ID   COME_METMP              Reviewed;         185 AA.
AC   Q6LWM0;
DT   22-JUL-2015, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Sulfopyruvate decarboxylase subunit beta {ECO:0000303|PubMed:24151448};
DE            EC=4.1.1.79 {ECO:0000305|PubMed:24151448};
GN   Name=comE {ECO:0000250|UniProtKB:P58416}; OrderedLocusNames=MMP1689;
OS   Methanococcus maripaludis (strain S2 / LL).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=267377;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S2 / LL;
RX   PubMed=15466049; DOI=10.1128/jb.186.20.6956-6969.2004;
RA   Hendrickson E.L., Kaul R., Zhou Y., Bovee D., Chapman P., Chung J.,
RA   Conway de Macario E., Dodsworth J.A., Gillett W., Graham D.E., Hackett M.,
RA   Haydock A.K., Kang A., Land M.L., Levy R., Lie T.J., Major T.A.,
RA   Moore B.C., Porat I., Palmeiri A., Rouse G., Saenphimmachak C., Soell D.,
RA   Van Dien S., Wang T., Whitman W.B., Xia Q., Zhang Y., Larimer F.W.,
RA   Olson M.V., Leigh J.A.;
RT   "Complete genome sequence of the genetically tractable hydrogenotrophic
RT   methanogen Methanococcus maripaludis.";
RL   J. Bacteriol. 186:6956-6969(2004).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RC   STRAIN=S2 / LL;
RX   PubMed=24151448; DOI=10.1155/2013/185250;
RA   Sarmiento F., Ellison C.K., Whitman W.B.;
RT   "Genetic confirmation of the role of sulfopyruvate decarboxylase in
RT   coenzyme M biosynthesis in Methanococcus maripaludis.";
RL   Archaea 2013:185250-185250(2013).
CC   -!- FUNCTION: Involved in the biosynthesis of the coenzyme M (2-
CC       mercaptoethanesulfonic acid). Catalyzes the decarboxylation of
CC       sulfopyruvate to sulfoacetaldehyde. {ECO:0000269|PubMed:24151448}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-sulfopyruvate + H(+) = CO2 + sulfoacetaldehyde;
CC         Xref=Rhea:RHEA:20948, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:57940, ChEBI:CHEBI:58246; EC=4.1.1.79;
CC         Evidence={ECO:0000305|PubMed:24151448};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000250|UniProtKB:P58416};
CC       Note=Binds 1 thiamine pyrophosphate per subunit.
CC       {ECO:0000250|UniProtKB:P58416};
CC   -!- PATHWAY: Cofactor biosynthesis; coenzyme M biosynthesis;
CC       sulfoacetaldehyde from phosphoenolpyruvate and sulfite: step 4/4.
CC       {ECO:0000305|PubMed:24151448}.
CC   -!- SUBUNIT: Heterododecamer composed of 6 subunits alpha and 6 subunits
CC       beta. {ECO:0000250|UniProtKB:P58416}.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene are partial coenzyme M
CC       auxotrophs; they grow poorly in the absence of coenzyme M and retain
CC       less than 3% of the wild type level of coenzyme M biosynthesis.
CC       {ECO:0000269|PubMed:24151448}.
CC   -!- SIMILARITY: Belongs to the TPP enzyme family. {ECO:0000305}.
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DR   EMBL; BX950229; CAF31245.1; -; Genomic_DNA.
DR   RefSeq; WP_011171633.1; NC_005791.1.
DR   AlphaFoldDB; Q6LWM0; -.
DR   SMR; Q6LWM0; -.
DR   STRING; 267377.MMP1689; -.
DR   DNASU; 2762371; -.
DR   EnsemblBacteria; CAF31245; CAF31245; MMP1689.
DR   GeneID; 2762371; -.
DR   KEGG; mmp:MMP1689; -.
DR   PATRIC; fig|267377.15.peg.1729; -.
DR   eggNOG; arCOG01614; Archaea.
DR   HOGENOM; CLU_117492_1_0_2; -.
DR   OMA; GSVLMNM; -.
DR   OrthoDB; 84988at2157; -.
DR   BioCyc; MMAR267377:MMP_RS08705-MON; -.
DR   BRENDA; 4.1.1.79; 3262.
DR   UniPathway; UPA00355; UER00472.
DR   Proteomes; UP000000590; Chromosome.
DR   GO; GO:0050545; F:sulfopyruvate decarboxylase activity; ISS:UniProtKB.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; ISS:UniProtKB.
DR   GO; GO:0019295; P:coenzyme M biosynthetic process; IDA:CACAO.
DR   CDD; cd03372; TPP_ComE; 1.
DR   InterPro; IPR022494; Sulfopyruvate_deCO2ase_bsu.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR011766; TPP_enzyme-bd_C.
DR   Pfam; PF02775; TPP_enzyme_C; 1.
DR   SUPFAM; SSF52518; SSF52518; 1.
DR   TIGRFAMs; TIGR03846; sulfopy_beta; 1.
PE   1: Evidence at protein level;
KW   Coenzyme M biosynthesis; Decarboxylase; Lyase; Reference proteome;
KW   Thiamine pyrophosphate.
FT   CHAIN           1..185
FT                   /note="Sulfopyruvate decarboxylase subunit beta"
FT                   /id="PRO_0000433483"
SQ   SEQUENCE   185 AA;  20281 MW;  D27D05094CEEEA25 CRC64;
     MELTRYEIIK ILMEYVTDEI VVCNIGIPSK ELFKINDREK NFYMLGSMGL SSSIGHGLAL
     SVNEKVIAID GDGSVLMNMG SLATIGKTTP KDFLLLIVDN CAYGSTGNQE THSTCTDLYQ
     VSKACGIDSI GVFNEEQLRD AVKLALSESG TKVIVAKARP HNENVPNINL VPTEIKHRFM
     NAIKK