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Database: UniProt
Entry: J2JGL5_9NOCA
LinkDB: J2JGL5_9NOCA
Original site: J2JGL5_9NOCA 
ID   J2JGL5_9NOCA            Unreviewed;       617 AA.
AC   J2JGL5;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 35.
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:EJI99332.1};
GN   ORFNames=JVH1_2940 {ECO:0000313|EMBL:EJI99332.1};
OS   Rhodococcus sp. JVH1.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=745408 {ECO:0000313|EMBL:EJI99332.1, ECO:0000313|Proteomes:UP000009024};
RN   [1] {ECO:0000313|EMBL:EJI99332.1, ECO:0000313|Proteomes:UP000009024}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JVH1 {ECO:0000313|EMBL:EJI99332.1,
RC   ECO:0000313|Proteomes:UP000009024};
RX   PubMed=22965106; DOI=10.1128/JB.01066-12;
RA   Brooks S.L., Van Hamme J.D.;
RT   "Whole-Genome Shotgun Sequence of Rhodococcus Species Strain JVH1.";
RL   J. Bacteriol. 194:5492-5493(2012).
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:EJI99332.1}.
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DR   EMBL; AKKP01000046; EJI99332.1; -; Genomic_DNA.
DR   RefSeq; WP_009475031.1; NZ_AKKP01000046.1.
DR   AlphaFoldDB; J2JGL5; -.
DR   PATRIC; fig|745408.3.peg.2788; -.
DR   UniPathway; UPA00226; -.
DR   Proteomes; UP000009024; 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         164
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02094"
FT   BINDING         231
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02094"
SQ   SEQUENCE   617 AA;  64590 MW;  4064FB52CE35A449 CRC64;
     MTDAPTPTAD VHPVLAAVTE RIIERSKPER TVYLNRIRAA GDRGPARGKL ACANLAHGFA
     ASGPADKKAL RSFVKPNIAI VSSYNDMLSA HQPFEHFPRQ LKAAVMEAGG IAQFAGGVPA
     MCDGITQGRD GMQLSLFSRD VIAMATAIGL SHDMFDGALM LGVCDKIVPG MLIGALGFGH
     LPTIFVPAGP MTSGLPNNEK SRVRQLYAEG KAEREELLDA EAASYHGAGT CTFFGTANSN
     QLLMEVMGLH LPGSSFVNPG TPLRDALTSE AGRRVTGLTA LGEEYTPVGE VVDEKAVVNG
     CVALLATGGS TNHTMHLVAI ARAAGITLTW DDLSELSAVV PLLARIYPNG SADVNHFHAA
     GGLGYVVSSM LDAGLLHEDV KTVVGPGLRR YTEEPKLSGE GVEWQPGTRI SLDTNVLRGP
     EDPFDVNGGL KMLTGNLGSC VMKTSAVHPD HRVVTAPAKV FDDQLDFLAA FEAGTLTGDF
     VAVLRYQGPR ANGMPELHKL TPVLGVLQDQ GRKVALVTDG RMSGASGKVP AAIHLTPEAA
     ADGLLARVRD GDVLTVDAVT GSVNVHLDDE ELAARPATGR ALGADEWVGT GRELFAGLRA
     AVGPATQGAS VFHPQPV
//
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