ID   KDSGA_PSEPU             Reviewed;         255 AA.
AC   P0DOV8;
DT   30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2016, sequence version 1.
DT   03-AUG-2022, entry version 12.
DE   RecName: Full=2-dehydro-3,6-dideoxy-6-sulfogluconate aldolase {ECO:0000305};
DE            EC=4.1.2.58 {ECO:0000269|PubMed:26195800};
DE   AltName: Full=2-keto-3,6-dideoxy-6-sulfogluconate aldolase {ECO:0000303|PubMed:26195800};
DE            Short=KDSG aldolase {ECO:0000303|PubMed:26195800};
GN   ORFNames=PpSQ1_00455 {ECO:0000312|EMBL:KHL76360.1};
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 retro-aldol cleavage of 2-dehydro-3,6-dideoxy-
CC       6-sulfo-D-gluconate to (2S)-3-sulfolactaldehyde and pyruvate. Is
CC       involved in a degradation pathway of sulfoquinovose (SQ) that allows
CC       P.putida SQ1 to use SQ as the sole carbon and energy source for growth.
CC       {ECO:0000269|PubMed:26195800}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-dehydro-3,6-dideoxy-6-sulfo-D-gluconate = (2S)-3-
CC         sulfolactaldehyde + pyruvate; Xref=Rhea:RHEA:47924,
CC         ChEBI:CHEBI:15361, ChEBI:CHEBI:88094, ChEBI:CHEBI:90109; EC=4.1.2.58;
CC         Evidence={ECO:0000269|PubMed:26195800};
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000250|UniProtKB:Q47098};
CC       Note=Binds 1 divalent metal cation per subunit.
CC       {ECO:0000250|UniProtKB:Q47098};
CC   -!- SUBUNIT: Homohexamer; trimer of dimers. {ECO:0000250|UniProtKB:Q47098}.
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 HpcH/HpaI aldolase family. {ECO:0000305}.
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DR   EMBL; JTCJ01000004; KHL76360.1; -; Genomic_DNA.
DR   AlphaFoldDB; P0DOV8; -.
DR   SMR; P0DOV8; -.
DR   BRENDA; 4.1.2.58; 5092.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.60; -; 1.
DR   InterPro; IPR005000; Aldolase/citrate-lyase_domain.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR   Pfam; PF03328; HpcH_HpaI; 1.
DR   SUPFAM; SSF51621; SSF51621; 1.
PE   1: Evidence at protein level;
KW   Lyase; Metal-binding.
FT   CHAIN           1..255
FT                   /note="2-dehydro-3,6-dideoxy-6-sulfogluconate aldolase"
FT                   /id="PRO_0000438493"
FT   ACT_SITE        38
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q47098"
FT   BINDING         141
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250|UniProtKB:Q47098"
FT   BINDING         167
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250|UniProtKB:Q47098"
FT   SITE            63
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250|UniProtKB:Q47098"
FT   SITE            77
FT                   /note="Increases basicity of active site His"
FT                   /evidence="ECO:0000250|UniProtKB:Q47098"
SQ   SEQUENCE   255 AA;  26927 MW;  D02B32D1B60380F0 CRC64;
     MLKRQSAPLG TWLMSASAST AEALGYAGFD WLLVDMEHVP IEFRDLWHIL QAIQCTGAQP
     IVRVAANDPV LLKRALDLGS TNVMVPFVEN AEQARAAVSA VKYPPMGTRG FAAVHRASRY
     GTWKGYGQQA NDSVSCILQI ETATALANLE EIAAVPGVDA LFLGPGDLSS VCGHIGNPAH
     PDIQAMISDA IVRCKAIGMP IGIVGGTPEL VGSYLEQGYA FAAVASDMAM MMSKANELLV
     ALKGRQAPEA VATAY