9WK27_9SPHN
LinkDB: I9WK27_9SPHN
Original site: I9WK27_9SPHN 
ID   I9WK27_9SPHN            Unreviewed;       608 AA.
AC   I9WK27;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 39.
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=WSK_0654 {ECO:0000313|EMBL:EIZ80681.1};
OS   Novosphingobium sp. Rr 2-17.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Novosphingobium.
OX   NCBI_TaxID=555793 {ECO:0000313|EMBL:EIZ80681.1, ECO:0000313|Proteomes:UP000004732};
RN   [1] {ECO:0000313|EMBL:EIZ80681.1, ECO:0000313|Proteomes:UP000004732}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RR2-17 {ECO:0000313|Proteomes:UP000004732};
RX   PubMed=22933764; DOI=10.1128/JB.01159-12;
RA   Gan H.M., Chew T.H., Hudson A.O., Savka M.A.;
RT   "Genome Sequence of Novosphingobium sp. Strain Rr 2-17, a Nopaline Crown
RT   Gall-Associated Bacterium Isolated from Vitis vinifera L. Grapevine.";
RL   J. Bacteriol. 194:5137-5138(2012).
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:EIZ80681.1}.
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DR   EMBL; AKFJ01000010; EIZ80681.1; -; Genomic_DNA.
DR   RefSeq; WP_008993616.1; NZ_AKFJ01000010.1.
DR   AlphaFoldDB; I9WK27; -.
DR   PATRIC; fig|555793.3.peg.657; -.
DR   eggNOG; COG0129; Bacteria.
DR   OrthoDB; 9807077at2; -.
DR   UniPathway; UPA00226; -.
DR   Proteomes; UP000004732; 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:UP000004732}.
FT   REGION          560..581
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         160
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02094"
FT   BINDING         227
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02094"
SQ   SEQUENCE   608 AA;  64349 MW;  7E3501BC4F30C21A CRC64;
     MANFHPGIHP VVARVTDRII QRSGESRKRY LDLVERETDR HSDRSFLSCS NLAHGFAASG
     EDKPALSGSK AVNLGIVTAY NDMLSAHQPY GRYPEQMKLF AREVGATAQV ASGVPAMCDG
     VTQGFDGMEL SLFSRDTIAL STAIALSHAM FDGMALLGIC DKIVPGLVIG ALRFGHLPAV
     FVPAGPMPSG ISNKDKQKVR QLYAEGKVGR EELLASESAS YHAAGTCTFY GTANSNQMMM
     EMMGLHVPGS AFVPPNTPLR QALTRKATHR LAEITRKGQD YRPMAHVVDE KAIVNAICGL
     LATGGSTNHA IHLPAMARAA GVLINWEDFD ELSSVVPLIA RVYPNGSGDV NHFHAAGGMA
     WIASELLGAG LAHGDVLTIA EGGMDAYATE PVLSGDTVEW RPAPKVSGDE TMLKPVSDPF
     LPDGGMRLVE GNLGRATFKT SAVDAERWTI EAPCRVFDTQ EGVAQAFKAG ELDRDVVVVV
     RFQGPRANGM PELHKLTPPL GVLQDRGHKV ALVTDGRMSG ASGKVPAAIH VTPEAFAGGP
     LAFLQDGDIV RLSADDGTLS TTADLSGREP APTPPPASGM GRELFAMFRL NASGAEQGAS
     SMLELAGL
//
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