ID   COMB_METJA              Reviewed;         224 AA.
AC   Q58540;
DT   05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT   05-DEC-2001, sequence version 2.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=2-phosphosulfolactate phosphatase;
DE            EC=3.1.3.71;
GN   Name=comB; OrderedLocusNames=MJ1140;
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.
RC   STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX   PubMed=11589710; DOI=10.1046/j.0014-2956.2001.02451.x;
RA   Graham D.E., Graupner M., Xu H., White R.H.;
RT   "Identification of coenzyme M biosynthetic 2-phosphosulfolactate
RT   phosphatase. A member of a new class of Mg2+-dependent acid phosphatases.";
RL   Eur. J. Biochem. 268:5176-5188(2001).
CC   -!- FUNCTION: Hydrolyzes both enantiomers of 2-phosphosulfolactate. Able to
CC       hydrolyze both enantiomers of 2-hydroxycarboxylic acids with
CC       pseudosymmetric centers of inversion. Specifically hydrolyzes (S)-
CC       phospholactate and (S)-phosphoglycerate.
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;
CC   -!- ACTIVITY REGULATION: Inhibited by vanadate.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 5.5.;
CC       Temperature dependence:
CC         Optimum temperature is 75 degrees Celsius.;
CC   -!- PATHWAY: Cofactor biosynthesis; coenzyme M biosynthesis;
CC       sulfoacetaldehyde from phosphoenolpyruvate and sulfite: step 2/4.
CC   -!- SUBUNIT: Monomer.
CC   -!- SIMILARITY: Belongs to the ComB family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB99140.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; L77117; AAB99140.1; ALT_INIT; Genomic_DNA.
DR   PIR; C64442; C64442.
DR   RefSeq; WP_064496734.1; NC_000909.1.
DR   AlphaFoldDB; Q58540; -.
DR   SMR; Q58540; -.
DR   STRING; 243232.MJ_1140; -.
DR   DNASU; 1452036; -.
DR   EnsemblBacteria; AAB99140; AAB99140; MJ_1140.
DR   GeneID; 1452036; -.
DR   KEGG; mja:MJ_1140; -.
DR   eggNOG; arCOG04871; Archaea.
DR   HOGENOM; CLU_070028_0_1_2; -.
DR   InParanoid; Q58540; -.
DR   OMA; RLFMSTT; -.
DR   OrthoDB; 84054at2157; -.
DR   PhylomeDB; Q58540; -.
DR   BioCyc; MetaCyc:MON-2263; -.
DR   UniPathway; UPA00355; UER00470.
DR   Proteomes; UP000000805; 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:0050545; F:sulfopyruvate decarboxylase activity; IDA:MENGO.
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   1: Evidence at protein level;
KW   Coenzyme M biosynthesis; Hydrolase; Magnesium; Reference proteome.
FT   CHAIN           1..224
FT                   /note="2-phosphosulfolactate phosphatase"
FT                   /id="PRO_0000081459"
SQ   SEQUENCE   224 AA;  25114 MW;  B981C5B5635404E9 CRC64;
     MITLCNRFTE YKCGNVAIVV DVLRASTTIT TLLSFIDEVY ITTSTSKKEN AIYIGERKGR
     KIEGFDFGNS PTEILANKDI IKERYENGEK VILTTTNGTR VLKSLDAEHI FIGAIVNAKY
     VAKAVEDFED VSLVPCHREN NFAIDDFIGC GVIAKYLNGE FDEFIKAALE LTKHDWMSLI
     LNSSSAENLK NLGYEKDVTF AILENSIDAV GIYKKDKSKV VRFK