ID   PSLS_METJA              Reviewed;         251 AA.
AC   Q57703;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 127.
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=MJ0255;
OS   Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS   10045 / NBRC 100440) (Methanococcus jannaschii).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanocaldococcaceae; Methanocaldococcus.
OX   NCBI_TaxID=243232;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX   PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA   Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA   Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA   Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA   Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA   Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA   Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA   Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA   Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT   "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT   jannaschii.";
RL   Science 273:1058-1073(1996).
RN   [2]
RP   CHARACTERIZATION, AND MUTAGENESIS OF LYS-137.
RC   STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX   PubMed=11830598; DOI=10.1074/jbc.m201011200;
RA   Graham D.E., Xu H., White R.H.;
RT   "Identification of coenzyme M biosynthetic phosphosulfolactate synthase: a
RT   new family of sulfonate-biosynthesizing enzymes.";
RL   J. Biol. Chem. 277:13421-13429(2002).
CC   -!- FUNCTION: Catalyzes the addition of sulfite to phosphoenolpyruvate
CC       (PEP) to yield (2R)-phospho-3-sulfolactate (PSL).
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 8.5.;
CC   -!- PATHWAY: Cofactor biosynthesis; coenzyme M biosynthesis;
CC       sulfoacetaldehyde from phosphoenolpyruvate and sulfite: step 1/4.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000305}.
CC   -!- MISCELLANEOUS: The enzyme is stereospecific.
CC   -!- SIMILARITY: Belongs to the phosphosulfolactate synthase family.
CC       {ECO:0000305}.
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; L77117; AAB98242.1; -; Genomic_DNA.
DR   PIR; H64331; H64331.
DR   RefSeq; WP_010869753.1; NC_000909.1.
DR   PDB; 1QWG; X-ray; 1.60 A; A=1-251.
DR   PDBsum; 1QWG; -.
DR   AlphaFoldDB; Q57703; -.
DR   SMR; Q57703; -.
DR   STRING; 243232.MJ_0255; -.
DR   EnsemblBacteria; AAB98242; AAB98242; MJ_0255.
DR   GeneID; 1451109; -.
DR   KEGG; mja:MJ_0255; -.
DR   eggNOG; arCOG04896; Archaea.
DR   HOGENOM; CLU_062679_2_0_2; -.
DR   InParanoid; Q57703; -.
DR   OMA; MFEASNA; -.
DR   OrthoDB; 37705at2157; -.
DR   PhylomeDB; Q57703; -.
DR   BioCyc; MetaCyc:MON-2262; -.
DR   BRENDA; 4.4.1.19; 3260.
DR   SABIO-RK; Q57703; -.
DR   UniPathway; UPA00355; UER00469.
DR   EvolutionaryTrace; Q57703; -.
DR   Proteomes; UP000000805; Chromosome.
DR   GO; GO:0043817; F:phosphosulfolactate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0050545; F:sulfopyruvate decarboxylase activity; IDA:MENGO.
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   1: Evidence at protein level;
KW   3D-structure; Coenzyme M biosynthesis; Lyase; Reference proteome.
FT   CHAIN           1..251
FT                   /note="Phosphosulfolactate synthase"
FT                   /id="PRO_0000080830"
FT   MUTAGEN         137
FT                   /note="K->N: Loss of function."
FT                   /evidence="ECO:0000269|PubMed:11830598"
FT   HELIX           5..7
FT                   /evidence="ECO:0007829|PDB:1QWG"
FT   STRAND          16..22
FT                   /evidence="ECO:0007829|PDB:1QWG"
FT   HELIX           25..35
FT                   /evidence="ECO:0007829|PDB:1QWG"
FT   HELIX           36..38
FT                   /evidence="ECO:0007829|PDB:1QWG"
FT   STRAND          40..44
FT                   /evidence="ECO:0007829|PDB:1QWG"
FT   HELIX           48..51
FT                   /evidence="ECO:0007829|PDB:1QWG"
FT   HELIX           54..65
FT                   /evidence="ECO:0007829|PDB:1QWG"
FT   TURN            66..68
FT                   /evidence="ECO:0007829|PDB:1QWG"
FT   STRAND          70..73
FT                   /evidence="ECO:0007829|PDB:1QWG"
FT   HELIX           75..83
FT                   /evidence="ECO:0007829|PDB:1QWG"
FT   HELIX           87..97
FT                   /evidence="ECO:0007829|PDB:1QWG"
FT   STRAND          101..104
FT                   /evidence="ECO:0007829|PDB:1QWG"
FT   STRAND          107..109
FT                   /evidence="ECO:0007829|PDB:1QWG"
FT   HELIX           113..125
FT                   /evidence="ECO:0007829|PDB:1QWG"
FT   STRAND          129..134
FT                   /evidence="ECO:0007829|PDB:1QWG"
FT   HELIX           139..142
FT                   /evidence="ECO:0007829|PDB:1QWG"
FT   HELIX           147..160
FT                   /evidence="ECO:0007829|PDB:1QWG"
FT   STRAND          163..167
FT                   /evidence="ECO:0007829|PDB:1QWG"
FT   TURN            170..172
FT                   /evidence="ECO:0007829|PDB:1QWG"
FT   HELIX           187..194
FT                   /evidence="ECO:0007829|PDB:1QWG"
FT   HELIX           199..201
FT                   /evidence="ECO:0007829|PDB:1QWG"
FT   STRAND          202..205
FT                   /evidence="ECO:0007829|PDB:1QWG"
FT   HELIX           209..219
FT                   /evidence="ECO:0007829|PDB:1QWG"
FT   STRAND          225..229
FT                   /evidence="ECO:0007829|PDB:1QWG"
FT   HELIX           230..232
FT                   /evidence="ECO:0007829|PDB:1QWG"
FT   HELIX           233..241
FT                   /evidence="ECO:0007829|PDB:1QWG"
FT   HELIX           245..247
FT                   /evidence="ECO:0007829|PDB:1QWG"
FT   TURN            248..250
FT                   /evidence="ECO:0007829|PDB:1QWG"
SQ   SEQUENCE   251 AA;  28368 MW;  9B3F2CD349880E4C CRC64;
     MKAFEFLYED FQRGLTVVLD KGLPPKFVED YLKVCGDYID FVKFGWGTSA VIDRDVVKEK
     INYYKDWGIK VYPGGTLFEY AYSKGKFDEF LNECEKLGFE AVEISDGSSD ISLEERKNAI
     KRAKDNGFMV LTEVGKKMPD KDKQLTIDDR IKLINFDLDA GADYVIIEGR ESGKGIGLFD
     KEGKVKENEL DVLAKNVDIN KVIFEAPQKS QQVAFILKFG SSVNLANIAF DEVISLETLR
     RGLRGDTFGK V