ID A0A061PH36_9BACL Unreviewed; 325 AA.
AC A0A061PH36;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Pyruvate dehydrogenase E1 component subunit beta {ECO:0000256|ARBA:ARBA00016138};
DE EC=1.2.4.1 {ECO:0000256|ARBA:ARBA00012281};
GN ORFNames=JCM19039_4107 {ECO:0000313|EMBL:GAK14206.1};
OS Geomicrobium sp. JCM 19039.
OC Bacteria; Bacillota; Bacilli; Bacillales; Geomicrobium.
OX NCBI_TaxID=1460636 {ECO:0000313|EMBL:GAK14206.1, ECO:0000313|Proteomes:UP000027177};
RN [1] {ECO:0000313|EMBL:GAK14206.1, ECO:0000313|Proteomes:UP000027177}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 19039 {ECO:0000313|EMBL:GAK14206.1,
RC ECO:0000313|Proteomes:UP000027177};
RA Kudo T., Nakahara T., Zhang X., Taniyama S., Arakawa O., Murase S.,
RA Nakata H., Oshima K., Suda W., Kitamura K., Iida T., Oshida Y., Inoue T.,
RA Hongoh Y., Hattori M., Ohkuma M.;
RT "Draft Genome Sequences of Geomicrobium sp. Strains JCM 19037, JCM 19038,
RT JCM 19039, and JCM 19055, Isolated from Aquatic Samples.";
RL Genome Announc. 2:e00622-14(2014).
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}.
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:GAK14206.1}.
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DR EMBL; BAXB01000028; GAK14206.1; -; Genomic_DNA.
DR RefSeq; WP_042430057.1; NZ_BAXB01000028.1.
DR AlphaFoldDB; A0A061PH36; -.
DR OrthoDB; 9771835at2; -.
DR Proteomes; UP000027177; 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:GAK14206.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000027177}.
FT DOMAIN 4..179
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 325 AA; 35388 MW; 9AB4DE56686F0279 CRC64;
MAEMTMIQAI TEAMRTELKN DENVLLFGED VGHYGGVFRA TSGLQEEFGE DRVFDTPLAE
SGIGGLAIGL GLTGFRPIME IQFFGFLFEV MDGVAGQMSR THYRSGGHYS SPITIRAPFG
GGVKTPELHS DSLEGLIAQT PGISVVIPST PYDAKGLLIS AIRSNDPVVF LEHMKLYRSF
KGEVPDEEYT IEIGKADIKR EGTDITIVSY GAMVHEALKA ADKLAEEDIN AEVIDLRTVS
PLDLETIIES VKKTNRAMVV QEAQRQAGVA ATVSAEISER AILHLEAPVG RIAAPDTVYA
FASDEDAWLP NAEDIYEKAK ETIEF
//
