ID   A0A1G8WR70_9EURY        Unreviewed;       355 AA.
AC   A0A1G8WR70;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   SubName: Full=Pyruvate dehydrogenase E1 component beta subunit {ECO:0000313|EMBL:SDJ80100.1};
GN   ORFNames=SAMN05216226_109133 {ECO:0000313|EMBL:SDJ80100.1};
OS   Halovenus aranensis.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haloarculaceae; Halovenus.
OX   NCBI_TaxID=890420 {ECO:0000313|EMBL:SDJ80100.1, ECO:0000313|Proteomes:UP000198856};
RN   [1] {ECO:0000313|EMBL:SDJ80100.1, ECO:0000313|Proteomes:UP000198856}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBRC-M10015 {ECO:0000313|EMBL:SDJ80100.1,
RC   ECO:0000313|Proteomes:UP000198856};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
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DR   EMBL; FNFC01000009; SDJ80100.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G8WR70; -.
DR   STRING; 890420.SAMN05216226_109133; -.
DR   OrthoDB; 6779at2157; -.
DR   Proteomes; UP000198856; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0006082; P:organic acid metabolic process; IEA:UniProt.
DR   GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR   GO; GO:0044272; P:sulfur compound biosynthetic process; IEA:UniProt.
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:SDJ80100.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198856}.
FT   DOMAIN          34..209
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
FT   REGION          1..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        15..29
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   355 AA;  39105 MW;  987A5B1B7C4BFD6E CRC64;
     MSSYAETLAE NVEEQSEEPT QRETPEESDS VDELTLVEAI CDGLHTEMSQ DERVMMLGED
     IGRNGGVFRA TDALYEEFGD DRVVDTPLAE SGIIGASIGL ALSGMRPVGE IQFMGFLYPG
     FDQLVSHASR LRSRTHGQLN LPMVVRMPYG GGIRAPEHHS ESKEAFFVHE PGLKVVTPST
     PYDAKGLLTA AIRDPDPVMF LEPKLIYRAF REEVPERSYE IDLGEAAVRR EGTDISVFTW
     GAMTRPSLIA AEELAEEGID CEVVDLRSLS PLDFDTIIDS FEKTGRGAIV HEAPKTGGLG
     AEIAATIQEE ALMYQEAPIK RIAGYDAHIP LHALEDYYLP QAVRIQDGIR EAMAF
//