ID A0A0X3APG3_9FLAO Unreviewed; 326 AA.
AC A0A0X3APG3;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Pyruvate dehydrogenase E1 component subunit beta {ECO:0000256|ARBA:ARBA00016138};
GN ORFNames=Ga0061079_10582 {ECO:0000313|EMBL:CVK16123.1};
OS Apibacter mensalis.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Apibacter.
OX NCBI_TaxID=1586267 {ECO:0000313|EMBL:CVK16123.1, ECO:0000313|Proteomes:UP000182761};
RN [1] {ECO:0000313|EMBL:CVK16123.1, ECO:0000313|Proteomes:UP000182761}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R-53146 {ECO:0000313|EMBL:CVK16123.1,
RC ECO:0000313|Proteomes:UP000182761};
RA McClelland M., Jain A., Saraogi P., Mendelson R., Westerman R.,
RA SanMiguel P., Csonka L.;
RL Submitted (JAN-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 -!- SUBUNIT: Heterodimer of an alpha and a beta chain.
CC {ECO:0000256|ARBA:ARBA00011870}.
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DR EMBL; FCOR01000005; CVK16123.1; -; Genomic_DNA.
DR RefSeq; WP_055425333.1; NZ_LIVM01000005.1.
DR AlphaFoldDB; A0A0X3APG3; -.
DR STRING; 1586267.GCA_001418685_00967; -.
DR OrthoDB; 9771835at2; -.
DR Proteomes; UP000182761; Unassembled WGS sequence.
DR GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IEA:UniProtKB-UniRule.
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:CVK16123.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000182761}.
FT DOMAIN 4..179
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 326 AA; 36058 MW; 0248B29B19B221B0 CRC64;
MKEVQFRQAI CEAMSEEMRR DPSIYLIGEE VANYNGAYKA SKGMVDEFGA KRVIDSPIAE
SGFTGISVGA AMNGCRPIVE FMTFNFSLVA IDQIINNAAK IYQMTGGQWN VPIVFRGPTA
SAGQLGATHS QAFESWFANC PGLKVIVPSN PYDAKGLLKS AIRDNDPVIF MESEQMYGDK
MEIPEDEYLI PIGVADIKKP GSDVTIVSFG KIMKVALQAA AELEKEGINA EVIDLRTVRP
LDYDTVINSV KKTNRLVLLI EEWPFASIAS EVAYMVQQKA FDYLDAPIKR ITTADTSAPY
SSSLFSKWYP NMHQVITAVK DTLYKK
//
