ID V5YWB7_SERMA Unreviewed; 604 AA.
AC V5YWB7;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 13-SEP-2023, entry version 28.
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:BAO21196.1};
OS Serratia marcescens.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Serratia.
OX NCBI_TaxID=615 {ECO:0000313|EMBL:BAO21196.1};
RN [1] {ECO:0000313|EMBL:BAO21196.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=IOMTU 115 {ECO:0000313|EMBL:BAO21196.1};
RA Tada T., Miyoshi-Akiyama T., Kirikae T.;
RT "Genetic environments surrounding aac(6')-Ial.";
RL Submitted (DEC-2013) 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}.
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DR EMBL; AB894481; BAO21196.1; -; Genomic_DNA.
DR AlphaFoldDB; V5YWB7; -.
DR UniPathway; UPA00226; -.
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 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 604 AA; 64282 MW; B4300765F6FEC3F1 CRC64;
MINPTLSRVT QRIIDRSQAS RAAYLARIEA ARAQTVHRAQ LACGNLAHGF AACQPDDKAS
LKNMVRSDIA IITAYNDMLS AHQPYEHYPQ RLKQALKAVG AVGQVAGGVP AMCDGVTQGQ
DGMELSLMSR DVIAMSAAVG LSHNMFDGAL FLGICDKIVP GLVMAALSFG HLPALFVPAG
PMSSGLPNKE KVRVRQLYAE GKADRLALLE AEAASYHGIG TCTFYGTANT NQMVMEVMGL
HLPGASFVHP DTPLRDALND AAARQVTRLT DTAGNYLPIG RLVDEKVVVN GIVSLLATGG
STNLTMHLVA MARAAGIIIT WDDFSELSEA VPLLCRIYPN GPADINQFQA AGGVPLVVRE
LLQHGLLHED VHTVAGFGLR RYTQEPWLDN DQLVWREGVA GSLDASVIAS VTQPFEHHGG
TKVMAGNLGR AVMKTSAVPA DNQIIEAPAV VFDSQHDIVP AFEAGKLDRD CVVVVRFQGP
QANGMPELHK LMPPLGVLMD RGFKVALVTD GRLSGASGKV PSAIHVTPEA YTGGLLAKVR
DGDPIRVNGR SGELQVLVDA DELARRTPCQ PDLSAEHIGC GRELFGALRS QLSGAEQGAC
CIKF
//