ID A0A1B1ZU14_9PSEU Unreviewed; 616 AA.
AC A0A1B1ZU14;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
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=AFB00_26765 {ECO:0000313|EMBL:ANY09251.1};
OS Pseudonocardia sp. HH130630-07.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Pseudonocardia.
OX NCBI_TaxID=1690815 {ECO:0000313|EMBL:ANY09251.1, ECO:0000313|Proteomes:UP000092926};
RN [1] {ECO:0000313|EMBL:ANY09251.1, ECO:0000313|Proteomes:UP000092926}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HH130630-07 {ECO:0000313|EMBL:ANY09251.1,
RC ECO:0000313|Proteomes:UP000092926};
RA Oliw E.H.;
RL Submitted (JAN-2016) 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}.
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DR EMBL; CP013854; ANY09251.1; -; Genomic_DNA.
DR RefSeq; WP_068799465.1; NZ_CP013854.1.
DR AlphaFoldDB; A0A1B1ZU14; -.
DR STRING; 1690815.AFB00_26765; -.
DR KEGG; phh:AFB00_26765; -.
DR OrthoDB; 4744252at2; -.
DR UniPathway; UPA00226; -.
DR Proteomes; UP000092926; Chromosome.
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:UP000092926}.
FT BINDING 167
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02094"
FT BINDING 234
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02094"
SQ SEQUENCE 616 AA; 64198 MW; 8E17CA937CAFF5A4 CRC64;
MTTSAEHRPE LHPVVEEITR RVVARSATTR AAYLERVRSA AAAGPATGPA RDGLGCSNLA
HGVAACGPDK LTLSASPARN LAVVTAYNDM LSAHQPFETY PALIKQAARE AGGVAQVAGG
VPAMCDGITQ GRAGMELSLF SRDVIAMSTA VALSHDMFDA AVLLGVCDKI VPGLVMGALS
FGHLPVLLAP AGPMTSGLPN KEKARVRQLF AAGEAGRDEL LAAESQSYHG PGTCTFFGTA
NSNQLLMEIM GLHLPGSTFV NPGTGLRDAL TAETARRALA AAGDRSMAMG EIVDEKAVVN
GIVALLATGG STNHTMHLVA MAAAAGVRIT WDDFSDLSSV VPLLARIYPN GQADVNHFRA
AGGIQLLTRE LLSAGLLHDD VGTVDGPGLH RYTREPFLED GGLVWREGPE ESLDKSVLRG
VADPFAPEGG LRVLHGNLGR SVVKTSAVEP DHRYIEAPAV VVDDQDDLLA AYAAGELDGR
DLVAVVRYQG PRANGMPELH KLIPALGVLQ DRGQRVALVT DGRMSGASGK IPAALHVTPE
AARGGPLEKL RDGDVLRVDT LNGTLSVLVD ADEFDAREPV RRGGPSGPTF GAGRELFAAF
RAVVGPADEG AAVTFQ
//
