ID   COME_METJA              Reviewed;         188 AA.
AC   P58416; Q57704;
DT   05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT   05-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Sulfopyruvate decarboxylase subunit beta {ECO:0000303|PubMed:10940029};
DE            EC=4.1.1.79 {ECO:0000269|PubMed:10940029};
GN   Name=comE {ECO:0000303|PubMed:10940029}; OrderedLocusNames=MJ0256;
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, SUBUNIT, AND COFACTOR.
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   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000269|PubMed:10940029};
CC       Note=Binds 1 thiamine pyrophosphate per subunit.
CC       {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 TPP enzyme family. {ECO:0000305}.
CC   -!- CAUTION: The sequence corresponding to this entry was originally
CC       entered in Swiss-Prot as AC Q57704 in November 1997 and was deleted in
CC       July 1999 because TIGR removed the CDS for that ORF. We have recreated
CC       it because of the evidence (PubMed:10940029) that it really exists.
CC       {ECO:0000305|PubMed:10940029}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; L77117; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; A64332; A64332.
DR   RefSeq; WP_064496438.1; NC_000909.1.
DR   AlphaFoldDB; P58416; -.
DR   SMR; P58416; -.
DR   GeneID; 27929949; -.
DR   InParanoid; P58416; -.
DR   OMA; GSVLMNM; -.
DR   OrthoDB; 84988at2157; -.
DR   PhylomeDB; P58416; -.
DR   BioCyc; MetaCyc:MON-2266; -.
DR   SABIO-RK; P58416; -.
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; IDA:UniProtKB.
DR   GO; GO:0019295; P:coenzyme M biosynthetic process; IDA: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   1: Evidence at protein level;
KW   Coenzyme M biosynthesis; Decarboxylase; Lyase; Reference proteome;
KW   Thiamine pyrophosphate.
FT   CHAIN           1..188
FT                   /note="Sulfopyruvate decarboxylase subunit beta"
FT                   /id="PRO_0000090839"
SQ   SEQUENCE   188 AA;  20980 MW;  52A6C91E2D43B97D CRC64;
     MYPKRIDIIK KIVENVGEKE IIVSNIGIPS KELYYVKDRE RNFYMLGSMG LASSIGLGLA
     LNCEDKVIVI DGDGSILMNL GSLSTIGYMN PKNYILVIID NSAYGSTGNQ KTHTGKNTNL
     EEIAKGCGLD TITTESLEEF EKEFKNALNE EKCKVIIAKT IPYNEKCSNI EIPPVVLKYR
     FMEAIKRS