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Database: UniProt
Entry: A0A365UBB5_9RHOB
LinkDB: A0A365UBB5_9RHOB
Original site: A0A365UBB5_9RHOB 
ID   A0A365UBB5_9RHOB        Unreviewed;       600 AA.
AC   A0A365UBB5;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 21.
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   ORFNames=DRV85_03635 {ECO:0000313|EMBL:RBI86536.1};
OS   Rhodosalinus halophilus.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Rhodosalinus.
OX   NCBI_TaxID=2259333 {ECO:0000313|EMBL:RBI86536.1, ECO:0000313|Proteomes:UP000253370};
RN   [1] {ECO:0000313|EMBL:RBI86536.1, ECO:0000313|Proteomes:UP000253370}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E84 {ECO:0000313|EMBL:RBI86536.1,
RC   ECO:0000313|Proteomes:UP000253370};
RA   Liu Z.-W., Lu D.-C.;
RT   "Rhodosalinus sp. strain E84T genomic sequence and assembly.";
RL   Submitted (JUL-2018) 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}.
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:RBI86536.1}.
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DR   EMBL; QNTQ01000004; RBI86536.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A365UBB5; -.
DR   OrthoDB; 9807077at2; -.
DR   UniPathway; UPA00226; -.
DR   Proteomes; UP000253370; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000253370}.
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   600 AA;  62919 MW;  44F608B5626280C3 CRC64;
     MPLDATIARV TDTIMARSAD TRRDYLDRMR RAADEGPRRA HLSCSNQAHA YAASGPDKET
     LAGHRAPNLG IVTAYNDMLS AHQPFERFPD LIRAAARAAG GTAQVAGGVP AMCDGVTQGQ
     AGMELSLFSR DVIALAAGVA LSHNTFDAAA YLGVCDKIVP GLVIAAATFG HLPTVFIPAG
     PMTSGLPNDE KAKVRQQFAA GEVDREALMR AEMAAYHGPG TCTFYGTANS NQMLMEIMGL
     HLPGASFVNP GTPLRDALTA AAVERVLGLT RLGNAYTPAC DILDERAFVN GMVGLMATGG
     STNLVIHLPA MARAAGILLE PEDFDAVSSV TPLMARIYPN GLADVNHFHA AGGMAYLIGE
     LLEAGLLHAD VTTVAGPGLS RYTEEPKLQD GALSWQAGPR ESLNDRILRP HDDPFQPTGG
     LAQLTGNLGE GVIKISAVRP EHQAIEAPAR VFDDPAAVLA AFKAGQFTED CVIVLRFQGP
     RANGMPELHG LTPALSVLLD RGLKVALVTD GRMSGASGKV PAALHLSPEA AMGGALAMLQ
     DGDLIRLDAR AGTLETEADL GARSPATPDL SANRHGTGRE LFQLFRDRVG EARYGAASLV
//
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