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Database: UniProt
Entry: A0A0M9UBK4_9CHLR
LinkDB: A0A0M9UBK4_9CHLR
Original site: A0A0M9UBK4_9CHLR 
ID   A0A0M9UBK4_9CHLR        Unreviewed;       661 AA.
AC   A0A0M9UBK4;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=Pyruvate dehydrogenase E1 component subunit beta {ECO:0000256|ARBA:ARBA00016138};
GN   Name=bkdA {ECO:0000313|EMBL:GAP61937.1};
GN   ORFNames=ARMA_0360 {ECO:0000313|EMBL:GAP61937.1}, SE16_05695
GN   {ECO:0000313|EMBL:KPL88322.1};
OS   Ardenticatena maritima.
OC   Bacteria; Chloroflexota; Ardenticatenia; Ardenticatenales;
OC   Ardenticatenaceae; Ardenticatena.
OX   NCBI_TaxID=872965 {ECO:0000313|EMBL:GAP61937.1, ECO:0000313|Proteomes:UP000037784};
RN   [1] {ECO:0000313|EMBL:GAP61937.1, ECO:0000313|Proteomes:UP000037784}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=110S {ECO:0000313|EMBL:GAP61937.1,
RC   ECO:0000313|Proteomes:UP000037784};
RA   Kawaichi S., Yoshida T., Sako Y., Nakamura R.;
RT   "Draft Genome Sequence of a Heterotrophic Facultative Anaerobic
RT   Thermophilic Bacterium, Ardenticatena maritima Strain 110ST.";
RL   Genome Announc. 3:e01145-15(2015).
RN   [2] {ECO:0000313|EMBL:KPL88322.1, ECO:0000313|Proteomes:UP000050502}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=110S {ECO:0000313|EMBL:KPL88322.1,
RC   ECO:0000313|Proteomes:UP000050502};
RA   Hemp J., Ward L.M., Pace L.A., Fischer W.W.;
RT   "Whole genome sequence of Ardenticatena maritima DSM 23922.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Proteomes:UP000037784}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=110S {ECO:0000313|Proteomes:UP000037784};
RA   Kawaichi S., Yoshida T., Sako Y., Nakamura R.;
RT   "Draft Genome Sequence of a Heterotrophic Facultative Anaerobic Bacterium
RT   Ardenticatena maritima Strain 110S.";
RL   Submitted (AUG-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   -!- 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:GAP61937.1}.
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DR   EMBL; BBZA01000021; GAP61937.1; -; Genomic_DNA.
DR   EMBL; LGKN01000004; KPL88322.1; -; Genomic_DNA.
DR   RefSeq; WP_054491868.1; NZ_BBZA01000021.1.
DR   AlphaFoldDB; A0A0M9UBK4; -.
DR   STRING; 872965.SE16_05695; -.
DR   PATRIC; fig|872965.6.peg.1165; -.
DR   InParanoid; A0A0M9UBK4; -.
DR   OrthoDB; 8732661at2; -.
DR   Proteomes; UP000037784; Unassembled WGS sequence.
DR   Proteomes; UP000050502; Unassembled WGS sequence.
DR   GO; GO:0003863; F:3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) activity; IEA:UniProtKB-EC.
DR   CDD; cd02000; TPP_E1_PDC_ADC_BCADC; 1.
DR   CDD; cd07036; TPP_PYR_E1-PDHc-beta_like; 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   ECO:0000313|EMBL:GAP61937.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037784}.
FT   DOMAIN          339..515
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   661 AA;  72291 MW;  AE42E425A3735671 CRC64;
     MTLLQEDALQ MYTYMLKMRM IEERASALYR EANSPIVGRI YTGRGQEAIS VGAAYALEKD
     DVIAPLYRDL GANLVRGITT REVFCQYMGR ANSHNRGKDS GIHFGDRERG IVSMVSNLTA
     SVPVATGVAL GFVYRQEPRV VMTFFGDGST AHGSWHEGVN MAAAQRLPVV FVLENNQWAL
     STPTHKHTAL RELADRAKGY GMPGVRVDGN DVLAVYEAAR EAVARARAGE GPTLIEAVTM
     RMEGHSITDP AQYVPREMLE EWAARDPIAR FEAFLREQGW LDDETAARIR REIADEIEEA
     VQFALNSPEP RPEEALTDVF APANVPEVRP PASAARSTMS YRAAIRDAIF TAFARDERVF
     LMGEDVSYGG VYGISKDLAE TFGERRVIDT PIAEAAIVGA ATGAALFGLR PIAEIQFADF
     IAPAMDILVN MTAKYHYRTR WPVPLVIRTP AGAIIESHGS TGPFHSQSPE AWFAHTPGLK
     IVVPSTPYDA KGLLLAALED PNPVLYFEQK ALYNLRGEVP EGYYTVPLGK AAVRREGDDL
     SIITYGALVA EALKAAEMLA AEGISVEVLD LRTLVPLDEE AVLATVRKTG KVLVAYEANM
     TCGFGAEVAT RIWEHAFEWL DAPLVRVSAP DTPTPSAPQL ARFWYPDAGK IAAAARDLAA
     Y
//
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