ID COMB_CLOB1 Reviewed; 239 AA. AC A7FPH4; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 11-SEP-2007, sequence version 1. DT 02-SEP-2026, entry version 86. 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}; GN OrderedLocusNames=CLB_3635; OS Clostridium botulinum (strain ATCC 19397 / Type A). OC Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales; Clostridiaceae; OC Clostridium; Clostridium botulinum group. OX NCBI_TaxID=441770; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 19397 / Type A; 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; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00490}; CC -!- SIMILARITY: Belongs to the ComB family. {ECO:0000255|HAMAP- CC Rule:MF_00490}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000726; ABS35102.1; -; Genomic_DNA. DR RefSeq; WP_012099545.1; NC_009697.1. DR AlphaFoldDB; A7FPH4; -. DR SMR; A7FPH4; -. DR GeneID; 5187232; -. DR KEGG; cba:CLB_3635; -. DR HOGENOM; CLU_070028_0_0_9; -. DR GO; GO:0050532; F:2-phosphosulfolactate phosphatase activity; IEA:UniProtKB-UniRule. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0050545; F:sulfopyruvate decarboxylase activity; IEA:TreeGrafter. DR FunFam; 3.90.1560.10:FF:000001; Probable 2-phosphosulfolactate phosphatase; 1. DR Gene3D; 3.90.1560.10; ComB-like; 1. DR HAMAP; MF_00490; ComB; 1. DR InterPro; IPR005238; ComB-like. DR InterPro; IPR036702; ComB-like_sf. DR NCBIfam; NF002052; PRK00886.1-1; 1. DR NCBIfam; NF002055; PRK00886.1-4; 1. DR PANTHER; PTHR37311; 2-PHOSPHOSULFOLACTATE PHOSPHATASE-RELATED; 1. DR PANTHER; PTHR37311:SF1; 2-PHOSPHOSULFOLACTATE PHOSPHATASE-RELATED; 1. DR Pfam; PF04029; 2-ph_phosp; 1. DR SUPFAM; SSF142823; ComB-like; 1. PE 3: Inferred from homology; KW Hydrolase; Magnesium. FT CHAIN 1..239 FT /note="Probable 2-phosphosulfolactate phosphatase" FT /id="PRO_1000014460" SQ SEQUENCE 239 AA; 26658 MW; 0BF3B8F51CF732B0 CRC64; MNIDIVISAD HIDEKGLINK TVIIIDILRA TSVITTAINN GCKKVIPVLT VEEAKDIAKN SEEDIILGGE RNALKIDGFN FSNSPLEYTK KYVEGKTVVL STTNGTRAIN NSFNAKTILI SALINSKATA KAIDKLHEDL IIINSGTNGQ FSIDDFICSG YLIDCLYNIR KDLELSDIAK TAHYIYTNNK DIESFVKKAT HYSRLKSLNL EKDLEYCFQK DIIDVVPQYK DGYIIKSNI //