ID   COMB_CLOBK              Reviewed;         239 AA.
AC   B1IH09;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 67.
DE   RecName: Full=Probable 2-phosphosulfolactate phosphatase {ECO:0000255|HAMAP-Rule:MF_00490};
DE            EC=3.1.3.71 {ECO:0000255|HAMAP-Rule:MF_00490};
GN   Name=comB {ECO:0000255|HAMAP-Rule:MF_00490}; OrderedLocusNames=CLD_0930;
OS   Clostridium botulinum (strain Okra / Type B1).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=498213;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Okra / Type B1;
RX   PubMed=18060065; DOI=10.1371/journal.pone.0001271;
RA   Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C.,
RA   Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.;
RT   "Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4
RT   and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within
RT   plasmids.";
RL   PLoS ONE 2:E1271-E1271(2007).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R)-O-phospho-3-sulfolactate + H2O = (2R)-3-sulfolactate +
CC         phosphate; Xref=Rhea:RHEA:23416, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15597, ChEBI:CHEBI:43474, ChEBI:CHEBI:58738; EC=3.1.3.71;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00490};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00490};
CC   -!- SIMILARITY: Belongs to the ComB family. {ECO:0000255|HAMAP-
CC       Rule:MF_00490}.
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DR   EMBL; CP000939; ACA46797.1; -; Genomic_DNA.
DR   RefSeq; WP_015958152.1; NC_010516.1.
DR   AlphaFoldDB; B1IH09; -.
DR   SMR; B1IH09; -.
DR   EnsemblBacteria; ACA46797; ACA46797; CLD_0930.
DR   KEGG; cbb:CLD_0930; -.
DR   HOGENOM; CLU_070028_0_0_9; -.
DR   OMA; RLFMSTT; -.
DR   Proteomes; UP000008541; Chromosome.
DR   GO; GO:0050532; F:2-phosphosulfolactate phosphatase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.90.1560.10; -; 1.
DR   HAMAP; MF_00490; ComB; 1.
DR   InterPro; IPR005238; ComB-like.
DR   InterPro; IPR036702; ComB-like_sf.
DR   PANTHER; PTHR37311; PTHR37311; 1.
DR   Pfam; PF04029; 2-ph_phosp; 1.
DR   SUPFAM; SSF142823; SSF142823; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Magnesium.
FT   CHAIN           1..239
FT                   /note="Probable 2-phosphosulfolactate phosphatase"
FT                   /id="PRO_1000126224"
SQ   SEQUENCE   239 AA;  26749 MW;  5B609E7FD720CF54 CRC64;
     MNIDIVISAD HIDEKRLINK TVIIIDILRA TSVITTAINN GCKKVIPVLT VEEAKDIAKN
     SKEDIILGGE RNALKIDGFN FSNSPLEYTK NYVEGKTVVL STTNGTRAIN NSFNAKTILI
     SALINSKATA KAIDKLNEDL IIINSGTNGQ FSIDDFICSG YLIDCLYNIR KDLELSDIAK
     TAHYIYMNNK DIESFVKKAT HYSRLKSLNL EKDLEYCFQK DIIDVVPQYK DGYIIKSNI