ID   SGL_PSEPU               Reviewed;         291 AA.
AC   P0DOV6;
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=6-deoxy-6-sulfogluconolactonase {ECO:0000305};
DE            EC=3.1.1.99 {ECO:0000269|PubMed:26195800};
DE   AltName: Full=6-deoxy-6-sulfogluconolactone lactonase {ECO:0000303|PubMed:26195800};
DE            Short=SGL lactonase {ECO:0000303|PubMed:26195800};
GN   ORFNames=PpSQ1_00410 {ECO:0000312|EMBL:KHL76347.1};
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 hydrolysis of 6-deoxy-6-sulfo-D-glucono-1,5-
CC       lactone to form 6-deoxy-6-sulfo-D-gluconate. Is involved in a
CC       degradation pathway of sulfoquinovose (SQ) that allows P.putida SQ1 to
CC       use SQ as the sole carbon and energy source for growth.
CC       {ECO:0000269|PubMed:26195800}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=6-deoxy-6-sulfo-D-glucono-1,5-lactone + H2O = 6-deoxy-6-sulfo-
CC         D-gluconate + H(+); Xref=Rhea:RHEA:47908, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:88091, ChEBI:CHEBI:88093; EC=3.1.1.99;
CC         Evidence={ECO:0000269|PubMed:26195800};
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000250|UniProtKB:Q15493};
CC       Note=Binds 1 divalent metal cation per subunit.
CC       {ECO:0000250|UniProtKB:Q15493};
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 SMP-30/CGR1 family. {ECO:0000305}.
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DR   EMBL; JTCJ01000004; KHL76347.1; -; Genomic_DNA.
DR   RefSeq; WP_039601087.1; NZ_JTCJ01000004.1.
DR   AlphaFoldDB; P0DOV6; -.
DR   SMR; P0DOV6; -.
DR   PRIDE; P0DOV6; -.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 2.120.10.30; -; 1.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR013658; SGL.
DR   InterPro; IPR005511; SMP-30.
DR   Pfam; PF08450; SGL; 1.
DR   PRINTS; PR01790; SMP30FAMILY.
PE   1: Evidence at protein level;
KW   Hydrolase; Metal-binding.
FT   CHAIN           1..291
FT                   /note="6-deoxy-6-sulfogluconolactonase"
FT                   /id="PRO_0000438491"
FT   ACT_SITE        198
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q15493"
FT   BINDING         17
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250|UniProtKB:Q15493"
FT   BINDING         148
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250|UniProtKB:Q15493"
FT   BINDING         198
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250|UniProtKB:Q15493"
SQ   SEQUENCE   291 AA;  32226 MW;  24950AD9B8D166CA CRC64;
     MNETLKCVVR QPSVLGECPV WSVREQVLYW ADILAGRLHR LDPRDGSVST LQLPEELGCF
     GLREQGGFIV ALRSGIYLLD AHGQLGERLA ENPTGAEHSR FNDGRVDPWG RFWAGTLWQP
     RDRNGGQLLR VDAEHRAQVM AGDVMVSNGL AFSPDRAWAY HSDTPNHVLY RYPLDEDGQP
     GTRQLLREFA RGSGGRPDGA AFDSAGCYWS AQFDGGRVLR LSPDGQVLDE IQLPTRWPTM
     VAFGGEDLRT LYITSSRENR SAEELADWPL SGCVFATRVN VPGCAEPLFA G