ID   COME_METTH              Reviewed;         185 AA.
AC   O27275;
DT   05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 106.
DE   RecName: Full=Sulfopyruvate decarboxylase subunit beta {ECO:0000250|UniProtKB:P58416};
DE            EC=4.1.1.79 {ECO:0000250|UniProtKB:P58416};
GN   Name=comE {ECO:0000250|UniProtKB:P58416}; OrderedLocusNames=MTH_1207;
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: Involved in the biosynthesis of the coenzyme M (2-
CC       mercaptoethanesulfonic acid). Catalyzes the decarboxylation of
CC       sulfopyruvate to sulfoacetaldehyde. {ECO:0000250|UniProtKB:P58416}.
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:0000250|UniProtKB:P58416};
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:0000250|UniProtKB:P58416}.
CC   -!- SUBUNIT: Heterododecamer composed of 6 subunits alpha and 6 subunits
CC       beta. {ECO:0000250|UniProtKB:P58416}.
CC   -!- SIMILARITY: Belongs to the TPP enzyme family. {ECO:0000305}.
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DR   EMBL; AE000666; AAB85696.1; -; Genomic_DNA.
DR   PIR; B69028; B69028.
DR   RefSeq; WP_010876831.1; NC_000916.1.
DR   AlphaFoldDB; O27275; -.
DR   SMR; O27275; -.
DR   STRING; 187420.MTH_1207; -.
DR   EnsemblBacteria; AAB85696; AAB85696; MTH_1207.
DR   GeneID; 1471615; -.
DR   KEGG; mth:MTH_1207; -.
DR   PATRIC; fig|187420.15.peg.1185; -.
DR   HOGENOM; CLU_117492_1_0_2; -.
DR   OMA; GSVLMNM; -.
DR   UniPathway; UPA00355; UER00472.
DR   Proteomes; UP000005223; 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; ISS:UniProtKB.
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   3: Inferred from homology;
KW   Coenzyme M biosynthesis; Decarboxylase; Lyase; Reference proteome;
KW   Thiamine pyrophosphate.
FT   CHAIN           1..185
FT                   /note="Sulfopyruvate decarboxylase subunit beta"
FT                   /id="PRO_0000090840"
SQ   SEQUENCE   185 AA;  20008 MW;  62682769A6F3F4DC CRC64;
     MMLERIEAIE RITGVLEDEL VICNLGFPSR ELYSIRDSPR HFYMLGSMGM ASSIGLGLAL
     SQERRVVVLD GDGSILMNLG GLVTAAAQSP GNLIIVLLDN RCYATTGSQC TYADVIDLGA
     VAESMGFNVI RFADDLNFEQ ALAMDGPVFA HVPVKPGNAD VPVIDLDAEE IIERFIKEVR
     GATED