ID W0FR18_9BACT Unreviewed; 309 AA.
AC W0FR18;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 12.
DE SubName: Full=Pyruvate synthase subunit porB {ECO:0000313|EMBL:AHF25919.1};
OS uncultured bacterium Contigcl_1539.
OC Bacteria; environmental samples.
OX NCBI_TaxID=1393650 {ECO:0000313|EMBL:AHF25919.1};
RN [1] {ECO:0000313|EMBL:AHF25919.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=24223817;
RA Wang L., Hatem A., Catalyurek U.V., Morrison M., Yu Z.;
RT "Metagenomic insights into the carbohydrate-active enzymes carried by the
RT microorganisms adhering to solid digesta in the rumen of cows.";
RL PLoS ONE 8:E78507-E78507(2013).
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DR EMBL; KC246858; AHF25919.1; -; Genomic_DNA.
DR AlphaFoldDB; W0FR18; -.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR CDD; cd03376; TPP_PFOR_porB_like; 1.
DR Gene3D; 3.40.50.970; -; 1.
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 Pyruvate {ECO:0000313|EMBL:AHF25919.1}.
FT DOMAIN 59..218
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 309 AA; 34639 MW; 4ACBCDFEB5B5966F CRC64;
MAYNLKQEMS KKERFEAGHR LCAGCGAGIV CRAMMRAVDP EDQAVICNAT SCLEVSSFQY
PYTAWHDSYI HSAFENTAAT AAGVESAYVA LKRRGKIDGN VKILAIGGDG GTYDIGFQSL
SGAMERGHDF TYFCYDNEAY MNTGTQRSSA TPRFASATTT PSGVESVGKK QNQKDLTQIM
VAHGSPYVAQ TTMIGTFQDF HEKAHKAIYT EGPTFVNVLT PCPRGWQYPA EILPEICKKA
VDTCIWPLYE VEEGEYHLTY KPKNKLSVEE FMKLQGRFKH CFQPGNEWTI EEAQNYVDRK
WEELLEKCN
//
