ID   COMB_METTH              Reviewed;         226 AA.
AC   O27250;
DT   05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 116.
DE   RecName: Full=2-phosphosulfolactate phosphatase;
DE            EC=3.1.3.71;
GN   Name=comB; OrderedLocusNames=MTH_1182;
OS   Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS   10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX   NCBI_TaxID=187420;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX   PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA   Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA   Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA   Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA   Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA   Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA   Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA   Reeve J.N.;
RT   "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT   functional analysis and comparative genomics.";
RL   J. Bacteriol. 179:7135-7155(1997).
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- PATHWAY: Cofactor biosynthesis; coenzyme M biosynthesis;
CC       sulfoacetaldehyde from phosphoenolpyruvate and sulfite: step 2/4.
CC   -!- SIMILARITY: Belongs to the ComB family. {ECO:0000305}.
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DR   EMBL; AE000666; AAB85671.1; -; Genomic_DNA.
DR   PIR; F69024; F69024.
DR   AlphaFoldDB; O27250; -.
DR   SMR; O27250; -.
DR   STRING; 187420.MTH_1182; -.
DR   EnsemblBacteria; AAB85671; AAB85671; MTH_1182.
DR   KEGG; mth:MTH_1182; -.
DR   PATRIC; fig|187420.15.peg.1160; -.
DR   HOGENOM; CLU_070028_0_0_2; -.
DR   OMA; RLFMSTT; -.
DR   UniPathway; UPA00355; UER00470.
DR   Proteomes; UP000005223; 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   GO; GO:0019295; P:coenzyme M biosynthetic process; 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   InterPro; IPR027639; ComB_archaeal.
DR   PANTHER; PTHR37311; PTHR37311; 1.
DR   Pfam; PF04029; 2-ph_phosp; 1.
DR   SUPFAM; SSF142823; SSF142823; 1.
DR   TIGRFAMs; TIGR00298; TIGR00298; 1.
PE   3: Inferred from homology;
KW   Coenzyme M biosynthesis; Hydrolase; Magnesium; Reference proteome.
FT   CHAIN           1..226
FT                   /note="2-phosphosulfolactate phosphatase"
FT                   /id="PRO_0000081460"
SQ   SEQUENCE   226 AA;  24807 MW;  C83853251C5804A7 CRC64;
     MAMRIRLSFE RPEGSGLCIM VDLLRASATI TAALDRFREV IPVADIEEAM EYSRKGYLVA
     GERGGETLPG FIANSPLEVK NYRGDVLVLT TSNGTRILES VKSDALVGCL NNLDAVAEAA
     RELSDEVEVV MAGVNGRFAI EDFLCAGEII AAIDGEMDEY AEASVLAVQD RSLVDDAIRR
     SRSAERLGGL GFMDDVEYCI KRNITGNVPV YRDGRIELME EIRRLH