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Database: UniProt
Entry: R5B887_9BACT
LinkDB: R5B887_9BACT
Original site: R5B887_9BACT 
ID   R5B887_9BACT            Unreviewed;       257 AA.
AC   R5B887;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Thiamine pyrophosphate tpp-binding domaiN-containing protein {ECO:0000313|EMBL:CCX51840.1};
GN   ORFNames=BN689_01651 {ECO:0000313|EMBL:CCX51840.1};
OS   Alistipes sp. CAG:514.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae;
OC   Alistipes.
OX   NCBI_TaxID=1262696 {ECO:0000313|EMBL:CCX51840.1, ECO:0000313|Proteomes:UP000018254};
RN   [1] {ECO:0000313|EMBL:CCX51840.1, ECO:0000313|Proteomes:UP000018254}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:514 {ECO:0000313|Proteomes:UP000018254};
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:CCX51840.1}.
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DR   EMBL; CAWO010000062; CCX51840.1; -; Genomic_DNA.
DR   AlphaFoldDB; R5B887; -.
DR   STRING; 1262696.BN689_01651; -.
DR   Proteomes; UP000018254; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   Gene3D; 3.40.50.970; -; 1.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR   PANTHER; PTHR48084; 2-OXOGLUTARATE OXIDOREDUCTASE SUBUNIT KORB-RELATED; 1.
DR   PANTHER; PTHR48084:SF3; SUBUNIT OF PYRUVATE:FLAVODOXIN OXIDOREDUCTASE-RELATED; 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   Reference proteome {ECO:0000313|Proteomes:UP000018254}.
FT   DOMAIN          75..218
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   257 AA;  28390 MW;  FF12F5F5E7FF5E1C CRC64;
     MTREEIIEKG QVVYKKPTLL NDTPMHYCPG CSHGVVHKIV SEVIEEMGMT DKTIAISPVG
     CAVFAYKYID VDWEEAAHGR APALASATKR LWPDRLVFTY QGDGDLACIG TAETIHALNR
     GENITIIFIN NAIYGMTGGQ MAPTTLLGMK TATCPYGREV SLHGYPLKIT EIAATLDGTC
     YVTRQAVHTV AAINRTKKAI RKAFEYSMQG KGSNLVEVVS TCNSGWKMSP EKANKWMEEN
     MFEFYHLGDL KDKGVEL
//
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