ID M1YVX5_NITG3 Unreviewed; 346 AA.
AC M1YVX5;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Pyruvate dehydrogenase E1 component subunit beta {ECO:0000256|ARBA:ARBA00016138};
GN Name=pdhB {ECO:0000313|EMBL:CCQ89785.1};
GN ORFNames=NITGR_170042 {ECO:0000313|EMBL:CCQ89785.1};
OS Nitrospina gracilis (strain 3/211).
OC Bacteria; Nitrospinae/Tectomicrobia group; Nitrospinota; Nitrospinia;
OC Nitrospinales; Nitrospinaceae; Nitrospina.
OX NCBI_TaxID=1266370 {ECO:0000313|EMBL:CCQ89785.1, ECO:0000313|Proteomes:UP000011704};
RN [1] {ECO:0000313|EMBL:CCQ89785.1, ECO:0000313|Proteomes:UP000011704}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3/211 {ECO:0000313|EMBL:CCQ89785.1,
RC ECO:0000313|Proteomes:UP000011704};
RX PubMed=23439773; DOI=10.3389/fmicb.2013.00027;
RA Luecker S., Nowka B., Rattei T., Spieck E., and Daims H.;
RT "The genome of Nitrospina gracilis illuminates the metabolism and evolution
RT of the major marine nitrite oxidizer.";
RL Front. Microbiol. 4:27-27(2013).
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 -!- 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:CCQ89785.1}.
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DR EMBL; CAQJ01000019; CCQ89785.1; -; Genomic_DNA.
DR RefSeq; WP_005006564.1; NZ_HG422173.1.
DR AlphaFoldDB; M1YVX5; -.
DR STRING; 1266370.NITGR_170042; -.
DR HOGENOM; CLU_012907_1_0_0; -.
DR InParanoid; M1YVX5; -.
DR OrthoDB; 9780894at2; -.
DR Proteomes; UP000011704; 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:CCQ89785.1};
KW Pyruvate {ECO:0000313|EMBL:CCQ89785.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000011704}.
FT DOMAIN 24..199
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 346 AA; 37514 MW; 9E231326CE840802 CRC64;
MPWAEALIAK QTVDKAPEGE GRVLTYVDAL REALAIALDL DPKVFVLGQG VNDARGMFGV
TTGLNQDFGE HRVFDTPLSE EGLTGICTGA ALNGARPVYL HNRPDFLLLA FNQIVTHASK
FHYIDHGQSK VPWVIWAAIG RGWGSGSQHS QAIQGMLLGV PGLKIIMPST AYDAKGLMLA
AIADNNPVLI FEHRWAMKTK GIVPEGIYRV PIGRGVYRSH GEHLTVVGTS HALLLAQDAL
DDLKADGITA DVIDLRTLKP LDEDIILESV KKTGKLLVVD TGWAMGGVCA EIGCLVAEKA
FEHLKAPVKR IGLPDAPTPA GYTLEQYYYP DKERIAQAIR ELAKRA
//
