ID A0A0H3CB86_CAUVN Unreviewed; 602 AA.
AC A0A0H3CB86;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-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 ECO:0000313|EMBL:ACL95599.1};
GN OrderedLocusNames=CCNA_02134 {ECO:0000313|EMBL:ACL95599.1};
OS Caulobacter vibrioides (strain NA1000 / CB15N) (Caulobacter crescentus).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=565050 {ECO:0000313|EMBL:ACL95599.1, ECO:0000313|Proteomes:UP000001364};
RN [1] {ECO:0000313|EMBL:ACL95599.1, ECO:0000313|Proteomes:UP000001364}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NA1000 / CB15N {ECO:0000313|Proteomes:UP000001364};
RX PubMed=20472802; DOI=10.1128/JB.00255-10;
RA Marks M.E., Castro-Rojas C.M., Teiling C., Du L., Kapatral V.,
RA Walunas T.L., Crosson S.;
RT "The genetic basis of laboratory adaptation in Caulobacter crescentus.";
RL J. Bacteriol. 192:3678-3688(2010).
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; CP001340; ACL95599.1; -; Genomic_DNA.
DR RefSeq; WP_010919918.1; NC_011916.1.
DR RefSeq; YP_002517507.1; NC_011916.1.
DR AlphaFoldDB; A0A0H3CB86; -.
DR SMR; A0A0H3CB86; -.
DR GeneID; 7330440; -.
DR KEGG; ccs:CCNA_02134; -.
DR PATRIC; fig|565050.3.peg.2092; -.
DR HOGENOM; CLU_014271_1_2_5; -.
DR OrthoDB; 9807077at2; -.
DR PhylomeDB; A0A0H3CB86; -.
DR UniPathway; UPA00226; -.
DR Proteomes; UP000001364; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000001364}.
FT BINDING 156
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02094"
FT BINDING 223
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02094"
SQ SEQUENCE 602 AA; 63186 MW; 4387C546F2FC5FD9 CRC64;
MSLNPVIADV TARIVARSKD SRAAYLANMD RAIENQPGRA KLSCANWAHA FAASPGVDKL
RALDPNAPNI GIVSAYNDML SAHQPLEAYP ALIKDAARDV GATAQFAGGV PAMCDGVTQG
RPGMELSLFS RDVIAMATAV ALTHDAFDSA LYLGVCDKIV PGLVIGALTF SHLPALFVPA
GPMTSGLPNS EKARIRALYA EGKVGREELL AAESASYHGP GTCTFYGTAN TNQMLMELMG
FHLPGSAFVH PNTPLREALV KESARRVAAV TNKGNEFIPV GRMIDEKSFV NGVVGLMATG
GSTNLALHII AMAAAAGVQL TLEDLDDISK ATPLLARVYP NGSADVNHFQ AAGGMAFVIR
ELLKAGLVHE DVQTIAGAGL SLYAKEPVLE DGMLTWRDGA HESLDPAIVR PVSDPFSKEG
GLRLMAGNLG RGVMKISAVK PEHHVIEAPC AVFQEQEDFI AAFKRGELDR DVVVVVRFQG
PSANGMPELH NLSPSISVLL DRGHKVALVT DGRMSGASGK TPAAIHVTPE AAKGGPLAYV
QDGDVIRVNA ETGELKIMVD EATLLARTPA NVPASKPGFG RELFGWMRSG VGAADAGASV
FA
//
