ID   COMD_METJA              Reviewed;         169 AA.
AC   P58415;
DT   05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT   05-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Sulfopyruvate decarboxylase subunit alpha {ECO:0000303|PubMed:10940029};
DE            EC=4.1.1.79 {ECO:0000269|PubMed:10940029};
GN   Name=comD {ECO:0000303|PubMed:10940029}; OrderedLocusNames=MJ0255.1;
OS   Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS   10045 / NBRC 100440) (Methanococcus jannaschii).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanocaldococcaceae; Methanocaldococcus.
OX   NCBI_TaxID=243232;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX   PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA   Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA   Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA   Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA   Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA   Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA   Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA   Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA   Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT   "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT   jannaschii.";
RL   Science 273:1058-1073(1996).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP   REGULATION, AND SUBUNIT.
RC   STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX   PubMed=10940029; DOI=10.1128/jb.182.17.4862-4867.2000;
RA   Graupner M., Xu H., White R.H.;
RT   "Identification of the gene encoding sulfopyruvate decarboxylase, an enzyme
RT   involved in biosynthesis of coenzyme M.";
RL   J. Bacteriol. 182:4862-4867(2000).
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:10940029}.
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:10940029};
CC   -!- ACTIVITY REGULATION: Inhibited by oxygen when heated in air at 80
CC       degrees Celsius. The enzyme is reactivated by addition of dithionite.
CC       {ECO:0000269|PubMed:10940029}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.64 mM for 3-sulfopyruvate {ECO:0000269|PubMed:10940029};
CC         Vmax=52 umol/min/mg enzyme {ECO:0000269|PubMed:10940029};
CC   -!- PATHWAY: Cofactor biosynthesis; coenzyme M biosynthesis;
CC       sulfoacetaldehyde from phosphoenolpyruvate and sulfite: step 4/4.
CC       {ECO:0000305|PubMed:10940029}.
CC   -!- SUBUNIT: Heterododecamer composed of 6 subunits alpha and 6 subunits
CC       beta. {ECO:0000269|PubMed:10940029}.
CC   -!- SIMILARITY: Belongs to the ComD family. {ECO:0000305}.
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DR   EMBL; L77117; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; WP_064496437.1; NC_000909.1.
DR   AlphaFoldDB; P58415; -.
DR   SMR; P58415; -.
DR   GeneID; 27929948; -.
DR   InParanoid; P58415; -.
DR   OMA; IPMGQWT; -.
DR   OrthoDB; 80332at2157; -.
DR   PhylomeDB; P58415; -.
DR   BioCyc; MetaCyc:MON-2265; -.
DR   BRENDA; 4.1.1.79; 3260.
DR   SABIO-RK; P58415; -.
DR   UniPathway; UPA00355; UER00472.
DR   Proteomes; UP000000805; Chromosome.
DR   GO; GO:0050545; F:sulfopyruvate decarboxylase activity; IDA:MENGO.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IBA:GO_Central.
DR   GO; GO:0019295; P:coenzyme M biosynthetic process; IDA: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   1: Evidence at protein level;
KW   Coenzyme M biosynthesis; Decarboxylase; Lyase; Reference proteome.
FT   CHAIN           1..169
FT                   /note="Sulfopyruvate decarboxylase subunit alpha"
FT                   /id="PRO_0000090837"
SQ   SEQUENCE   169 AA;  19059 MW;  2FB248306F7D211C CRC64;
     MRGSLAIYNA LKDSNIDFIC SVPCANLKNL LKLIEEDKNI INIPATREEE AFGICAGAYL
     AGKKTAILMQ NSGIGNSINA IASLYKTFQI PTLLIISHRG DLKEQIPAQI PMGRWIEKLL
     DVCEIPTYKP KTPEEAYKLI KYASSYMYKI SYPVALLFDA LYWEYDLEK