ID A0A166DDA2_9EURY Unreviewed; 288 AA.
AC A0A166DDA2;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Pyruvate synthase subunit PorB {ECO:0000313|EMBL:KZX15468.1};
DE EC=1.2.7.1 {ECO:0000313|EMBL:KZX15468.1};
GN Name=porB {ECO:0000313|EMBL:KZX15468.1};
GN ORFNames=MBCUT_14630 {ECO:0000313|EMBL:KZX15468.1};
OS Methanobrevibacter cuticularis.
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX NCBI_TaxID=47311 {ECO:0000313|EMBL:KZX15468.1, ECO:0000313|Proteomes:UP000077275};
RN [1] {ECO:0000313|EMBL:KZX15468.1, ECO:0000313|Proteomes:UP000077275}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11139 {ECO:0000313|EMBL:KZX15468.1,
RC ECO:0000313|Proteomes:UP000077275};
RA Poehlein A., Seedorf H., Daniel R.;
RT "Genome sequence of Methanobrevibacter cuticularis DSM 11139.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
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:KZX15468.1}.
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; LWMW01000117; KZX15468.1; -; Genomic_DNA.
DR RefSeq; WP_067260033.1; NZ_LWMW01000117.1.
DR AlphaFoldDB; A0A166DDA2; -.
DR STRING; 47311.MBCUT_14630; -.
DR PATRIC; fig|47311.3.peg.1596; -.
DR OrthoDB; 296931at2157; -.
DR Proteomes; UP000077275; Unassembled WGS sequence.
DR GO; GO:0019164; F:pyruvate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR CDD; cd03376; TPP_PFOR_porB_like; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR PANTHER; PTHR42897; PYRUVATE SYNTHASE SUBUNIT PORB; 1.
DR PANTHER; PTHR42897:SF2; PYRUVATE SYNTHASE SUBUNIT PORB; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:KZX15468.1}; Pyruvate {ECO:0000313|EMBL:KZX15468.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000077275}.
FT DOMAIN 42..203
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT REGION 137..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..152
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 288 AA; 31235 MW; A235B048B836B016 CRC64;
MKIPEEELFA PGHRGCAGCG ATIGVRLALK VLGKNTVAIS ATGCLEVIST PFPETAWEIP
WIHVAFENAG AVASGVERAL KAQGKEDVNV VAFGGDGGTA DIGMQSLSGA MERGHNLIYI
CYDNEAYMNT GIQRSGSTPY GASTTTSPHG TESFGEDRPK KNMPLIIAAH GVPYVATASI
SYPEDFMKKV KKAAETNGPA YIHLNQPCTT GWGYDPSKTI ELGRLAVETG SWSLYEIVEG
EFKLTYKPQI RKPVNEYLNA QKRFKHLSDE EKEKIQEYVD KQCAELGI
//