ID C9RDJ5_METVM Unreviewed; 170 AA.
AC C9RDJ5;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=sulfopyruvate decarboxylase {ECO:0000256|ARBA:ARBA00038875};
DE EC=4.1.1.79 {ECO:0000256|ARBA:ARBA00038875};
GN OrderedLocusNames=Metvu_1521 {ECO:0000313|EMBL:ACX73374.1};
OS Methanocaldococcus vulcanius (strain ATCC 700851 / DSM 12094 / M7)
OS (Methanococcus vulcanius).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=579137 {ECO:0000313|EMBL:ACX73374.1, ECO:0000313|Proteomes:UP000002063};
RN [1] {ECO:0000313|EMBL:ACX73374.1, ECO:0000313|Proteomes:UP000002063}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700851 / DSM 12094 / M7
RC {ECO:0000313|Proteomes:UP000002063};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Lcollab F.I., Brettin T., Detter J.C.,
RA Han C., Tapia R., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Ovchinikova G., Sieprawska-Lupa M., Whitman W.B., Woyke T.;
RT "Complete sequence of chromosome of Methanocaldococcus vulcanius M7.";
RL Submitted (OCT-2009) 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}.
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DR EMBL; CP001787; ACX73374.1; -; Genomic_DNA.
DR RefSeq; WP_015733593.1; NC_013407.1.
DR AlphaFoldDB; C9RDJ5; -.
DR STRING; 579137.Metvu_1521; -.
DR GeneID; 8513868; -.
DR KEGG; mvu:Metvu_1521; -.
DR eggNOG; arCOG01613; Archaea.
DR HOGENOM; CLU_113594_0_0_2; -.
DR OrthoDB; 53192at2157; -.
DR Proteomes; UP000002063; Chromosome.
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}.
FT DOMAIN 1..100
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
SQ SEQUENCE 170 AA; 19049 MW; B86DB76B3D45BC85 CRC64;
MKGSLAIYNA LKDSGIEFIC SVPCANLKNL LNLIENDNST FTHIKATREE EAFGICAGAH
LAGKKTAILM QNSGIGNSIN AIASLYKTFQ IPTLLIISHR GDLKEKIPAQ IPMGRWIEKL
LDVCEIPTYK PKTPEEGYKL ITYASDYMER ISYPVALLFD ALYWEFDQEK
//
