ID K9NNW7_9PSED Unreviewed; 608 AA.
AC K9NNW7;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 46.
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 ECO:0000313|EMBL:AFY21454.1};
GN ORFNames=PputUW4_04262 {ECO:0000313|EMBL:AFY21454.1};
OS Pseudomonas sp. UW4.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1207075 {ECO:0000313|EMBL:AFY21454.1, ECO:0000313|Proteomes:UP000010397};
RN [1] {ECO:0000313|EMBL:AFY21454.1, ECO:0000313|Proteomes:UP000010397}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UW4 {ECO:0000313|EMBL:AFY21454.1,
RC ECO:0000313|Proteomes:UP000010397};
RX PubMed=23516524;
RA Duan J., Jiang W., Cheng Z., Heikkila J.J., Glick B.R.;
RT "The Complete Genome Sequence of the Plant Growth-Promoting Bacterium
RT Pseudomonas sp. UW4.";
RL PLoS ONE 8:E58640-E58640(2013).
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; CP003880; AFY21454.1; -; Genomic_DNA.
DR RefSeq; WP_015096576.1; NC_019670.1.
DR AlphaFoldDB; K9NNW7; -.
DR STRING; 1207075.PputUW4_04262; -.
DR KEGG; ppuu:PputUW4_04262; -.
DR PATRIC; fig|1207075.3.peg.4344; -.
DR eggNOG; COG0129; Bacteria.
DR HOGENOM; CLU_014271_1_2_6; -.
DR OrthoDB; 9807077at2; -.
DR UniPathway; UPA00226; -.
DR Proteomes; UP000010397; 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; 65157 MW; C4D2AE0CC05E4030 CRC64;
MHPRVLEVTE RLIARSRATR EAYLALIRGA ASDGPMRGKL QCANFAHGVA GCGSDDKNSL
RMMNAANIAI VSSYNDMLSA HQPYEVFPEL IKKALREIGS VGQFAGGTPA MCDGVTQGEP
GMELSLPSRE VIALSTAVAL SHNMFDGALL LGICDKIVPG LMMGALRFGH LPMIFVPGGP
MVSGISNKQK ADVRQKYAEG KATREELLES EMKSYHSPGT CTFYGTANTN QLLMEVMGLH
LPGASFVNPN TPLRDALTRE AAHQVTRLTK QNGDFMPIGE IVDERSLVNS IVALHATGGS
TNHTLHMPAI AMAAGIQLTW QDMADLSEVV PTLSHVYPNG KADINHFQAA GGMSFLIREL
LEAGLLHENV NTVMGHGLSR YTQEPFLDNG ELVWREGVTD SLDETILRPV ARAFSAEGGL
RVMEGNLGRG VMKVSAVAVE NQIVEAPAMV FQDQQDLADA FKAGLLEKDF VAVMRFQGPR
SNGMPELHKM TPFLGVLQDR GFKVALVTDG RMSGASGKIP AAIHVSPEAY VGGALARVQE
GDIIRVDGVK GTLELKVDAE EFAARTPAKG LLGNNIGTGR ELFGFMRMAF SSAEQGASAF
TSALETLN
//
