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Database: UniProt
Entry: D2YB67_VIBMI
LinkDB: D2YB67_VIBMI
Original site: D2YB67_VIBMI 
ID   D2YB67_VIBMI            Unreviewed;       598 AA.
AC   D2YB67;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   24-JAN-2024, entry version 38.
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=VMB_07640 {ECO:0000313|EMBL:EEW08021.1};
OS   Vibrio mimicus VM603.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=671074 {ECO:0000313|EMBL:EEW08021.1, ECO:0000313|Proteomes:UP000004827};
RN   [1] {ECO:0000313|EMBL:EEW08021.1, ECO:0000313|Proteomes:UP000004827}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VM603 {ECO:0000313|EMBL:EEW08021.1,
RC   ECO:0000313|Proteomes:UP000004827};
RX   PubMed=19860885; DOI=10.1186/1471-2148-9-258;
RA   Thompson C.C., Vicente A.C., Souza R.C., Vasconcelos A.T., Vesth T.,
RA   Alves N.Jr., Ussery D.W., Iida T., Thompson F.L.;
RT   "Genomic taxonomy of Vibrios.";
RL   BMC Evol. Biol. 9:258-258(2009).
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:EEW08021.1}.
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DR   EMBL; ACYU01000023; EEW08021.1; -; Genomic_DNA.
DR   RefSeq; WP_000581777.1; NZ_ACYU01000023.1.
DR   AlphaFoldDB; D2YB67; -.
DR   UniPathway; UPA00226; -.
DR   Proteomes; UP000004827; 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         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   598 AA;  63714 MW;  15D101C414A85F3C CRC64;
     MIHPVLAKVT QNLVERSREA RAAFIARSQA QEKAGKGRNS LSCGNLAHAV AASCSTEKKA
     ILDFTRSNVA IVTSYNDMLS AHQPYQHYPD RIKSVLAEYG HTAQVAGGVP AMCDGVTQGQ
     PGMDMSLFSR DLIAQATALS LSHNVFDATL LLGICDKIAP GQLMGALSYA HLPTAFMPAG
     LMATGISNEE KVDIRQKYAA GEVGKDALLN MECQAYHAPG TCTFYGTANT NQLVFEAMGL
     MLPGSAFVHP HSALRQALND AVTVKIASMT QGSAQYRPLY QVVTEQSLLN GIVALLASGG
     STNHTIHMLA VARAAGILLT WQDISDLSDV VPLLAKVYPN GPADMNAFQQ AGGVPALMKR
     LHEAKLLHAD VTPVFGEFSD QLSLPELVDG ELRWSPCEGT RDAQVIAASG ECFQTTGGTK
     VLSGNLGRAV IKVSAVKDDQ RIIEAPAVVF LCQHEVEAAY QRGELNKDCI VVVTHNGPAA
     NGMPELHKLM PILGNVQKAG FKVALVTDGR LSGASGKIPS AIHVSPEAVR GGAIGLVRDG
     DLIRLDCSTG TLENRTDMSH RQALALDTER DQQMWGRELF KVMRQAVSSA EQGASFIV
//
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