ID E7FVE3_ERYRH Unreviewed; 326 AA.
AC E7FVE3;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=Pyruvate dehydrogenase E1 component subunit beta {ECO:0000256|ARBA:ARBA00016138};
GN Name=pdhB {ECO:0000313|EMBL:EFY08863.1};
GN ORFNames=HMPREF0357_10970 {ECO:0000313|EMBL:EFY08863.1};
OS Erysipelothrix rhusiopathiae ATCC 19414.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Erysipelotrichaceae; Erysipelothrix.
OX NCBI_TaxID=525280 {ECO:0000313|EMBL:EFY08863.1, ECO:0000313|Proteomes:UP000003028};
RN [1] {ECO:0000313|EMBL:EFY08863.1, ECO:0000313|Proteomes:UP000003028}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19414 {ECO:0000313|EMBL:EFY08863.1,
RC ECO:0000313|Proteomes:UP000003028};
RA Muzny D., Qin X., Buhay C., Dugan-Rocha S., Ding Y., Chen G., Hawes A.,
RA Holder M., Jhangiani S., Johnson A., Khan Z., Li Z., Liu W., Liu X.,
RA Perez L., Shen H., Wang Q., Watt J., Xi L., Xin Y., Zhou J., Deng J.,
RA Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L., Villasana D., Johnson A.,
RA Liu J., Liyanage D., Lorensuhewa L., Robinson T., Song A., Song B.-B.,
RA Dinh H., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M.,
RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N.,
RA Okwuonu G., Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W.,
RA Jakkamsetti A., Pham P., Ruth R., San Lucas F., Warren J., Zhang J.,
RA Zhao Z., Zhou C., Zhu D., Lee S., Bess C., Blankenburg K., Forbes L.,
RA Fu Q., Gubbala S., Hirani K., Jayaseelan J.C., Lara F., Munidasa M.,
RA Palculict T., Patil S., Pu L.-L., Saada N., Tang L., Weissenberger G.,
RA Zhu Y., Hemphill L., Shang Y., Youmans B., Ayvaz T., Ross M.,
RA Santibanez J., Aqrawi P., Gross S., Joshi V., Fowler G., Nazareth L.,
RA Reid J., Worley K., Petrosino J., Highlander S., Gibbs R.;
RL Submitted (JAN-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:EFY08863.1}.
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DR EMBL; ACLK02000002; EFY08863.1; -; Genomic_DNA.
DR RefSeq; WP_003774734.1; NZ_ACLK02000002.1.
DR AlphaFoldDB; E7FVE3; -.
DR STRING; 1648.A2I91_01895; -.
DR GeneID; 60952185; -.
DR OrthoDB; 9771835at2; -.
DR Proteomes; UP000003028; Unassembled WGS sequence.
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; 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:EFY08863.1};
KW Pyruvate {ECO:0000313|EMBL:EFY08863.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000003028}.
FT DOMAIN 4..179
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 326 AA; 35562 MW; F0EF22EB5D4C9BA2 CRC64;
MAVKNMVEAI TDGLEVMLEN DEKVLIFGED VGKNGGVFRA TDGLQAKFGE DRVFDTPLAE
SGILGLSIGL GVEGFRPLPE IQFFGFITEA IDSITNQMAR MRYRTEGQLF APITIRSPYG
GGVATPEIHS DSYEGMIAQM PGMRVVVPSN PYDAKGLLIS SIKSNDPVLF LEHLKLYRGE
KVEVPEGIYE VPLDKANIVR EGTDISIVSY GAMVVEARKA ADILAEEGIS VEVVDLRTIA
PLDMETIGTS VSKTGRVLVV QEAQRIAGVA SHVMSEISER FFLDLVAPVS RVTAPDTTYP
LPQVEQIWLP NAQDIVTSAR KLVQEY
//
