ID A0A084TM67_9FLAO Unreviewed; 325 AA.
AC A0A084TM67;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=Pyruvate dehydrogenase E1 component subunit beta {ECO:0000256|ARBA:ARBA00016138};
GN ORFNames=IA57_02705 {ECO:0000313|EMBL:KFB01803.1};
OS Mangrovimonas yunxiaonensis.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Mangrovimonas.
OX NCBI_TaxID=1197477 {ECO:0000313|EMBL:KFB01803.1, ECO:0000313|Proteomes:UP000028521};
RN [1] {ECO:0000313|EMBL:KFB01803.1, ECO:0000313|Proteomes:UP000028521}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LY01 {ECO:0000313|EMBL:KFB01803.1,
RC ECO:0000313|Proteomes:UP000028521};
RX PubMed=25428978;
RA Li Y., Zhu H., Li C., Zhang H., Chen Z., Zheng W., Xu H., Zheng T.;
RT "Draft Genome Sequence of the Algicidal Bacterium Mangrovimonas
RT yunxiaonensis Strain LY01.";
RL Genome Announc. 2:0-0(2014).
RN [2] {ECO:0000313|Proteomes:UP000028521}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LY01 {ECO:0000313|Proteomes:UP000028521};
RA Li Y., Zheng T.;
RT "Genome sequence of Mangrovimonas yunxiaonensis.";
RL Submitted (JUL-2014) 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:KFB01803.1}.
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DR EMBL; JPFK01000003; KFB01803.1; -; Genomic_DNA.
DR RefSeq; WP_036118947.1; NZ_JPFK01000003.1.
DR AlphaFoldDB; A0A084TM67; -.
DR STRING; 1197477.IA57_02705; -.
DR eggNOG; COG0022; Bacteria.
DR OrthoDB; 9771835at2; -.
DR Proteomes; UP000028521; Unassembled WGS sequence.
DR GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IEA:UniProtKB-EC.
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:KFB01803.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000028521}.
FT DOMAIN 4..179
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 325 AA; 35878 MW; 87468B4B6D7BF352 CRC64;
MKTIQFREAV AEAMSEEMRR DESIYLMGEE VAEYNGAYKA SKGMLDEFGP KRVIDTPIAE
LGFAGIGVGS AMNGNRPIIE FMTFNFSLVG IDQIINNAAK IRQMSGGQFN CPIVFRGPTA
SAGQLAATHS QAFESWYANC PGLKVVVPSN PYDAKGLLKS AIRDDDPVIF MESEQMYGDK
GEVPEGEYLI PLGVADIKRK GDDVTIVSFG KIIKEAYKAA DELEKEGVSC EIIDLRTVRP
MDHDAILNSV KKTNRLVILE EAWPFGNIAT EITYQVQSQA FDYLDAPIEK INTADTPAPY
SPVLLEEWLP NSNDVVKAVK KVLYK
//
