ID Q67SE6_SYMTH Unreviewed; 326 AA.
AC Q67SE6;
DT 11-OCT-2004, integrated into UniProtKB/TrEMBL.
DT 11-OCT-2004, sequence version 1.
DT 27-MAR-2024, entry version 96.
DE SubName: Full=Pyruvate dehydrogenase E1 beta subunit {ECO:0000313|EMBL:BAD39397.1};
GN OrderedLocusNames=STH412 {ECO:0000313|EMBL:BAD39397.1};
OS Symbiobacterium thermophilum (strain T / IAM 14863).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Symbiobacteriaceae;
OC Symbiobacterium.
OX NCBI_TaxID=292459 {ECO:0000313|EMBL:BAD39397.1, ECO:0000313|Proteomes:UP000000417};
RN [1] {ECO:0000313|EMBL:BAD39397.1, ECO:0000313|Proteomes:UP000000417}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T / IAM 14863 {ECO:0000313|Proteomes:UP000000417};
RX PubMed=15383646; DOI=10.1093/nar/gkh830;
RA Ueda K., Yamashita A., Ishikawa J., Shimada M., Watsuji T., Morimura K.,
RA Ikeda H., Hattori M., Beppu T.;
RT "Genome sequence of Symbiobacterium thermophilum, an uncultivable bacterium
RT that depends on microbial commensalism.";
RL Nucleic Acids Res. 32:4937-4944(2004).
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
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DR EMBL; AP006840; BAD39397.1; -; Genomic_DNA.
DR RefSeq; WP_011194546.1; NC_006177.1.
DR AlphaFoldDB; Q67SE6; -.
DR STRING; 292459.STH412; -.
DR KEGG; sth:STH412; -.
DR eggNOG; COG0022; Bacteria.
DR HOGENOM; CLU_012907_1_0_9; -.
DR OrthoDB; 8732661at2; -.
DR Proteomes; UP000000417; Chromosome.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR CDD; cd07036; TPP_PYR_E1-PDHc-beta_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; IPR033248; Transketolase_C.
DR PANTHER; PTHR42980:SF1; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT BETA, MITOCHONDRIAL; 1.
DR PANTHER; PTHR42980; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT BETA-RELATED; 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.
PE 4: Predicted;
KW Pyruvate {ECO:0000313|EMBL:BAD39397.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000417}.
FT DOMAIN 4..179
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 326 AA; 35555 MW; EE0EA68DE7E2E6CB CRC64;
MAKLTLIQAI NDALRVAMRQ DSTIVLLGED IGINGGVFRA TDGLIQEFGP ERVIDCPLAE
SGYIGAAIGM AVNGLKPVAE VQFDGFLAPA HEQVANHLSR IRHRSRGRFT CPMVIRIPSW
GGIKALEHHS ESIENWYLNI PGLKMVAPSN PYDAKGLLLA AIADPDPVLY MEPKRLYRAF
RAEVPEGYYT VPLGQAAVVR EGTDMTVLTY GVHVHTALEA AEQAASQYGW QAEVIDLRSL
NPLDLDTIIG SVKKTGRAVV VSEAPRTGGF HSELVALIND HALEYLEAPV ARVTGFDVPM
PYLLSEDLYI PDAGRVLEAM QAVRTY
//
