ID A0A0R0MNW9_9BURK Unreviewed; 346 AA.
AC A0A0R0MNW9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Pyruvate dehydrogenase E1 component subunit beta {ECO:0000256|ARBA:ARBA00016138};
GN ORFNames=AO057_12590 {ECO:0000313|EMBL:KRI00696.1};
OS Curvibacter sp. PAE-UM.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Curvibacter.
OX NCBI_TaxID=1714344 {ECO:0000313|EMBL:KRI00696.1, ECO:0000313|Proteomes:UP000051912};
RN [1] {ECO:0000313|EMBL:KRI00696.1, ECO:0000313|Proteomes:UP000051912}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PAE-UM {ECO:0000313|EMBL:KRI00696.1,
RC ECO:0000313|Proteomes:UP000051912};
RA Ma D.;
RT "The whole genome sequence of a typical ultramicrobacteria PAE-UM from
RT river sediment.";
RL Submitted (SEP-2015) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRI00696.1}.
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DR EMBL; LKCX01000017; KRI00696.1; -; Genomic_DNA.
DR RefSeq; WP_057676272.1; NZ_KQ483358.1.
DR AlphaFoldDB; A0A0R0MNW9; -.
DR STRING; 1714344.AO057_12590; -.
DR OrthoDB; 9780894at2; -.
DR Proteomes; UP000051912; Unassembled WGS sequence.
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; 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:KRI00696.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051912}.
FT DOMAIN 7..182
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 346 AA; 37232 MW; 912D69ED348E910F CRC64;
MTTTRKLTMA QAIAEAIGQE MERDNKVFVM GEDIGKYGGI FGATGGLLDK FGPERIMDTP
ISETAFIGTA TGAAAAGLRP IAELMFVDFF GVCMDQIYNH LAKNTYMAGG NIKLPVVLTT
AIGGGYNDAA QHSQCLYATF AHMPGLKVVV PSNAYDAKGL MTQAIRDDNP VLFMYHKGIM
GLPWMAYFEG SSNEVPQEQY TIPFGVAKVV REGSDLTIVT LSQMVQKSLL AAEELKKQGI
SAEVLDLRTL VPLDRKAVLK SVAKTGRLLV ADEDYLSFGL TGEIAALVAE NLDTVVLKAP
VKRLAVPDVP IPYSRPLEKF VIPQVENIVA ASQALMKGRV AEGQPA
//
