ID H1KWX1_9EURY Unreviewed; 168 AA.
AC H1KWX1;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=sulfopyruvate decarboxylase {ECO:0000256|ARBA:ARBA00038875};
DE EC=4.1.1.79 {ECO:0000256|ARBA:ARBA00038875};
GN ORFNames=MetfoDRAFT_0294 {ECO:0000313|EMBL:EHP89104.1};
OS Methanotorris formicicus Mc-S-70.
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanotorris.
OX NCBI_TaxID=647171 {ECO:0000313|EMBL:EHP89104.1, ECO:0000313|Proteomes:UP000003706};
RN [1] {ECO:0000313|EMBL:EHP89104.1, ECO:0000313|Proteomes:UP000003706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mc-S-70 {ECO:0000313|EMBL:EHP89104.1,
RC ECO:0000313|Proteomes:UP000003706};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Land M.L., Hauser L., Sieprawska-Lupa M., Takai K., Miyazaki J.,
RA Whitman W., Woyke T.J.;
RT "The draft genome of Methanotorris formicicus Mc-S-70.";
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in the biosynthesis of the coenzyme M (2-
CC mercaptoethanesulfonic acid). Catalyzes the decarboxylation of
CC sulfopyruvate to sulfoacetaldehyde. {ECO:0000256|ARBA:ARBA00037396}.
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:0000256|ARBA:ARBA00036439};
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme M biosynthesis;
CC sulfoacetaldehyde from phosphoenolpyruvate and sulfite: step 4/4.
CC {ECO:0000256|ARBA:ARBA00037914}.
CC -!- SUBUNIT: Heterododecamer composed of 6 subunits alpha and 6 subunits
CC beta. {ECO:0000256|ARBA:ARBA00038733}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EHP89104.1}.
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DR EMBL; AGJL01000004; EHP89104.1; -; Genomic_DNA.
DR RefSeq; WP_007043740.1; NZ_AGJL01000004.1.
DR AlphaFoldDB; H1KWX1; -.
DR STRING; 647171.MetfoDRAFT_0294; -.
DR PATRIC; fig|647171.4.peg.291; -.
DR OrthoDB; 53192at2157; -.
DR Proteomes; UP000003706; Unassembled WGS sequence.
DR GO; GO:0050545; F:sulfopyruvate decarboxylase activity; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0019295; P:coenzyme M biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd07035; TPP_PYR_POX_like; 1.
DR Gene3D; 3.40.50.970; -; 1.
DR InterPro; IPR022502; Sulfopyruvate_deCO2ase_alpha.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR NCBIfam; TIGR03845; sulfopyru_alph; 1.
DR PANTHER; PTHR42818:SF1; SULFOPYRUVATE DECARBOXYLASE; 1.
DR PANTHER; PTHR42818; SULFOPYRUVATE DECARBOXYLASE SUBUNIT ALPHA; 1.
DR Pfam; PF02776; TPP_enzyme_N; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
PE 4: Predicted;
KW Coenzyme M biosynthesis {ECO:0000256|ARBA:ARBA00022545};
KW Pyruvate {ECO:0000313|EMBL:EHP89104.1}.
FT DOMAIN 1..99
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
SQ SEQUENCE 168 AA; 18710 MW; 56F6B19E2FC97F8C CRC64;
MKGSESIYKA IKESGIDFIA SVPCANLKNL LNLIYNDEEI IHVPVTREEE GFGVCAGAHL
SGKKTALLMQ NSGLGNSINA IGSLYKVYDI PILLIISHRG DLKEKIPAQI PMGQWTKKLL
DVLNIPYYCP KTPEEAYKII PYASNLSIKM DYPVAVLFDA LYWEYDAL
//
