ID   SGD_PSEPU               Reviewed;         579 AA.
AC   P0DOV7;
DT   30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2016, sequence version 1.
DT   03-AUG-2022, entry version 13.
DE   RecName: Full=6-deoxy-6-sulfo-D-gluconate dehydratase {ECO:0000305};
DE            Short=SG dehydratase {ECO:0000303|PubMed:26195800};
DE            EC=4.2.1.162 {ECO:0000269|PubMed:26195800};
GN   ORFNames=PpSQ1_00400 {ECO:0000312|EMBL:KHL76345.1};
OS   Pseudomonas putida (Arthrobacter siderocapsulatus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=303;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SQ1;
RX   PubMed=27408681; DOI=10.1186/s40793-015-0033-x;
RA   Felux A.K., Franchini P., Schleheck D.;
RT   "Permanent draft genome sequence of sulfoquinovose-degrading Pseudomonas
RT   putida strain SQ1.";
RL   Stand. Genomic Sci. 10:42-42(2015).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND INDUCTION.
RC   STRAIN=SQ1;
RX   PubMed=26195800; DOI=10.1073/pnas.1507049112;
RA   Felux A.K., Spiteller D., Klebensberger J., Schleheck D.;
RT   "Entner-Doudoroff pathway for sulfoquinovose degradation in Pseudomonas
RT   putida SQ1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 112:E4298-E4305(2015).
CC   -!- FUNCTION: Catalyzes the dehydration of 6-deoxy-6-sulfo-D-gluconate to
CC       2-dehydro-3,6-dideoxy-6-sulfo-D-gluconate. Is involved in a degradation
CC       pathway of sulfoquinovose (SQ) that allows P.putida SQ1 to use SQ as
CC       the sole carbon and energy source for growth.
CC       {ECO:0000269|PubMed:26195800}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=6-deoxy-6-sulfo-D-gluconate = 2-dehydro-3,6-dideoxy-6-sulfo-D-
CC         gluconate + H2O; Xref=Rhea:RHEA:47912, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:88093, ChEBI:CHEBI:88094; EC=4.2.1.162;
CC         Evidence={ECO:0000269|PubMed:26195800};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000250|UniProtKB:Q1JUQ1};
CC       Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250|UniProtKB:Q1JUQ1};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q1JUQ1}.
CC   -!- INDUCTION: Is highly up-regulated during growth on sulfoquinovose,
CC       compared to growth on glucose or succinate (at protein level).
CC       {ECO:0000269|PubMed:26195800}.
CC   -!- SIMILARITY: Belongs to the IlvD/Edd family. {ECO:0000305}.
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DR   EMBL; JTCJ01000004; KHL76345.1; -; Genomic_DNA.
DR   RefSeq; WP_039601085.1; NZ_JTCJ01000004.1.
DR   AlphaFoldDB; P0DOV7; -.
DR   SMR; P0DOV7; -.
DR   GO; GO:0016836; F:hydro-lyase activity; IEA:InterPro.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:UniProt.
DR   GO; GO:0044238; P:primary metabolic process; IEA:UniProt.
DR   Gene3D; 3.50.30.80; -; 1.
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   Pfam; PF00920; ILVD_EDD; 1.
DR   SUPFAM; SSF143975; SSF143975; 1.
DR   PROSITE; PS00886; ILVD_EDD_1; 1.
PE   1: Evidence at protein level;
KW   Iron; Iron-sulfur; Lyase; Metal-binding.
FT   CHAIN           1..579
FT                   /note="6-deoxy-6-sulfo-D-gluconate dehydratase"
FT                   /id="PRO_0000438492"
FT   BINDING         59
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:Q1JUQ1"
FT   BINDING         127
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:Q1JUQ1"
FT   BINDING         200
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:Q1JUQ1"
SQ   SEQUENCE   579 AA;  62544 MW;  E85EF176DEEBD4F2 CRC64;
     MSEKHKKIEE LRSQRWFAPD TIRAFAHRQR LQQIGLRREE FMGKPVIAIL NTWSEMSPCH
     SHLRDRAEAV KRGVWAAGGF PVELPVQSVG EVMVKPTTML YRNLLAMEAE ELLRSLPIDG
     AVLLGGCDKS TPGLLMGALS MDLPVIYCPA GPMSNGQWRG VKTGAGTHTK KYWDERRLGL
     IDTVAWEELE GAMTRSIGTC NTVGTASTMT SIADAMGFTL PGASSIPAAD GAHPRMASQC
     GSAIVDLVWR DRRPSTWLTD KHVANGVAVY MAMGGSTNAA IHLIAIARRA GIDLTLDQLA
     AAAAKIPVLL NLFPSGTALM EDYHFAGGLR ALMRKIEPHL HLECEGATGQ SWDSLLADAP
     CYDDDIIRSL DNPVVSLEQG ATLALLRGNL CPDGAVMKSS AAEPRLRRHS GPALVFDDHE
     TLSRMIDDPA LEVTADTVLI LRNAGPVGAP GMPEWGNLPI PKRLLEAGVR DLLRISDSRM
     SGTHYGSCVL HVAPEAAVGG PLALVRTGDI IDLDVAAGTL NMRVSDDELA RRRAGHVPQH
     KTYGRSFAAL YQQHVTQANE GCDFDFLQAG EAVPEPPIH