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Database: UniProt
Entry: U5T614_9GAMM
LinkDB: U5T614_9GAMM
Original site: U5T614_9GAMM 
ID   U5T614_9GAMM            Unreviewed;       611 AA.
AC   U5T614;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   24-JAN-2024, entry version 44.
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=SPICUR_03880 {ECO:0000313|EMBL:AGY91763.1};
OS   Spiribacter curvatus.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Spiribacter.
OX   NCBI_TaxID=1335757 {ECO:0000313|EMBL:AGY91763.1, ECO:0000313|Proteomes:UP000017640};
RN   [1] {ECO:0000313|EMBL:AGY91763.1, ECO:0000313|Proteomes:UP000017640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAH-SP71 {ECO:0000313|EMBL:AGY91763.1,
RC   ECO:0000313|Proteomes:UP000017640};
RX   PubMed=24225341; DOI=10.1186/1471-2164-14-787;
RA   Lopez-Perez M., Ghai R., Leon M.J., Rodriguez-Olmos A., Copa-Patino J.L.,
RA   Soliveri J., Sanchez-Porro C., Ventosa A., Rodriguez-Valera F.;
RT   "Genomes of "Spiribacter", a streamlined, successful halophilic
RT   bacterium.";
RL   BMC Genomics 14:787-787(2013).
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; CP005990; AGY91763.1; -; Genomic_DNA.
DR   RefSeq; WP_023366242.1; NC_022664.1.
DR   AlphaFoldDB; U5T614; -.
DR   STRING; 1335757.SPICUR_03880; -.
DR   KEGG; spiu:SPICUR_03880; -.
DR   PATRIC; fig|1335757.3.peg.759; -.
DR   eggNOG; COG0129; Bacteria.
DR   HOGENOM; CLU_014271_1_2_6; -.
DR   OrthoDB; 9807077at2; -.
DR   UniPathway; UPA00226; -.
DR   Proteomes; UP000017640; 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:UP000017640}.
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   611 AA;  64164 MW;  C9737AEF85C8E46B CRC64;
     MPALNTAVAA VTRRIEARSE SDRAAYLDRL QAAADAGPVR TGLSCTNLAH AFAAAPDGDK
     ARLKGLEQAN VGIVSAYNDM LSAHQPLERF PGLLKQAVRE AGGTAQFAGG VPAMCDGVTQ
     GQPGMELSLF SRDVIAMATG VALSHNTFDA GLCLGVCDKI VPGLLIGALH FGHLPFIFVP
     AGPMTSGMPN DEKARIRGLY AEGKVGRDAL LESETQSYHG PGTCTFYGTA NSNQMLMEVM
     GLHLPGAAFV NPNTPLRDAL TIAAGHRVSR ITARGDEYTP VGRVIDARAI VNGIVGLLAT
     GGSTNHTIHM VAIARAAGLH VDWSDFDTLS RVVPLLTRIY PNGQADVNHF HAAGGMGFLI
     RELLDAGLLH EDVMTVAGEG LRAYAREPML AEGGVGWQEA PTQSADQSVV RPVAEPFDAD
     GGLRVLDGNL GRAVIKTSAV RPDHRRIEAP ARVFNDQQAV LAAFRAGELE GDFVCVVRGQ
     GPRANGMPEL HKLTPELGVL QSRGQRVALV TDGRMSGASG KVPAAIHLHP EGASGGAISC
     IRDGDLICLD ADAGTLEARV PEAEWTAREV EPIDNAVQHG IGREMFAGFR AMASSAESGA
     ITFYPVTATE A
//
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