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Database: UniProt
Entry: A8F582_PSELT
LinkDB: A8F582_PSELT
Original site: A8F582_PSELT 
ID   A8F582_PSELT            Unreviewed;       274 AA.
AC   A8F582;
DT   13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2007, sequence version 1.
DT   27-MAR-2024, entry version 67.
DE   SubName: Full=Thiamine pyrophosphate protein domain protein TPP-binding {ECO:0000313|EMBL:ABV33316.1};
GN   OrderedLocusNames=Tlet_0750 {ECO:0000313|EMBL:ABV33316.1};
OS   Pseudothermotoga lettingae (strain ATCC BAA-301 / DSM 14385 / NBRC 107922 /
OS   TMO) (Thermotoga lettingae).
OC   Bacteria; Thermotogota; Thermotogae; Thermotogales; Thermotogaceae;
OC   Pseudothermotoga.
OX   NCBI_TaxID=416591 {ECO:0000313|EMBL:ABV33316.1, ECO:0000313|Proteomes:UP000002016};
RN   [1] {ECO:0000313|EMBL:ABV33316.1, ECO:0000313|Proteomes:UP000002016}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-301 / DSM 14385 / NBRC 107922 / TMO
RC   {ECO:0000313|Proteomes:UP000002016};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Foster B., Bruce D., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Nelson K., Gogarten J.P., Noll K.,
RA   Richardson P.;
RT   "Complete sequence of Thermotoga lettingae TMO.";
RL   Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ABV33316.1, ECO:0000313|Proteomes:UP000002016}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-301 / DSM 14385 / NBRC 107922 / TMO
RC   {ECO:0000313|Proteomes:UP000002016};
RX   PubMed=19307556; DOI=10.1073/pnas.0901260106;
RA   Zhaxybayeva O., Swithers K.S., Lapierre P., Fournier G.P., Bickhart D.M.,
RA   DeBoy R.T., Nelson K.E., Nesbo C.L., Doolittle W.F., Gogarten J.P.,
RA   Noll K.M.;
RT   "On the chimeric nature, thermophilic origin, and phylogenetic placement of
RT   the Thermotogales.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:5865-5870(2009).
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DR   EMBL; CP000812; ABV33316.1; -; Genomic_DNA.
DR   AlphaFoldDB; A8F582; -.
DR   STRING; 416591.Tlet_0750; -.
DR   KEGG; tle:Tlet_0750; -.
DR   eggNOG; COG1013; Bacteria.
DR   HOGENOM; CLU_048564_2_0_0; -.
DR   Proteomes; UP000002016; Chromosome.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   CDD; cd03375; TPP_OGFOR; 1.
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:SF1; 2-OXOGLUTARATE SYNTHASE SUBUNIT KORB; 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:UP000002016}.
FT   DOMAIN          55..201
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   274 AA;  30441 MW;  354885942F0C724E CRC64;
     MNFLKVERLI PYLREGRWPT IWCPGCGNGI ILKAFLEAVD ELKIRRDRMA VVSGIGCSSR
     ATGYIDFNTL HTLHGRAIAF ATGVKLAKPD FKVAVLGGDG DILAIGGNHF LHACRRNIDL
     TIVVFNNMIY GMTGGQNSPT TPLEKVASTA PFGNIEKPLD VVKVATAAGA TYVARATVYH
     YPLLVRYIMK ALKHRGTSVV EAVTNCHTYY GRYNKIPNAA KMLEYFKNNS VMLDKSKNMS
     PEELENKIVI GEFHEEDKPT FHDLYKKIAA KFIS
//
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