ID   COMDE_METAC             Reviewed;         387 AA.
AC   Q8TKU6;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Sulfopyruvate decarboxylase {ECO:0000303|PubMed:19761441};
DE            Short=SpyrDC {ECO:0000303|PubMed:19761441};
DE            EC=4.1.1.79 {ECO:0000269|PubMed:19761441};
GN   Name=comDE {ECO:0000303|PubMed:19761441}; OrderedLocusNames=MA_3298;
OS   Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 /
OS   C2A).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=188937;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A;
RX   PubMed=11932238; DOI=10.1101/gr.223902;
RA   Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W.,
RA   Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J.,
RA   Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P.,
RA   McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D.,
RA   Cann I., Graham D.E., Grahame D.A., Guss A.M., Hedderich R.,
RA   Ingram-Smith C., Kuettner H.C., Krzycki J.A., Leigh J.A., Li W., Liu J.,
RA   Mukhopadhyay B., Reeve J.N., Smith K., Springer T.A., Umayam L.A.,
RA   White O., White R.H., de Macario E.C., Ferry J.G., Jarrell K.F., Jing H.,
RA   Macario A.J.L., Paulsen I.T., Pritchett M., Sowers K.R., Swanson R.V.,
RA   Zinder S.H., Lander E., Metcalf W.W., Birren B.;
RT   "The genome of Methanosarcina acetivorans reveals extensive metabolic and
RT   physiological diversity.";
RL   Genome Res. 12:532-542(2002).
RN   [2]
RP   FUNCTION AS A SULFOPYRUVATE DECARBOXYLASE, CATALYTIC ACTIVITY, SUBSTRATE
RP   SPECIFICITY, AND COFACTOR.
RX   PubMed=19761441; DOI=10.1042/bj20090999;
RA   Graham D.E., Taylor S.M., Wolf R.Z., Namboori S.C.;
RT   "Convergent evolution of coenzyme M biosynthesis in the Methanosarcinales:
RT   cysteate synthase evolved from an ancestral threonine synthase.";
RL   Biochem. J. 424:467-478(2009).
CC   -!- FUNCTION: Involved in the biosynthesis of the coenzyme M (2-
CC       mercaptoethanesulfonic acid). Catalyzes the decarboxylation of
CC       sulfopyruvate to sulfoacetaldehyde. Is not able to decarboxylate the
CC       analogous compounds 2-oxoglutarate or 2-oxosuberate.
CC       {ECO:0000269|PubMed:19761441}.
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:0000269|PubMed:19761441};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000269|PubMed:19761441};
CC       Note=Binds 1 thiamine pyrophosphate per subunit.
CC       {ECO:0000269|PubMed:19761441};
CC   -!- PATHWAY: Cofactor biosynthesis; coenzyme M biosynthesis. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the TPP enzyme family. {ECO:0000305}.
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DR   EMBL; AE010299; AAM06668.1; -; Genomic_DNA.
DR   RefSeq; WP_011023231.1; NC_003552.1.
DR   AlphaFoldDB; Q8TKU6; -.
DR   SMR; Q8TKU6; -.
DR   STRING; 188937.MA_3298; -.
DR   EnsemblBacteria; AAM06668; AAM06668; MA_3298.
DR   GeneID; 1475191; -.
DR   KEGG; mac:MA_3298; -.
DR   HOGENOM; CLU_042853_0_0_2; -.
DR   InParanoid; Q8TKU6; -.
DR   OMA; PILASWR; -.
DR   OrthoDB; 45859at2157; -.
DR   PhylomeDB; Q8TKU6; -.
DR   BioCyc; MetaCyc:MON-15916; -.
DR   UniPathway; UPA00355; -.
DR   Proteomes; UP000002487; Chromosome.
DR   GO; GO:0050545; F:sulfopyruvate decarboxylase activity; IBA:GO_Central.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IBA:GO_Central.
DR   GO; GO:0019295; P:coenzyme M biosynthetic process; IBA:GO_Central.
DR   CDD; cd03372; TPP_ComE; 1.
DR   InterPro; IPR022502; Sulfopyruvate_deCO2ase_alpha.
DR   InterPro; IPR022494; Sulfopyruvate_deCO2ase_bsu.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR   InterPro; IPR011766; TPP_enzyme-bd_C.
DR   Pfam; PF02775; TPP_enzyme_C; 1.
DR   Pfam; PF02776; TPP_enzyme_N; 1.
DR   SUPFAM; SSF52518; SSF52518; 2.
DR   TIGRFAMs; TIGR03846; sulfopy_beta; 1.
DR   TIGRFAMs; TIGR03845; sulfopyru_alph; 1.
PE   1: Evidence at protein level;
KW   Coenzyme M biosynthesis; Decarboxylase; Lyase; Reference proteome;
KW   Thiamine pyrophosphate.
FT   CHAIN           1..387
FT                   /note="Sulfopyruvate decarboxylase"
FT                   /id="PRO_0000392657"
SQ   SEQUENCE   387 AA;  42301 MW;  CF8FD1AF3796957F CRC64;
     MYVVNPEEKV IEIMKQTGID LAATLPCDRI KNLLPLVSEN FPEIKLTREE NGVGICAGIY
     LAGGKPMMLI QSTGLGNMIN ALESLNVTCK IPLPILASWR GVYKEGIEAQ VPLGAHLPSI
     LEGAGLTYTI IGETEKLPLL ENVILDAFEN SRPHIALVSP KVWEASECCA WQAAGMPIKP
     EIMERTCRFS LTSGTLKPFM LRNDAICTLA SELDDEITVT NLGVPCKELY ACRDRELNFY
     MFGSMGLVSS IGLGLALRSE KTVITFDGDG SLLMNPNALL EIAKEAPKNL IIIALDNGAY
     GSTGSQETCA LRYIDLEIFA NACGIQNTAK VNSKEGVIEA FRKFKAMREL SFIHVILKPG
     NTNAPNIPMS PEEATKRFKE TLDVKKF