ID   PSLS_METTH              Reviewed;         258 AA.
AC   O27710;
DT   21-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 114.
DE   RecName: Full=Phosphosulfolactate synthase;
DE            EC=4.4.1.19;
DE   AltName: Full=(2R)-phospho-3-sulfolactate synthase;
DE            Short=PSL synthase;
GN   Name=comA; OrderedLocusNames=MTH_1674;
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   -!- FUNCTION: Catalyzes the addition of sulfite to phosphoenolpyruvate
CC       (PEP) to yield (2R)-phospho-3-sulfolactate (PSL). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R)-O-phospho-3-sulfolactate = H(+) + phosphoenolpyruvate +
CC         sulfite; Xref=Rhea:RHEA:22784, ChEBI:CHEBI:15378, ChEBI:CHEBI:15597,
CC         ChEBI:CHEBI:17359, ChEBI:CHEBI:58702; EC=4.4.1.19;
CC   -!- PATHWAY: Cofactor biosynthesis; coenzyme M biosynthesis;
CC       sulfoacetaldehyde from phosphoenolpyruvate and sulfite: step 1/4.
CC   -!- SIMILARITY: Belongs to the phosphosulfolactate synthase family.
CC       {ECO:0000305}.
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DR   EMBL; AE000666; AAB86146.1; -; Genomic_DNA.
DR   PIR; G69090; G69090.
DR   RefSeq; WP_010877281.1; NC_000916.1.
DR   AlphaFoldDB; O27710; -.
DR   SMR; O27710; -.
DR   STRING; 187420.MTH_1674; -.
DR   EnsemblBacteria; AAB86146; AAB86146; MTH_1674.
DR   GeneID; 1470759; -.
DR   KEGG; mth:MTH_1674; -.
DR   PATRIC; fig|187420.15.peg.1634; -.
DR   HOGENOM; CLU_062679_2_0_2; -.
DR   OMA; MFEASNA; -.
DR   UniPathway; UPA00355; UER00469.
DR   Proteomes; UP000005223; Chromosome.
DR   GO; GO:0043817; F:phosphosulfolactate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019295; P:coenzyme M biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR022370; Arch_ComA.
DR   InterPro; IPR003830; ComA_synth.
DR   InterPro; IPR036112; ComA_synth_sf.
DR   Pfam; PF02679; ComA; 1.
DR   SUPFAM; SSF102110; SSF102110; 1.
DR   TIGRFAMs; TIGR03849; arch_ComA; 1.
PE   3: Inferred from homology;
KW   Coenzyme M biosynthesis; Lyase; Reference proteome.
FT   CHAIN           1..258
FT                   /note="Phosphosulfolactate synthase"
FT                   /id="PRO_0000080831"
SQ   SEQUENCE   258 AA;  29409 MW;  CC28CAA55E622CC5 CRC64;
     MNAFDFLTPP RSGKPRKNGI TMVLDKGMGP ASARDLMEIS SDYVDFIKFG WGTLPLHRRD
     TVKEKVDMYR SFDVEPYPGG TLFEIAHLND KVEEYFQEAR SLGFETLEIS NGTVEIETEE
     KCRLIEMAVD EGFMVLSEVG KKDPERDRLL EPDDRVRLVR ADLRAGASMV LMEARESGQN
     IGIYDERGNI REDEFNHLTD RLPMDRIIWE APQKSQQVYF ILKIGPDVNL GNIPPEEITA
     LETIRRGLRG DTLGKVNL