ID D7E8W0_METEZ Unreviewed; 384 AA.
AC D7E8W0;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=sulfopyruvate decarboxylase {ECO:0000256|ARBA:ARBA00038875};
DE EC=4.1.1.79 {ECO:0000256|ARBA:ARBA00038875};
GN OrderedLocusNames=Metev_0883 {ECO:0000313|EMBL:ADI73781.1};
OS Methanohalobium evestigatum (strain ATCC BAA-1072 / DSM 3721 / NBRC 107634
OS / OCM 161 / Z-7303).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanohalobium.
OX NCBI_TaxID=644295 {ECO:0000313|EMBL:ADI73781.1, ECO:0000313|Proteomes:UP000000391};
RN [1] {ECO:0000313|EMBL:ADI73781.1, ECO:0000313|Proteomes:UP000000391}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1072 / DSM 3721 / NBRC 107634 / OCM 161 / Z-7303
RC {ECO:0000313|Proteomes:UP000000391};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Saunders E., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Mikhailova N., Sieprawska-Lupa M., Whitman W.B., Anderson I.,
RA Woyke T.;
RT "Complete sequence chromosome of Methanohalobium evestigatum Z-7303.";
RL Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases.
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};
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DR EMBL; CP002069; ADI73781.1; -; Genomic_DNA.
DR AlphaFoldDB; D7E8W0; -.
DR STRING; 644295.Metev_0883; -.
DR KEGG; mev:Metev_0883; -.
DR HOGENOM; CLU_042853_0_0_2; -.
DR Proteomes; UP000000391; 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; cd03372; TPP_ComE; 1.
DR CDD; cd07035; TPP_PYR_POX_like; 1.
DR Gene3D; 3.40.50.970; -; 2.
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_TPP-bd.
DR NCBIfam; TIGR03846; sulfopy_beta; 1.
DR NCBIfam; TIGR03845; sulfopyru_alph; 1.
DR PANTHER; PTHR42818:SF1; SULFOPYRUVATE DECARBOXYLASE; 1.
DR PANTHER; PTHR42818; SULFOPYRUVATE DECARBOXYLASE SUBUNIT ALPHA; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR Pfam; PF02776; TPP_enzyme_N; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
PE 4: Predicted;
KW Coenzyme M biosynthesis {ECO:0000256|ARBA:ARBA00022545};
KW Reference proteome {ECO:0000313|Proteomes:UP000000391}.
FT DOMAIN 12..112
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 236..356
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 384 AA; 42000 MW; E10D7FFDF3106BAE CRC64;
MSTSNKSDDP ENIVVQMMLD NGIDYLATLP CDRIKNLLPL ISKNFVEIPL TREENGVGIC
AGLYMAGAKP MMAIQSSGLG NMINALESLN IACDIPLPVL ASWRGVYKEG IESQKPLGKS
LPSILEGAGI EYTIIDEVEK LYLVDRAISD SFKNRRPHII LMSPRVWEPS TCSARVEQDS
ENLKERSYEI NFKTNISKPE MVRYDAISVI SPLLDDEALV ANIGVPCKEL YSVNDRELNY
YMLGSLGLAS SIGMGIALKS ERDVVVLDGD GSILMNPNAL IEIARAKPSN LIVVALDNGA
YGSTGSQETL TAKFFDLELF ARASGFINTT KVHTKDELED AFVKAKNSGE LAFIHVILKS
GNVSCETVPL SPVEVTDRFM KALK
//
