ID A0A1B7ZCX5_9FLAO Unreviewed; 803 AA.
AC A0A1B7ZCX5;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Pyruvate dehydrogenase E1 component subunit beta {ECO:0000256|ARBA:ARBA00016138};
GN ORFNames=A9200_14165 {ECO:0000313|EMBL:OBR40975.1};
OS Maribacter hydrothermalis.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Maribacter.
OX NCBI_TaxID=1836467 {ECO:0000313|EMBL:OBR40975.1, ECO:0000313|Proteomes:UP000092164};
RN [1] {ECO:0000313|Proteomes:UP000092164}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T28 {ECO:0000313|Proteomes:UP000092164};
RA Zhan P.;
RL Submitted (JUN-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}.
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:OBR40975.1}.
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DR EMBL; LZFP01000004; OBR40975.1; -; Genomic_DNA.
DR RefSeq; WP_068482964.1; NZ_LZFP01000004.1.
DR AlphaFoldDB; A0A1B7ZCX5; -.
DR STRING; 1836467.BTR34_15865; -.
DR KEGG; mart:BTR34_15865; -.
DR OrthoDB; 9769337at2; -.
DR Proteomes; UP000092164; 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; 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); 2.
DR SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000092164}.
FT DOMAIN 469..643
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 803 AA; 90069 MW; D315DE165330E710 CRC64;
MDVSSKTSND ISFDDFKEQI ISDYEIAFLS RTCSLLGRKE VLTGKAKFGI FGDGKELPQL
AMARSFKNGD FRSGYYRDQT FMMALGLLKP KDFFHALYAT TDIEKEPMSA GRQMGGHFLT
HSLNTDGSWK DLTKQKNSSA DISCTAGQMP RLLGLAQASK VYRNQKGLDS AKFSVNGNEI
AWGTIGNAST SEGMFFETIN AAGVLQVPMV ISIWDDEYGI SVPAKHHTTK EDISKVLKGF
QRTDDENGYE IFKVNGWDYT ALMHAYENAA DIARQEHVPV MIHVKELTQP QGHSTSGSHE
RYKDNNRLAW ERDNDCNKRF KEWILESGIA NNEELESIEK RIKRTVREAK KQAWEEYLEG
LLSAKNTLVS LIDQAAAKSP NKNFLNKLKN DLIATEEPIK KDLAISARKS LRFLLGETST
EKTALVNWTT NFLKESQDTY SKHLYSENEN KATNINAIAP IFKDDAEEVD GRVILRDNFD
KLFEKYPNTL IFGEDTGAIG DVNQGLEGMQ EKYGDIRVSD TGIRETTIIG QGLGMALRGL
RPIAEIQYLD YIFYALPTLT DDLASLLYRT AGKQKAPLII RTRGHRLEGI WHSGSEMGGL
IHLLRGMYIL APRNMTQAAG FYNTLLKSDE PALVIESLNG YRLKEKKPSN LGEYCTPIGK
IETIKEGNDI TLVSYGSTLR IVEKAAKELL EVGIDAEIID AQTLLPFDIT KDVLESIKKT
NRLLVIDEDV PGGCSAYLLN EIIEKQGAFK YLDSPPQTLS AKAHRPAYGS DGDYFSKPNR
EDIFEKVYAI MHEVSPNDYP KLR
//