EDD_ZYMMO
ID EDD_ZYMMO Reviewed; 607 AA.
AC P21909; Q5NQL2;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 2.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Phosphogluconate dehydratase {ECO:0000255|HAMAP-Rule:MF_02094};
DE EC=4.2.1.12 {ECO:0000255|HAMAP-Rule:MF_02094, ECO:0000269|PubMed:2254282};
DE AltName: Full=6-phosphogluconate dehydratase {ECO:0000303|PubMed:2254282};
GN Name=edd {ECO:0000255|HAMAP-Rule:MF_02094, ECO:0000303|PubMed:2254282};
GN OrderedLocusNames=ZMO0368;
OS Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC Zymomonadaceae; Zymomonas.
OX NCBI_TaxID=264203;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP PATHWAY.
RC STRAIN=ATCC 31821 / ZM4 / CP4;
RX PubMed=2254282; DOI=10.1128/jb.172.12.7227-7240.1990;
RA Barnell W.O., Yi K.C., Conway T.;
RT "Sequence and genetic organization of a Zymomonas mobilis gene cluster that
RT encodes several enzymes of glucose metabolism.";
RL J. Bacteriol. 172:7227-7240(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 31821 / ZM4 / CP4;
RA Ahn J.Y., Kang H.S.;
RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31821 / ZM4 / CP4;
RX PubMed=15592456; DOI=10.1038/nbt1045;
RA Seo J.-S., Chong H., Park H.S., Yoon K.-O., Jung C., Kim J.J., Hong J.H.,
RA Kim H., Kim J.-H., Kil J.-I., Park C.J., Oh H.-M., Lee J.-S., Jin S.-J.,
RA Um H.-W., Lee H.-J., Oh S.-J., Kim J.Y., Kang H.L., Lee S.Y., Lee K.J.,
RA Kang H.S.;
RT "The genome sequence of the ethanologenic bacterium Zymomonas mobilis
RT ZM4.";
RL Nat. Biotechnol. 23:63-68(2005).
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, ECO:0000269|PubMed:2254282}.
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 ECO:0000269|PubMed:2254282};
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, ECO:0000305|PubMed:2254282}.
CC -!- SIMILARITY: Belongs to the IlvD/Edd family. {ECO:0000255|HAMAP-
CC Rule:MF_02094, ECO:0000305}.
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DR EMBL; M60615; AAA27693.1; -; Genomic_DNA.
DR EMBL; AF313764; AAG29866.1; -; Genomic_DNA.
DR EMBL; AE008692; AAV88992.1; -; Genomic_DNA.
DR PIR; C37855; C37855.
DR RefSeq; WP_011240289.1; NZ_CP035711.1.
DR AlphaFoldDB; P21909; -.
DR SMR; P21909; -.
DR STRING; 264203.ZMO0368; -.
DR EnsemblBacteria; AAV88992; AAV88992; ZMO0368.
DR GeneID; 58026217; -.
DR KEGG; zmo:ZMO0368; -.
DR eggNOG; COG0129; Bacteria.
DR HOGENOM; CLU_014271_1_2_5; -.
DR OMA; CANIAHV; -.
DR OrthoDB; 193579at2; -.
DR UniPathway; UPA00226; -.
DR Proteomes; UP000001173; 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 1: Evidence at protein level;
KW 4Fe-4S; Carbohydrate metabolism; Gluconate utilization; Iron; Iron-sulfur;
KW Lyase; Metal-binding; Reference proteome.
FT CHAIN 1..607
FT /note="Phosphogluconate dehydratase"
FT /id="PRO_0000103559"
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"
FT CONFLICT 580..607
FT /note="GRELFDIFRQNAAKAEDGAVAIYAGAGI -> ARIV (in Ref. 1 and
FT 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 607 AA; 65392 MW; 5CFBA00D332C4A18 CRC64;
MTDLHSTVEK VTARVIERSR ETRKAYLDLI QYEREKGVDR PNLSCSNLAH GFAAMNGDKP
ALRDFNRMNI GVVTSYNDML SAHEPYYRYP EQMKVFAREV GATVQVAGGV PAMCDGVTQG
QPGMEESLFS RDVIALATSV SLSHGMFEGA ALLGICDKIV PGLLMGALRF GHLPTILVPS
GPMTTGIPNK EKIRIRQLYA QGKIGQKELL DMEAACYHAE GTCTFYGTAN TNQMVMEVLG
LHMPGSAFVT PGTPLRQALT RAAVHRVAEL GWKGDDYRPL GKIIDEKSIV NAIVGLLATG
GSTNHTMHIP AIARAAGVIV NWNDFHDLSE VVPLIARIYP NGPRDINEFQ NAGGMAYVIK
ELLSANLLNR DVTTIAKGGI EEYAKAPALN DAGELVWKPA GEPGDDTILR PVSNPFAKDG
GLRLLEGNLG RAMYKASAVD PKFWTIEAPV RVFSDQDDVQ KAFKAGELNK DVIVVVRFQG
PRANGMPELH KLTPALGVLQ DNGYKVALVT DGRMSGATGK VPVALHVSPE ALGGGAIGKL
RDGDIVRISV EEGKLEALVP ADEWNARPHA EKPAFRPGTG RELFDIFRQN AAKAEDGAVA
IYAGAGI
