EDD_RHIME
ID EDD_RHIME Reviewed; 606 AA.
AC Q9Z3S0;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Phosphogluconate dehydratase {ECO:0000255|HAMAP-Rule:MF_02094};
DE EC=4.2.1.12 {ECO:0000255|HAMAP-Rule:MF_02094};
GN Name=edd {ECO:0000255|HAMAP-Rule:MF_02094, ECO:0000303|PubMed:10400573};
GN OrderedLocusNames=R00702; ORFNames=SMc03068;
OS Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS meliloti).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=266834;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10400573; DOI=10.1128/jb.181.14.4176-4184.1999;
RA Willis L.B., Walker G.C.;
RT "A novel Sinorhizobium meliloti operon encodes an alpha-glucosidase and a
RT periplasmic-binding-protein-dependent transport system for alpha-
RT glucosides.";
RL J. Bacteriol. 181:4176-4184(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11481430; DOI=10.1073/pnas.161294398;
RA Capela D., Barloy-Hubler F., Gouzy J., Bothe G., Ampe F., Batut J.,
RA Boistard P., Becker A., Boutry M., Cadieu E., Dreano S., Gloux S.,
RA Godrie T., Goffeau A., Kahn D., Kiss E., Lelaure V., Masuy D., Pohl T.,
RA Portetelle D., Puehler A., Purnelle B., Ramsperger U., Renard C.,
RA Thebault P., Vandenbol M., Weidner S., Galibert F.;
RT "Analysis of the chromosome sequence of the legume symbiont Sinorhizobium
RT meliloti strain 1021.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11474104; DOI=10.1126/science.1060966;
RA Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F.,
RA Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G.,
RA Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P.,
RA Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S.,
RA Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I.,
RA Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S.,
RA Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C.,
RA Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R.,
RA Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H.,
RA Wong K., Yeh K.-C., Batut J.;
RT "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL Science 293:668-672(2001).
CC -!- FUNCTION: Catalyzes the dehydration of 6-phospho-D-gluconate to 2-
CC dehydro-3-deoxy-6-phospho-D-gluconate. {ECO:0000255|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:0000255|HAMAP-Rule:MF_02094};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02094};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000255|HAMAP-Rule:MF_02094};
CC -!- PATHWAY: Carbohydrate metabolism; Entner-Doudoroff pathway.
CC {ECO:0000255|HAMAP-Rule:MF_02094}.
CC -!- SIMILARITY: Belongs to the IlvD/Edd family. {ECO:0000255|HAMAP-
CC Rule:MF_02094, ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF045609; AAD12045.1; -; Genomic_DNA.
DR EMBL; AL591688; CAC45274.1; -; Genomic_DNA.
DR RefSeq; NP_384808.1; NC_003047.1.
DR RefSeq; WP_003527052.1; NC_003047.1.
DR AlphaFoldDB; Q9Z3S0; -.
DR SMR; Q9Z3S0; -.
DR STRING; 266834.SMc03068; -.
DR EnsemblBacteria; CAC45274; CAC45274; SMc03068.
DR GeneID; 61602169; -.
DR KEGG; sme:SMc03068; -.
DR PATRIC; fig|266834.11.peg.2078; -.
DR eggNOG; COG0129; Bacteria.
DR HOGENOM; CLU_014271_1_2_5; -.
DR OMA; CANIAHV; -.
DR UniPathway; UPA00226; -.
DR Proteomes; UP000001976; 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; -; 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 PANTHER; PTHR43661:SF1; PTHR43661:SF1; 1.
DR Pfam; PF00920; ILVD_EDD; 1.
DR SUPFAM; SSF143975; SSF143975; 1.
DR TIGRFAMs; TIGR01196; edd; 1.
DR PROSITE; PS00886; ILVD_EDD_1; 1.
DR PROSITE; PS00887; ILVD_EDD_2; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; Carbohydrate metabolism; Gluconate utilization; Iron; Iron-sulfur;
KW Lyase; Metal-binding; Reference proteome.
FT CHAIN 1..606
FT /note="Phosphogluconate dehydratase"
FT /id="PRO_0000103558"
FT BINDING 156
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02094"
FT BINDING 223
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02094"
SQ SEQUENCE 606 AA; 63924 MW; A81753F746D8A1BD CRC64;
MSADSRIAAI TARIVERSKP YREPYLDRVR SAATNGPHRT VLGCGNLAHG FAVCSPAEKV
ALAGDRVPNL GIITSYNDML SAHQPFETYP ALIREAAHEA GGVAQVAGGV PAMCDGVTQG
QPGMELSLFS RDVIAMAAGI GLSHNMFDAA VYLGVCDKIV PGLAIAALTF GHLPAVFIPA
GPMTTGLPND EKAKVRQLFA EGKVGRDELL EAESKSYHGP GTCTFYGTAN SNQMLMEIMG
FHLPGASFIN PGTPLRDALT REATKRALAI TALGNEFTPA GEMIDERSIV NGVVGLHATG
GSTNHTMHLV AMARAAGIVL TWQDISELSD LVPLLARVYP NGLADVNHFH AAGGMGFLIA
QLLRKGLLHD DVRTVYGQGL SAYAIDVKLG ENGSVKREPA PEASADPKVL ATVDRPFQHT
GGLKMLSGNI GKAVIKISAV KPESHVIEAP AKIFNDQAEL NAAFKAGKLE GDFVAVVRFQ
GPKANGMPEL HKLTTVLGIL QDRGQKVAIL TDGRMSGASG KVPAAIHVTP EAKEGGPIAR
IQEGDIVRID AINGKVEVLV EDIALKTRVP AHIDLSDNEF GMGRELFAPF RQIAGAADRG
GSVLFH
