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Database: UniProt
Entry: A0A063BLH4_9BURK
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ID   A0A063BLH4_9BURK        Unreviewed;       617 AA.
AC   A0A063BLH4;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   24-JAN-2024, entry version 33.
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=LIG30_0740 {ECO:0000313|EMBL:KDB10397.1};
OS   Burkholderia sp. lig30.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia.
OX   NCBI_TaxID=1192124 {ECO:0000313|EMBL:KDB10397.1, ECO:0000313|Proteomes:UP000027020};
RN   [1] {ECO:0000313|EMBL:KDB10397.1, ECO:0000313|Proteomes:UP000027020}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LIG30 {ECO:0000313|Proteomes:UP000027020};
RA   Woo H.L., Utturkar S.M., Klingeman D.M., Simmons B.A., DeAngelis K.M.,
RA   Brown S.D., Hazen T.C.;
RT   "Draft Genome of the Lignin-degrading Burkholderia sp. Strain LIG30,
RT   Isolated from Wet Tropical Forest Soil.";
RL   Submitted (MAR-2014) 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:KDB10397.1}.
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DR   EMBL; JGVW01000022; KDB10397.1; -; Genomic_DNA.
DR   RefSeq; WP_038709130.1; NZ_JGVW01000022.1.
DR   AlphaFoldDB; A0A063BLH4; -.
DR   STRING; 1192124.LIG30_0740; -.
DR   PATRIC; fig|1192124.4.peg.374; -.
DR   eggNOG; COG0129; Bacteria.
DR   OrthoDB; 9807077at2; -.
DR   UniPathway; UPA00226; -.
DR   Proteomes; UP000027020; 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:UP000027020}.
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   617 AA;  65057 MW;  67561A326AA40773 CRC64;
     MSSLHPTLAK VTARVIARSQ STRSAYLQRI DHAQGRFPAR GALSCANLAH GFAGLEGNDK
     LAIKAIRQPN IGIVSAYNEM LSAHAPYKDF PDIIKAAARG HGGVAQFAGG VPAMCDGITQ
     GNAGMELSLF SREVIAMSTA VALTHNMFDA ALCLGICDKI VPGLLIGALQ FGHLPTIFVP
     AGPMTSGLSN DDKAKIRQQF ATGQVGRDAL LEAESAAYHG HGTCTFYGTA NSNQMLMELM
     GLHLPGSAFV HPHTPLRDAL TAEAARRVLD LTVERGNYTP IGHVIDEKAI VNGIVALLAT
     GGSTNHTLHL VAIARAAGIL IDWDDFDELS AAVPLLAKIY PNGKADVNHF HAAGGIAFLV
     RNLLEGGLLH EDVTTVAGRG LSHYTKEPKL IDGKLTWVDG AAESHDANVL RGIREPFQPD
     GGLRLMQGRL GRGVIKISAV APEHRTVKAG AIVFDSQEAV QEAFDRGELK RDFVAVVRFQ
     GARANGMPEL HRLTPLLGVL QDQGFHVALV TDGRMSGASG KVPAVIHVSP EALLSGPLGK
     IRTGDTIVID AQAGVLDVEI DDAQWQAREV ALPLHQADNE AGFGRELFGV FRAAAAPAEQ
     GASVFGALAG EAARATV
//
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