ID   COMD_METMP              Reviewed;         167 AA.
AC   Q6M060;
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 alpha {ECO:0000250|UniProtKB:P58415};
DE            EC=4.1.1.79 {ECO:0000250|UniProtKB:P58415};
GN   Name=comD; OrderedLocusNames=MMP0411;
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).
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; BX950229; CAF29967.1; -; Genomic_DNA.
DR   RefSeq; WP_011170355.1; NC_005791.1.
DR   AlphaFoldDB; Q6M060; -.
DR   SMR; Q6M060; -.
DR   STRING; 267377.MMP0411; -.
DR   DNASU; 2761582; -.
DR   EnsemblBacteria; CAF29967; CAF29967; MMP0411.
DR   GeneID; 2761582; -.
DR   KEGG; mmp:MMP0411; -.
DR   PATRIC; fig|267377.15.peg.415; -.
DR   eggNOG; arCOG01613; Archaea.
DR   HOGENOM; CLU_113594_0_0_2; -.
DR   OMA; IPMGQWT; -.
DR   OrthoDB; 80332at2157; -.
DR   BioCyc; MMAR267377:MMP_RS02190-MON; -.
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; 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..167
FT                   /note="Sulfopyruvate decarboxylase subunit alpha"
FT                   /id="PRO_0000433482"
SQ   SEQUENCE   167 AA;  18467 MW;  EE774B6D249DD3A4 CRC64;
     MNASEAVYKA ILDSGVDFVT SVPCANLKTV LNYLNDDKDI QHIPVTREEE GIGVCTGAYL
     GGRKTALLMQ NSGLGNSINA IGSLVKVYKI PILIIISHRG DLKEKISAQI PMGQWTKKLL
     ETVEIPYFSP KTPDEAYKLI KDASELSINM EYPVAILLDA LYWEHDK