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Database: UniProt
Entry: A0A2U2N622_9GAMM
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ID   A0A2U2N622_9GAMM        Unreviewed;       620 AA.
AC   A0A2U2N622;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 19.
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=DEM34_04860 {ECO:0000313|EMBL:PWG64661.1};
OS   Spiribacter halobius.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Spiribacter.
OX   NCBI_TaxID=2182432 {ECO:0000313|EMBL:PWG64661.1, ECO:0000313|Proteomes:UP000245474};
RN   [1] {ECO:0000313|EMBL:PWG64661.1, ECO:0000313|Proteomes:UP000245474}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E85 {ECO:0000313|EMBL:PWG64661.1,
RC   ECO:0000313|Proteomes:UP000245474};
RA   Zheng W.-S., Lu D.-C., Du Z.-J.;
RT   "Spiribacter halobius sp. nov., a moderately halophilic bacterium isolated
RT   from marine solar saltern.";
RL   Submitted (MAY-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:PWG64661.1}.
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DR   EMBL; QFFI01000005; PWG64661.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2U2N622; -.
DR   OrthoDB; 9807077at2; -.
DR   UniPathway; UPA00226; -.
DR   Proteomes; UP000245474; 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:UP000245474}.
FT   BINDING         157
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02094"
FT   BINDING         224
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02094"
SQ   SEQUENCE   620 AA;  65657 MW;  D055E0EA32E0B4A7 CRC64;
     MPPCHPVVAR VTERIEARSR PGREDYLRRL QAAADEGPVR RGLSCTNLAH AFAAAPEADK
     EALKALQRPN VAIVSAYNDM LSAHQPLERF PALLKQAVRE AGGTAQFAGG VPAMCDGVTQ
     GQPGMELSLF SRDVIAMATA VALSHNVFDA GLCLGVCDKI VPGLLIGALH FGHLPFIFVP
     GGPMTSGLPN EEKARIRAEF AEGRVGRDAL LESEAKSYHG PGTCTFYGTA NSNQMMMEVM
     GLHLPGAAFV NPNTPLRDAL TIAAGHRVMA LTARGETYTP VGRVVDERAL VNAIVGLLAT
     GGSTNHTIHL VAIARAAGIQ VTWDDFHELS SVVPLLTRIY PSGKADVNHF HAAGGMGFLV
     RELLDAGLLH EDVLTVAGEG LRRYAEEPWL HDGGVAWRAA PAASADPEVL RPVSEPFSAD
     GGLRVLDGNL GRAVIKVSAV KPEHRVVEAP ARVFEDQQQV LDAFRAGELD GDMVAVVRFQ
     GPRANGMPEL HKLTPELGVL LGRGHKVALV TDGRMSGASG KVPAAIHVTP ECLAGGPLGR
     VRDGDIIRVD AERGRLEALV PEAEWQAREG VAASAVSQHG MGRELFGLFR AAATGAEDGA
     RSFGLDADSL RTALDHERVG
//
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