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Database: UniProt
Entry: A0A0H5CYZ2_9PSEU
LinkDB: A0A0H5CYZ2_9PSEU
Original site: A0A0H5CYZ2_9PSEU 
ID   A0A0H5CYZ2_9PSEU        Unreviewed;       604 AA.
AC   A0A0H5CYZ2;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   24-JAN-2024, entry version 32.
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};
OS   Alloactinosynnema sp. L-07.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae.
OX   NCBI_TaxID=1653480 {ECO:0000313|EMBL:CRK57375.1, ECO:0000313|Proteomes:UP000076116};
RN   [1] {ECO:0000313|Proteomes:UP000076116}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L-07 {ECO:0000313|Proteomes:UP000076116};
RA   Ramaraj T.;
RL   Submitted (MAY-2015) 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; LN850107; CRK57375.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0H5CYZ2; -.
DR   STRING; 1653480.gene:80946236; -.
DR   KEGG; alo:CRK57375; -.
DR   OrthoDB; 9807077at2; -.
DR   UniPathway; UPA00226; -.
DR   Proteomes; UP000076116; Chromosome i.
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:UP000076116}.
FT   BINDING         154
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02094"
FT   BINDING         221
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02094"
SQ   SEQUENCE   604 AA;  62700 MW;  FD337BE2F274DE66 CRC64;
     MNRTLTAVTD RIIARSADSR GAYLERMRKA AATGPARSSL GCANLAHGFA ACSPGEKLGL
     RAAVKPNIAI VSSYNDMLSA HQPFAEYPNQ LKAAVAGAGG VAQFAGGVPA MCDGITQGRA
     GMELSLFSRD LIAMSTAIAL SHDMFDGMLL LGVCDKIVPG LVIGALAFGH LPAVLVPAGP
     MASGLPNAEK SRVRQLHAEG KIGREDLLAA ESASYHSAGT CTFYGTANSN QLLMEVMGLH
     LPGASFVNPG TPLREALTAE AGRRVTGLTA LGENYTPVGE VVDERAVVNG VVALLATGGS
     TNHTMHLVAM AAAAGIDLRW DDFSALSAIV PSLTRIYPNG TADVNHFHAA GGTATLIGDL
     LDSGLLHPDV RTVAGLYDER YREEPTFDDG VLVWRPGPRD SLDKTVLRGV SDPFAPDGGL
     RMLSGGLGRA VIKVSAVQPE HRVVRAPARV FDDQNEFLAA FEAGALSGDF VAVLRFQGPM
     ANGMPELHKL TPALGVLQDR GDKVALVTDG RMSGASGKVP AAIHLTPEAA AGGPLARVRD
     GDLIVVDAES GSVDILVDPL DFAARTPDQQ RCAVHTGTGR ELFAPLRAAV GPADRGASVF
     GVLS
//
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