ID X5DTX4_9BACT Unreviewed; 822 AA.
AC X5DTX4;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE RecName: Full=Pyruvate dehydrogenase E1 component subunit beta {ECO:0000256|ARBA:ARBA00016138};
GN ORFNames=SAMN05444285_11023 {ECO:0000313|EMBL:SET30686.1};
OS Draconibacterium orientale.
OC Bacteria; Bacteroidota; Bacteroidia; Marinilabiliales; Prolixibacteraceae;
OC Draconibacterium.
OX NCBI_TaxID=1168034 {ECO:0000313|EMBL:SET30686.1, ECO:0000313|Proteomes:UP000181981};
RN [1] {ECO:0000313|EMBL:SET30686.1, ECO:0000313|Proteomes:UP000181981}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25947 {ECO:0000313|EMBL:SET30686.1,
RC ECO:0000313|Proteomes:UP000181981};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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 -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
CC -!- SUBUNIT: Heterodimer of an alpha and a beta chain.
CC {ECO:0000256|ARBA:ARBA00011870}.
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DR EMBL; FOHT01000010; SET30686.1; -; Genomic_DNA.
DR RefSeq; WP_038554418.1; NZ_FOHT01000010.1.
DR AlphaFoldDB; X5DTX4; -.
DR STRING; 1168034.FH5T_01000; -.
DR GeneID; 78099321; -.
DR eggNOG; COG0022; Bacteria.
DR eggNOG; COG1071; Bacteria.
DR HOGENOM; CLU_012907_2_1_10; -.
DR OrthoDB; 9769337at2; -.
DR Proteomes; UP000181981; Unassembled WGS sequence.
DR GO; GO:0016624; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor; IEA:InterPro.
DR CDD; cd02000; TPP_E1_PDC_ADC_BCADC; 1.
DR Gene3D; 3.40.50.920; -; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR InterPro; IPR001017; DH_E1.
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; PF00676; E1_dh; 2.
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); 2.
DR SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 475..648
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 822 AA; 91649 MW; D8F0C396C3AEA349 CRC64;
MPKSQFIDPV EVRKPGSIQF KEIPVNQYNK SIEEEKANFS NEEFVDIFHD MALIREFETM
LNLIKTKGEY EGIEYNHPGP AHLSIGQESA AVGMAYHLGV EDFIFGSHRS HGEILAKGMS
AIHNMSDDEL MDVMTNFFDG TILNIVKEGH EGNVKSLARR FLIYGTLAEI FARETGFNKG
LGGSMHAFFT PFGVYPNNAI VGGSGDIAVG AALFKKVNKK EGIVVANIGD ASMACGPVWE
GLAFASMDQF EQLWEGAYKG GLPIIFNIMN NQYGMGGQTC GETMGYDIAA RIGAGVNRDS
MHAERVDGYN PLAVIDAYKR KMELLKNKKG PVLLDVLTYR YSGHSPSDAS SYRSKEEVEA
WEKQDCIASY ASELVGAGVA KEAELADIKA DIVELMKYAM KLAIDDKVSP HMDMEKYPEL
IGDMMFSNES LDKMEDREVE VNHPMEENPR VQQLAKKERF AFDANGKPFS KIKQYQLRDG
IFEAVVDRFY KDPTLVAYGE ENRDWGGAFA VYRGLTEALP YNRLFNSPIS EASIIGTAIG
YAMCGGRVIP EIMYCDFLGR CGDEVFNQMP KWQAMSGNVI KMPVVVRVSV GSKYGAQHSQ
DWTSLVAHIP GLKVVFPVTP YDAKGLMNTA LQGTDPVIFF ESQRIYDIGE QFHEGGVPEG
YYEIPFGEPD VKREGKDITI LTIGATLYRA LEAADKLKEE YGMEAEVIDA RSIVPFNYEK
VLESVKKTGR IIISGDANSR GSFLNDMARN ITELAFDDLD APPVVVGSRN WITPAHELEK
YFFPQVDWFL DAIHEKIVPL KKHVVKNNYT NAEQIRRNKL GI
//
