ID I0JKP9_HALH3 Unreviewed; 332 AA.
AC I0JKP9;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE SubName: Full=Pyruvate dehydrogenase subunit E1-beta {ECO:0000313|EMBL:CCG44718.1};
DE EC=1.2.4.1 {ECO:0000313|EMBL:CCG44718.1};
GN Name=pdhB1 {ECO:0000313|EMBL:CCG44718.1};
GN OrderedLocusNames=HBHAL_2372 {ECO:0000313|EMBL:CCG44718.1};
OS Halobacillus halophilus (strain ATCC 35676 / DSM 2266 / JCM 20832 / KCTC
OS 3685 / LMG 17431 / NBRC 102448 / NCIMB 2269) (Sporosarcina halophila).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Halobacillus.
OX NCBI_TaxID=866895 {ECO:0000313|EMBL:CCG44718.1, ECO:0000313|Proteomes:UP000007397};
RN [1] {ECO:0000313|EMBL:CCG44718.1, ECO:0000313|Proteomes:UP000007397}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35676 / DSM 2266 / JCM 20832 / KCTC 3685 / LMG 17431 /
RC NBRC 102448 / NCIMB 2269 {ECO:0000313|Proteomes:UP000007397};
RX PubMed=22583374; DOI=10.1111/j.1462-2920.2012.02770.x;
RA Saum S.H., Pfeiffer F., Palm P., Rampp M., Schuster S.C., Muller V.,
RA Oesterhelt D.;
RT "Chloride and organic osmolytes: a hybrid strategy to cope with elevated
RT salinities by the moderately halophilic, chloride-dependent bacterium
RT Halobacillus halophilus.";
RL Environ. Microbiol. 15:1619-1633(2013).
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
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DR EMBL; HE717023; CCG44718.1; -; Genomic_DNA.
DR RefSeq; WP_014642620.1; NC_017668.1.
DR AlphaFoldDB; I0JKP9; -.
DR STRING; 866895.HBHAL_2372; -.
DR KEGG; hhd:HBHAL_2372; -.
DR PATRIC; fig|866895.3.peg.1378; -.
DR eggNOG; COG0022; Bacteria.
DR HOGENOM; CLU_012907_1_0_9; -.
DR Proteomes; UP000007397; Chromosome.
DR GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-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:CCG44718.1};
KW Pyruvate {ECO:0000313|EMBL:CCG44718.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007397}.
FT DOMAIN 10..185
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 332 AA; 36726 MW; 3D504A783F8A6CC7 CRC64;
MTTAIQVRKL TMVQAVTDAM KTMLQEDESV IVLGEDVGKN GGVFRATEGL FDQFGEERVI
DTPLAESGII GTSIGLAING FRPIAEMQFL GFIYPAFNQL MTHATRMRQR TMGRYTVPMV
IRAPYGAGVK APEIHSDSVE ALFTQIPGLK VVIPSNAYDA KGLLISSIED PDPVLFLEPM
RSYRSFRTEV PEEKYTVDLG KASYQKKGND VTLLTWGAMV PDTMKAVEQF EKQQNATCEV
IDLRTLYPLD KKTIQESVEK TGRVVIVHEA PATGGMNAEI ISVINDSAFF YLKAPVQKVT
GFDTPVPVYS LEKEYLPSSE KIIHAINQAL SY
//
