ID A0A0S8ZS27_9PSED Unreviewed; 608 AA.
AC A0A0S8ZS27;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=ASE98_01590 {ECO:0000313|EMBL:KQN56149.1};
OS Pseudomonas sp. Leaf48.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1736221 {ECO:0000313|EMBL:KQN56149.1, ECO:0000313|Proteomes:UP000051774};
RN [1] {ECO:0000313|EMBL:KQN56149.1, ECO:0000313|Proteomes:UP000051774}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf48 {ECO:0000313|EMBL:KQN56149.1,
RC ECO:0000313|Proteomes:UP000051774};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQN56149.1, ECO:0000313|Proteomes:UP000051774}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf48 {ECO:0000313|EMBL:KQN56149.1,
RC ECO:0000313|Proteomes:UP000051774};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KQN56149.1}.
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DR EMBL; LMLH01000001; KQN56149.1; -; Genomic_DNA.
DR RefSeq; WP_060539674.1; NZ_LMLH01000001.1.
DR AlphaFoldDB; A0A0S8ZS27; -.
DR STRING; 1736221.ASE98_01590; -.
DR OrthoDB; 9807077at2; -.
DR UniPathway; UPA00226; -.
DR Proteomes; UP000051774; 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}.
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; 65211 MW; DEF2D4CC9A6E189B CRC64;
MHPRVLEVTE RLIARSRATR EAYLALIRGA ASDGPMRGKL QCANFAHGVA GCGTEDKNSL
RMMNSANIAI VSSYNDMLSA HQPYEVFPEQ IKKALREIGS VGQFAGGTPA MCDGVTQGEP
GMELSLPSRE VIALSTAVAL SHNMFDGALM LGICDKIVPG LMMGALRFGH LPTIFVPGGP
MVSGISNKQK ADVRQRYAEG KASREELLES EMKSYHSPGT CTFYGTANTN QLLMEVMGLH
LPGASFVNPN TPLRDALTRE AAHQVTRLTK QSGDFMPIGE IVDERSLVNS IVALHATGGS
TNHTLHMPAI AMAAGIQLTW QDMADLSEVV PTLSHVYPNG KADINHFQAA GGMSFLIREL
LEAGLLHENV NTVLGHGLSR YTKEPFLDNG ELVWREGPTE SLDESILRPV ARAFSPEGGL
RVMEGNLGRG VMKVSAVALE NQIVEAPAMV FQDQQDLADA FKAGLLEKDF VAVMRFQGPR
SNGMPELHKM TPFLGVLQDR GFKVALVTDG RMSGASGKIP AAIHVSPEAY VGGALARVQE
GDIIRVDGVK GTLELKVDAE EFAARTPAKG LLANNIGSGR ELFGFMRMAF SSAEQGASAF
TSALETLN
//
