ID   COMD_METTH              Reviewed;         165 AA.
AC   O27274;
DT   05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 100.
DE   RecName: Full=Sulfopyruvate decarboxylase subunit alpha {ECO:0000250|UniProtKB:P58415};
DE            EC=4.1.1.79 {ECO:0000250|UniProtKB:P58415};
GN   Name=comD {ECO:0000250|UniProtKB:P58415}; OrderedLocusNames=MTH_1206;
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:P58415}.
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:P58415};
CC   -!- PATHWAY: Cofactor biosynthesis; coenzyme M biosynthesis;
CC       sulfoacetaldehyde from phosphoenolpyruvate and sulfite: step 4/4.
CC       {ECO:0000250|UniProtKB:P58415}.
CC   -!- SUBUNIT: Heterododecamer composed of 6 subunits alpha and 6 subunits
CC       beta. {ECO:0000250|UniProtKB:P58415}.
CC   -!- SIMILARITY: Belongs to the ComD family. {ECO:0000250|UniProtKB:P58415}.
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DR   EMBL; AE000666; AAB85695.1; -; Genomic_DNA.
DR   PIR; A69028; A69028.
DR   RefSeq; WP_010876830.1; NC_000916.1.
DR   AlphaFoldDB; O27274; -.
DR   SMR; O27274; -.
DR   STRING; 187420.MTH_1206; -.
DR   EnsemblBacteria; AAB85695; AAB85695; MTH_1206.
DR   GeneID; 1471614; -.
DR   KEGG; mth:MTH_1206; -.
DR   PATRIC; fig|187420.15.peg.1184; -.
DR   HOGENOM; CLU_113594_0_0_2; -.
DR   OMA; IPMGQWT; -.
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; IEA:InterPro.
DR   GO; GO:0019295; P:coenzyme M biosynthetic process; ISS:UniProtKB.
DR   InterPro; IPR022502; Sulfopyruvate_deCO2ase_alpha.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR   Pfam; PF02776; TPP_enzyme_N; 1.
DR   SUPFAM; SSF52518; SSF52518; 1.
DR   TIGRFAMs; TIGR03845; sulfopyru_alph; 1.
PE   3: Inferred from homology;
KW   Coenzyme M biosynthesis; Decarboxylase; Lyase; Reference proteome.
FT   CHAIN           1..165
FT                   /note="Sulfopyruvate decarboxylase subunit alpha"
FT                   /id="PRO_0000090838"
SQ   SEQUENCE   165 AA;  17721 MW;  241B37A64C78F50B CRC64;
     MKVDSSEAVY AGMKDAGIDF AVSVPCVNLR TVLEMVDADP AIMHVPVTRE EEGFGVAAGA
     HMAGKTTAIL MQNSGLGNSV NVLASLYSLY HIPITMIVSH RGTEGEFMEA QVPMGRATGD
     ILRILEIPFR TPRSPAEARE SIGELTDISL RTSKAVAVLL DVSYW