ID F4LR63_TEPAE Unreviewed; 310 AA.
AC F4LR63; L0S1Q0;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE SubName: Full=Putative transketolase C-terminal section {ECO:0000313|EMBL:CCP27086.1};
DE EC=2.2.1.1 {ECO:0000313|EMBL:CCP27086.1};
GN OrderedLocusNames=TEPIRE1_2251 {ECO:0000313|EMBL:CCP27086.1};
OS Tepidanaerobacter acetatoxydans (strain DSM 21804 / JCM 16047 / Re1).
OC Bacteria; Bacillota; Clostridia; Thermosediminibacterales;
OC Tepidanaerobacteraceae; Tepidanaerobacter.
OX NCBI_TaxID=1209989 {ECO:0000313|EMBL:CCP27086.1, ECO:0000313|Proteomes:UP000010802};
RN [1] {ECO:0000313|Proteomes:UP000010802}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Re1 {ECO:0000313|Proteomes:UP000010802};
RX PubMed=23469343; DOI=10.1128/genomeA.00213-12;
RA Manzoor S., Bongcam-Rudloff E., Schnurer A., Muller B.;
RT "First genome sequence of a syntrophic acetate-oxidizing bacterium,
RT Tepidanaerobacter acetatoxydans strain Re1.";
RL Genome Announc. 1:E00213-E00213(2013).
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DR EMBL; HF563609; CCP27086.1; -; Genomic_DNA.
DR RefSeq; WP_013779136.1; NC_019954.2.
DR AlphaFoldDB; F4LR63; -.
DR STRING; 1209989.TepRe1_2091; -.
DR KEGG; tae:TepiRe1_2251; -.
DR KEGG; tep:TepRe1_2091; -.
DR PATRIC; fig|1209989.3.peg.2592; -.
DR eggNOG; COG3958; Bacteria.
DR HOGENOM; CLU_009227_1_1_9; -.
DR OrthoDB; 9803371at2; -.
DR Proteomes; UP000010802; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004802; F:transketolase activity; IEA:UniProtKB-EC.
DR CDD; cd07033; TPP_PYR_DXS_TK_like; 1.
DR Gene3D; 3.40.50.920; -; 1.
DR Gene3D; 3.40.50.970; -; 1.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR009014; Transketo_C/PFOR_II.
DR InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR InterPro; IPR020826; Transketolase_BS.
DR InterPro; IPR033248; Transketolase_C.
DR PANTHER; PTHR43825; PYRUVATE DEHYDROGENASE E1 COMPONENT; 1.
DR PANTHER; PTHR43825:SF1; TRANSKETOLASE-LIKE PYRIMIDINE-BINDING DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF02779; Transket_pyr; 1.
DR Pfam; PF02780; Transketolase_C; 1.
DR SMART; SM00861; Transket_pyr; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
DR SUPFAM; SSF52922; TK C-terminal domain-like; 1.
DR PROSITE; PS00802; TRANSKETOLASE_2; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000010802};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CCP27086.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 59..81
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 5..170
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 310 AA; 33382 MW; C394E76F33E34A86 CRC64;
MTNMKSPRIA YGEALVELGL KNKQVVVLDA DLAHATQTVI FSEKFKDRFF NMGIAEQNMI
GVAAGLALSG FIPFASTFAI FGAGRAFEQI RNTVCYPNLN VKIAVTHAGI TVGEDGASHQ
AIEDISLMRS IPNMKVVVPC DAIETKKAIF AAAKIHGPVY IRIARPVAPI ITEENTDFKI
GKAQILRKGK DLSIFATGLM VDKAMKAANV LYGKGIETTV VNIHTIKPLD EELVLSEAAN
TGKVITVEEH SIIGGLGSAI AETLIGRLPV KMKRIGLNDT FGQSGNPNAL MEYYGLTVEN
IVKTVNEILN
//
