ID A7HJ31_FERNB Unreviewed; 273 AA.
AC A7HJ31;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE SubName: Full=Thiamine pyrophosphate protein domain protein TPP-binding {ECO:0000313|EMBL:ABS59914.1};
GN OrderedLocusNames=Fnod_0043 {ECO:0000313|EMBL:ABS59914.1};
OS Fervidobacterium nodosum (strain ATCC 35602 / DSM 5306 / Rt17-B1).
OC Bacteria; Thermotogota; Thermotogae; Thermotogales; Fervidobacteriaceae;
OC Fervidobacterium.
OX NCBI_TaxID=381764 {ECO:0000313|EMBL:ABS59914.1, ECO:0000313|Proteomes:UP000002415};
RN [1] {ECO:0000313|EMBL:ABS59914.1, ECO:0000313|Proteomes:UP000002415}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35602 / DSM 5306 / Rt17-B1
RC {ECO:0000313|Proteomes:UP000002415};
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., Saunders E., Brettin T., Bruce D., Detter J.C.,
RA Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Nelson K., Gogarten J.P., Noll K., Richardson P.;
RT "Complete sequence of Fervidobacterium nodosum Rt17-B1.";
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ABS59914.1, ECO:0000313|Proteomes:UP000002415}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35602 / DSM 5306 / Rt17-B1
RC {ECO:0000313|Proteomes:UP000002415};
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).
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; CP000771; ABS59914.1; -; Genomic_DNA.
DR RefSeq; WP_011993237.1; NC_009718.1.
DR AlphaFoldDB; A7HJ31; -.
DR STRING; 381764.Fnod_0043; -.
DR KEGG; fno:Fnod_0043; -.
DR eggNOG; COG1013; Bacteria.
DR HOGENOM; CLU_048564_2_0_0; -.
DR OrthoDB; 9775140at2; -.
DR Proteomes; UP000002415; 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:UP000002415}.
FT DOMAIN 52..199
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 273 AA; 30608 MW; DF7A52EB153A17B7 CRC64;
MKRDKLAQYL RSDRWPTVWC PGCGNGIILK SFIDAFDQTG MKTEETAVIS GIGCSSRSTG
YLDFNTMHTL HGRAIAFATG VSLAKPDFKV VVMGGDGDIT AIGGNHFIHA CRRNINLTII
IYNNMIYGMT GGQHSPTTPG GKIAGTMPFG NVEEQFDIVK LALSAGATYV ARSTVYHYPL
TVKYIKEALL HKGVSVVEVM SNCHTYYGRY NGLREPWQMM DFFKENTIMK EKAEKMSEEE
LKGKIVIGVF RKDESKPDFY TRYRMTYARS DKK
//
