ID F0I220_STRSA Unreviewed; 330 AA.
AC F0I220;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=Pyruvate dehydrogenase E1 component subunit beta {ECO:0000256|ARBA:ARBA00016138};
DE EC=1.2.4.1 {ECO:0000256|ARBA:ARBA00012281};
GN Name=acoB2 {ECO:0000313|EMBL:EGD29479.1};
GN ORFNames=HMPREF9381_0992 {ECO:0000313|EMBL:EGD29479.1};
OS Streptococcus sanguinis SK72.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=888809 {ECO:0000313|EMBL:EGD29479.1, ECO:0000313|Proteomes:UP000003332};
RN [1] {ECO:0000313|EMBL:EGD29479.1, ECO:0000313|Proteomes:UP000003332}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK72 {ECO:0000313|EMBL:EGD29479.1,
RC ECO:0000313|Proteomes:UP000003332};
RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA Petrosino J., Highlander S., Gibbs R.;
RL Submitted (FEB-2011) 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:EGD29479.1}.
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DR EMBL; AEXV01000007; EGD29479.1; -; Genomic_DNA.
DR RefSeq; WP_002902921.1; NZ_GL872376.1.
DR AlphaFoldDB; F0I220; -.
DR PATRIC; fig|888809.3.peg.974; -.
DR HOGENOM; CLU_012907_1_1_9; -.
DR Proteomes; UP000003332; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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; PTHR43257; PYRUVATE DEHYDROGENASE E1 COMPONENT BETA SUBUNIT; 1.
DR PANTHER; PTHR43257:SF2; PYRUVATE DEHYDROGENASE E1 COMPONENT SUBUNIT BETA; 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:EGD29479.1}.
FT DOMAIN 6..181
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 330 AA; 35753 MW; 1DBC06261EEE4CF9 CRC64;
METKTMSFRD TIILAMSEEM RRDENVLLMG EDVGVFGGDF GTSVGMLEEF GPERVRDCPI
SEAAISGAAA GAAMTGLRPI VDMTFMDFSV IAMDAIVNQA AKTRYMFGGK GQVPMTVRCA
AGNGVGSAAQ HSQSLESWFT HIPGLKVVAP GTPADMKGLL KSSIRDNNPV IILEYKSEFN
QKGEVPVDPE YVIPLGVGEI KKEGTDVTVV TYGKMLRRVM QAAEELAEEG ISVEVVDPRT
LVPLDKDIII NSVKKTGKVV LVNDAHKTSG FIGEISAIIS ESEAFDYLDA PIRRCAGEDV
PMPYAQNLEN AMIPTVESIK DAIRKTYHKE
//
