GenomeNet

Database: UniProt
Entry: A0A011RMU5_9LACT
LinkDB: A0A011RMU5_9LACT
Original site: A0A011RMU5_9LACT 
ID   A0A011RMU5_9LACT        Unreviewed;       328 AA.
AC   A0A011RMU5;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=Branched-chain alpha-keto acid dehydrogenase, E1 component, beta subunit {ECO:0000313|EMBL:EXJ23233.1};
DE            EC=1.2.4.4 {ECO:0000313|EMBL:EXJ23233.1};
GN   ORFNames=ADIAL_1380 {ECO:0000313|EMBL:EXJ23233.1};
OS   Alkalibacterium sp. AK22.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC   Alkalibacterium.
OX   NCBI_TaxID=1229520 {ECO:0000313|EMBL:EXJ23233.1, ECO:0000313|Proteomes:UP000020164};
RN   [1] {ECO:0000313|EMBL:EXJ23233.1, ECO:0000313|Proteomes:UP000020164}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AK22 {ECO:0000313|Proteomes:UP000020164};
RA   Singh A., Pinnaka A.K.;
RL   Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
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:EXJ23233.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; JANL01000032; EXJ23233.1; -; Genomic_DNA.
DR   RefSeq; WP_034301671.1; NZ_JANL01000032.1.
DR   AlphaFoldDB; A0A011RMU5; -.
DR   STRING; 1229520.ADIAL_1380; -.
DR   PATRIC; fig|1229520.3.peg.1345; -.
DR   eggNOG; COG0022; Bacteria.
DR   OrthoDB; 9771835at2; -.
DR   Proteomes; UP000020164; Unassembled WGS sequence.
DR   GO; GO:0003863; F:3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-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; PTHR42980:SF1; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT BETA, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR42980; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT BETA-RELATED; 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   Oxidoreductase {ECO:0000313|EMBL:EXJ23233.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000020164}.
FT   DOMAIN          4..180
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   328 AA;  36047 MW;  22DE1BF8B515E0AE CRC64;
     MAMMTYLEAI KKGIEEEMAR DERVVIFGED VGGVKGGVFG VTKGLAEKFG EERCFNTPLT
     EGQIGGLAVG LGLVGYRPIG EFQFADYILP AVNQLISEAS RMRYRTKGDW TAPVVYRAPY
     GGGVRGGLYH SQSTEKVLFG QPGLRIVTPS SPHDAKGLIK AAIRCDDPVL FYEHKRLYRL
     LKEDVPEEDY TVPLDKANVV REGEDLTVIA YGMVLNHALK AAETLSEEGI EAEIVDVRSL
     YPLDKETLVK AAKKTGKVLL VTEDNLEGSI MSEISAVIAE EALFDLDAPI RRLAGPDSPS
     MPYAIALERA FLVDEDKVRT AMRELAEF
//
DBGET integrated database retrieval system