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Database: UniProt
Entry: A0A1Y2N8D3_PSEAH
LinkDB: A0A1Y2N8D3_PSEAH
Original site: A0A1Y2N8D3_PSEAH 
ID   A0A1Y2N8D3_PSEAH        Unreviewed;       613 AA.
AC   A0A1Y2N8D3;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
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   ECO:0000313|EMBL:OSY43188.1};
GN   ORFNames=BG845_00793 {ECO:0000313|EMBL:OSY43188.1};
OS   Pseudonocardia autotrophica (Amycolata autotrophica) (Nocardia
OS   autotrophica).
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Pseudonocardia.
OX   NCBI_TaxID=2074 {ECO:0000313|EMBL:OSY43188.1, ECO:0000313|Proteomes:UP000194360};
RN   [1] {ECO:0000313|EMBL:OSY43188.1, ECO:0000313|Proteomes:UP000194360}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 535 {ECO:0000313|EMBL:OSY43188.1,
RC   ECO:0000313|Proteomes:UP000194360};
RA   Grumaz C., Vainshtein Y., Kirstahler P., Sohn K.;
RT   "Pseudonocardia autotrophica DSM535, a candidate organism with high
RT   potential of specific P450 cytochromes.";
RL   Submitted (SEP-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}.
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:OSY43188.1}.
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DR   EMBL; MIGB01000003; OSY43188.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2N8D3; -.
DR   STRING; 2074.BG845_00793; -.
DR   OrthoDB; 4744252at2; -.
DR   UniPathway; UPA00226; -.
DR   Proteomes; UP000194360; 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.
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:UP000194360}.
FT   BINDING         162
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02094"
FT   BINDING         229
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02094"
SQ   SEQUENCE   613 AA;  64391 MW;  50E1C97B6976DFE8 CRC64;
     MTVIPELHPV LDQVTRRVIA RSATTRSAYL QRIRAARPPA MAGPGRESLG CANLAHGAAA
     CGPDKLTLTA TPARNLAIVT AYNDMLSAHQ PFEGYPELIR AAAREAGGVA QVAGGVPAMC
     DGITQGRAGM ELSLFSRDVI AMSTAVALSH DMFDAAVLLG VCDKIVPGLV MGALSFGHLP
     VLLAPAGPMP SGLPNKEKAR IRQAYAAGEV GRDELLEAES RSYHGPGTCT FFGTANSNQL
     LMEIMGLHLP GSSFVNPGTP LRAALTAETA RRALAAADDP DRAMGEIIDE RAVLNGIVAL
     LATGGSTNHT MHLVAMAGAA GVRITWDDFS DLSAVVPLLA RIYPNGQADV NHFQAAGGVS
     LLVRELLQAG LLHDEVRTVD GPGLHRYTRE PFLDGPELVW REGPTESLDK SVLRGVGDPF
     SPDGGLRVLH GNLGRSVVKT SAVEPDHRFV EAPAVVFDHQ DELLDAYRAG ELDARDFVAV
     VRYQGPRANG MPELHKLTPA LGVLQDRGQR VAVVTDGRMS GASGKVPAAL HVTPEAARGG
     PLEKVRDGDP IRLDTLNGTL SLLVDADEFD AREPARRTIP SGPTFGTGRE LFGVFRAAVG
     PADEGAVIAG PGS
//
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