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Database: UniProt
Entry: R5E6Z7_9BURK
LinkDB: R5E6Z7_9BURK
Original site: R5E6Z7_9BURK 
ID   R5E6Z7_9BURK            Unreviewed;       353 AA.
AC   R5E6Z7;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Thiamine pyrophosphate enzyme TPP binding domain protein {ECO:0000313|EMBL:CCX88278.1};
GN   ORFNames=BN548_00053 {ECO:0000313|EMBL:CCX88278.1};
OS   Parasutterella excrementihominis CAG:233.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Sutterellaceae; Parasutterella.
OX   NCBI_TaxID=1263099 {ECO:0000313|EMBL:CCX88278.1, ECO:0000313|Proteomes:UP000018034};
RN   [1] {ECO:0000313|EMBL:CCX88278.1, ECO:0000313|Proteomes:UP000018034}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:233 {ECO:0000313|Proteomes:UP000018034};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) 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:CCX88278.1}.
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DR   EMBL; CAXE010000209; CCX88278.1; -; Genomic_DNA.
DR   AlphaFoldDB; R5E6Z7; -.
DR   Proteomes; UP000018034; Unassembled WGS sequence.
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}.
FT   DOMAIN          75..242
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   353 AA;  38323 MW;  612E0D313359FFA3 CRC64;
     MSEHQIKFYQ TGTFTVGNRL LQPDQRSGQA NIERYNSLNS GHRACQGCGE ALGARYAVDA
     AMRATEGRLI AANATGCLEV FSTPYPETSW QLPWFHSLFG NTAAVGSGMA AVARVKAKKS
     GKPLVRVIAQ GGDGGTTDIG FGCLSGMFER NDDVLYICYD NEGYMNTGVQ RSSATPPAVR
     TATTQIVGKH PGNAFGQGKD VPLIAMAHGI PYVATATIAD LRDLERKVAK AMTFHGARYI
     HILVPCPLGW GAKSADTVKL ARLAVETGLF PVFESEYGEI TKVTKIRQLQ PVENYMKLQK
     RYAHLFGPKG DADAFARIQA IAQRNIRRFG LLGEEEPEII PPSVQADERA DKV
//
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