ID   A0A2C8ZUS8_9MICO        Unreviewed;       342 AA.
AC   A0A2C8ZUS8;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 13.
DE   RecName: Full=Pyruvate dehydrogenase E1 component subunit beta {ECO:0000256|ARBA:ARBA00016138};
GN   ORFNames=SAMN06296378_1985 {ECO:0000313|EMBL:SOE69482.1};
OS   Salinibacterium xinjiangense.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Salinibacterium.
OX   NCBI_TaxID=386302 {ECO:0000313|EMBL:SOE69482.1, ECO:0000313|Proteomes:UP000219440};
RN   [1] {ECO:0000313|EMBL:SOE69482.1, ECO:0000313|Proteomes:UP000219440}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.05381 {ECO:0000313|EMBL:SOE69482.1,
RC   ECO:0000313|Proteomes:UP000219440};
RA   Ehlers B., Leendertz F.H.;
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall
CC       conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple
CC       copies of three enzymatic components: pyruvate dehydrogenase (E1),
CC       dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase
CC       (E3). {ECO:0000256|ARBA:ARBA00025211}.
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta chain.
CC       {ECO:0000256|ARBA:ARBA00011870}.
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DR   EMBL; OCST01000004; SOE69482.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2C8ZUS8; -.
DR   OrthoDB; 3457658at2; -.
DR   Proteomes; UP000219440; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
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; PTHR43257; PYRUVATE DEHYDROGENASE E1 COMPONENT BETA SUBUNIT; 1.
DR   PANTHER; PTHR43257:SF2; PYRUVATE DEHYDROGENASE E1 COMPONENT SUBUNIT BETA; 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:SOE69482.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000219440}.
FT   DOMAIN          4..185
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   342 AA;  36565 MW;  61FA9254669B9009 CRC64;
     MTVMSYLSAI GAAQREAMDA DDRVIIIGED VEANVYGTTG GGKSRSIEGD FLQRYGKNRI
     RNTPISEEGI VGAAAGAAMT GLRPIVDLSY SSFLYMAMDQ FVNQVAKNRY MFGGQASMPV
     VFRSAMFYGL NTGAHHSDRP YPMFMNVPGL KIIAPATPAD AKGLLRSAVD SDDPVLSFEA
     CLLWSTKEDV DEDEFWVPLG VARTAREGTD VTVVAISSSV PEAVAAAEEL AKEGVSVEVI
     DPRTLVPLDR NAILRSVAKT GRLVVAEPAH RTCGAAAEIS ALVAEEIFDS LRAPIIRVTA
     PDMQIPFSPS LEKQMYPTKA SIAAAIRRVV DLPALEPVAA AV
//