ID D5HAP8_SALRM Unreviewed; 665 AA.
AC D5HAP8;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE SubName: Full=Pyruvate dehydrogenase beta subunit {ECO:0000313|EMBL:CBH25103.1};
DE EC=1.2.4.4 {ECO:0000313|EMBL:CBH25103.1};
GN Name=bkdA2 {ECO:0000313|EMBL:CBH25103.1};
GN OrderedLocusNames=SRM_02182 {ECO:0000313|EMBL:CBH25103.1};
OS Salinibacter ruber (strain M8).
OC Bacteria; Rhodothermota; Rhodothermia; Rhodothermales; Salinibacteraceae;
OC Salinibacter.
OX NCBI_TaxID=761659 {ECO:0000313|EMBL:CBH25103.1, ECO:0000313|Proteomes:UP000000933};
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=M8;
RA Pena A., Teeling H., Huerta-Cepas J., Santos F., Yarza P.,
RA Brito-Echeverria J., Lucio M., Schmitt-Kopplin P., Meseguer I.,
RA Schenowitz C., Dossat C., Barbe V., Dopazo J., Rossello-Mora R.,
RA Schuler M., Glockner F.O., Amann R., Gabaldon T., Anton J.;
RT "Fine-scale evolution: genomic, phenotypic and ecological differentiation
RT in two coexisting Salinibacter ruber strains.";
RL ISME J. 4:882-95(2010).
RN [2] {ECO:0000313|EMBL:CBH25103.1, ECO:0000313|Proteomes:UP000000933}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M8 {ECO:0000313|EMBL:CBH25103.1,
RC ECO:0000313|Proteomes:UP000000933};
RX PubMed=20164864; DOI=10.1038/ismej.2010.6;
RA Pena A., Teeling H., Huerta-Cepas J., Santos F., Yarza P.,
RA Brito-Echeverria J., Lucio M., Schmitt-Kopplin P., Meseguer I.,
RA Schenowitz C., Dossat C., Barbe V., Dopazo J., Rossello-Mora R.,
RA Schuler M., Glockner F.O., Amann R., Gabaldon T., Anton J.;
RT "Fine-scale evolution: genomic, phenotypic and ecological differentiation
RT in two coexisting Salinibacter ruber strains.";
RL ISME J. 4:882-895(2010).
RN [3] {ECO:0000313|Proteomes:UP000000933}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M8 {ECO:0000313|Proteomes:UP000000933};
RG Genoscope;
RT "Genome sequence of Salinibacter ruber M8.";
RL Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
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DR EMBL; FP565814; CBH25103.1; -; Genomic_DNA.
DR RefSeq; WP_013062363.1; NC_014032.1.
DR AlphaFoldDB; D5HAP8; -.
DR KEGG; srm:SRM_02182; -.
DR PATRIC; fig|761659.10.peg.2375; -.
DR HOGENOM; CLU_012907_2_1_10; -.
DR Proteomes; UP000000933; Chromosome.
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; PTHR42980:SF1; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT BETA, MITOCHONDRIAL; 1.
DR PANTHER; PTHR42980; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT BETA-RELATED; 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:CBH25103.1}; Pyruvate {ECO:0000313|EMBL:CBH25103.1}.
FT DOMAIN 344..517
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 317..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 665 AA; 72468 MW; 183AA51FE90C20D2 CRC64;
MSSPESSVNA GPDLDAEALC RALLEPRVIE EKMLTLIRQG RIAKWFSGYG QEAVAAGTAW
ALDDRDYILP MHRNLGVWTT RDVDRERLFC QLMGKKGGFT NGRDRTFHFG LPEKNLVGMI
SHMAAMLPVA CGLGQAVRFR EADRVACAFC GDGGTREGDF HEALNLASVW DLPVLFLVEN
NGYGLSTPTD EAVAPDDIAD AAAGYDMPGM IVDGNDVFAV IEAVREARAH ARTKGPVLLE
MKTFRVRGHE EASGTAYVPD ELIEEWKEKD PLDRFAARVR EEGLLGADRM ESIRAELESA
VDELAEWALD RPAVTSTPEA ERDAVFAPSP DPDPPSPDAD TEETRFIDAI QDGLRAAMRD
DDEVIVMGQD IAEYGGAFKV TDGFVDEFGS ERVRNTPIIE DGALGAGMGL SIEGLPAVVE
MQYADFISCG FNQTVNNLAT THYRWGQPVN VTIRAPFGGG IGAGPFHSQS REAWFTHTPG
LKVVVPATPR DAKGLLRTAV ADPNPVLFFE HKKLYRSVRG AVPTEAYTLP FGEARVAREG
TDATIVTYGV GVHWALAEAE HQAEANGVEL EVVDLRTLVP WDRDTVRQSL DKTNRLLVLH
EASRTAGFGA EVAAELGEIG FELLDAPITR VAAEDLPVPN AKPLEDEIFS ATARLRPKVE
DLLAF
//
